From a313faccd5d2764f22b6a526796f216aefefd95a Mon Sep 17 00:00:00 2001 From: turtle89431 Date: Tue, 5 May 2026 00:58:01 -0700 Subject: [PATCH] Scrape wikipedia-science: 1807 new, 2658 updated, 4578 total (kb-cron) --- _index.db | Bin 57020416 -> 57102336 bytes .../wiki/Bibliography_of_biology-0.md | 55 ++ .../wiki/Bibliography_of_biology-1.md | 34 + .../wiki/Bibliography_of_biology-2.md | 58 ++ .../wiki/Index_of_anatomy_articles-0.md | 2 +- ...ndex_of_evolutionary_biology_articles-0.md | 110 +++ .../Index_of_molecular_biology_articles-0.md | 2 +- .../Index_of_molecular_biology_articles-1.md | 2 +- .../Index_of_molecular_biology_articles-2.md | 2 +- ...List_of_Accipitriformes_by_population-0.md | 32 + .../List_of_Anseriformes_by_population-0.md | 39 + .../List_of_Apodiformes_by_population-0.md | 32 + .../List_of_Bucerotiformes_by_population-0.md | 29 + ...List_of_Charadriiformes_by_population-0.md | 41 + .../List_of_Ciconiiformes_by_population-0.md | 24 + .../List_of_Columbiformes_by_population-0.md | 43 + .../List_of_Coraciiformes_by_population-0.md | 28 + .../List_of_Cuculiformes_by_population-0.md | 32 + .../wiki/List_of_EC_numbers_(EC_1)-0.md | 13 + .../wiki/List_of_EC_numbers_(EC_1)-1.md | 257 ++++++ .../wiki/List_of_EC_numbers_(EC_1)-10.md | 158 ++++ .../wiki/List_of_EC_numbers_(EC_1)-11.md | 117 +++ .../wiki/List_of_EC_numbers_(EC_1)-12.md | 150 ++++ .../wiki/List_of_EC_numbers_(EC_1)-13.md | 117 +++ .../wiki/List_of_EC_numbers_(EC_1)-14.md | 190 ++++ .../wiki/List_of_EC_numbers_(EC_1)-15.md | 190 ++++ .../wiki/List_of_EC_numbers_(EC_1)-16.md | 185 ++++ .../wiki/List_of_EC_numbers_(EC_1)-17.md | 159 ++++ .../wiki/List_of_EC_numbers_(EC_1)-2.md | 144 +++ .../wiki/List_of_EC_numbers_(EC_1)-3.md | 146 +++ .../wiki/List_of_EC_numbers_(EC_1)-4.md | 183 ++++ .../wiki/List_of_EC_numbers_(EC_1)-5.md | 202 +++++ .../wiki/List_of_EC_numbers_(EC_1)-6.md | 141 +++ .../wiki/List_of_EC_numbers_(EC_1)-7.md | 177 ++++ .../wiki/List_of_EC_numbers_(EC_1)-8.md | 183 ++++ .../wiki/List_of_EC_numbers_(EC_1)-9.md | 158 ++++ .../wiki/List_of_EC_numbers_(EC_2)-0.md | 13 + .../wiki/List_of_EC_numbers_(EC_2)-1.md | 369 ++++++++ .../wiki/List_of_EC_numbers_(EC_2)-10.md | 144 +++ .../wiki/List_of_EC_numbers_(EC_2)-11.md | 244 +++++ .../wiki/List_of_EC_numbers_(EC_2)-12.md | 198 +++++ .../wiki/List_of_EC_numbers_(EC_2)-13.md | 235 +++++ .../wiki/List_of_EC_numbers_(EC_2)-2.md | 31 + .../wiki/List_of_EC_numbers_(EC_2)-3.md | 69 ++ .../wiki/List_of_EC_numbers_(EC_2)-4.md | 315 +++++++ .../wiki/List_of_EC_numbers_(EC_2)-5.md | 71 ++ .../wiki/List_of_EC_numbers_(EC_2)-6.md | 318 +++++++ .../wiki/List_of_EC_numbers_(EC_2)-7.md | 88 ++ .../wiki/List_of_EC_numbers_(EC_2)-8.md | 101 +++ .../wiki/List_of_EC_numbers_(EC_2)-9.md | 166 ++++ .../wiki/List_of_EC_numbers_(EC_3)-0.md | 167 ++++ .../wiki/List_of_EC_numbers_(EC_3)-1.md | 227 +++++ .../wiki/List_of_EC_numbers_(EC_3)-10.md | 122 +++ .../wiki/List_of_EC_numbers_(EC_3)-2.md | 77 ++ .../wiki/List_of_EC_numbers_(EC_3)-3.md | 225 +++++ .../wiki/List_of_EC_numbers_(EC_3)-4.md | 161 ++++ .../wiki/List_of_EC_numbers_(EC_3)-5.md | 113 +++ .../wiki/List_of_EC_numbers_(EC_3)-6.md | 205 +++++ .../wiki/List_of_EC_numbers_(EC_3)-7.md | 198 +++++ .../wiki/List_of_EC_numbers_(EC_3)-8.md | 245 ++++++ .../wiki/List_of_EC_numbers_(EC_3)-9.md | 171 ++++ .../wiki/List_of_EC_numbers_(EC_4)-0.md | 202 +++++ .../wiki/List_of_EC_numbers_(EC_4)-1.md | 87 ++ .../wiki/List_of_EC_numbers_(EC_4)-2.md | 188 ++++ .../wiki/List_of_EC_numbers_(EC_4)-3.md | 245 ++++++ .../wiki/List_of_EC_numbers_(EC_4)-4.md | 203 +++++ .../wiki/List_of_EC_numbers_(EC_5)-0.md | 215 +++++ .../wiki/List_of_EC_numbers_(EC_5)-1.md | 194 ++++ .../wiki/List_of_EC_numbers_(EC_6)-0.md | 161 ++++ .../wiki/List_of_EC_numbers_(EC_6)-1.md | 164 ++++ .../wiki/List_of_EC_numbers_(EC_7)-0.md | 158 ++++ .../List_of_Falconiformes_by_population-0.md | 31 + .../List_of_Galliformes_by_population-0.md | 36 + .../List_of_Gaviiformes_by_population-0.md | 24 + .../List_of_Gruiformes_by_population-0.md | 52 ++ ...List_of_Musophagiformes_by_population-0.md | 23 + .../wiki/List_of_OBO_Foundry_ontologies-0.md | 17 + .../List_of_Otidiformes_by_population-0.md | 28 + .../List_of_Passeriformes_by_population-0.md | 27 + .../List_of_Pelecaniformes_by_population-0.md | 36 + ..._of_Phoenicopteriformes_by_population-0.md | 25 + .../List_of_Piciformes_by_population-0.md | 31 + ...ist_of_Podicipediformes_by_population-0.md | 29 + ...st_of_Procellariiformes_by_population-0.md | 32 + .../List_of_Psittaciformes_by_population-0.md | 45 + .../List_of_Pterocliformes_by_population-0.md | 28 + ...List_of_Sphenisciformes_by_population-0.md | 26 + ...ist_of_Struthioniformes_by_population-0.md | 24 + .../List_of_Suliformes_by_population-0.md | 31 + .../List_of_Tinamiformes_by_population-0.md | 24 + .../List_of_Trogoniformes_by_population-0.md | 24 + .../wiki/List_of_aging_processes-0.md | 32 + .../wiki/List_of_anatomical_isthmi-0.md | 25 + .../List_of_animals_by_number_of_legs-0.md | 20 + .../List_of_animals_by_number_of_neurons-0.md | 39 + .../List_of_animals_that_produce_silk-0.md | 53 ++ ...f_bacterial_disulfide_oxidoreductases-0.md | 17 + .../wiki/List_of_biodiversity_databases-0.md | 26 + .../List_of_bioinformatics_institutions-0.md | 38 + .../wiki/List_of_biological_databases-0.md | 177 ++++ .../wiki/List_of_birds_by_population-0.md | 35 + ...s_of_the_Cape_Peninsula_and_False_Bay-0.md | 82 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-1.md | 68 ++ .../wiki/List_of_camouflage_methods-0.md | 36 + .../List_of_carnivorans_by_population-0.md | 26 + .../wiki/List_of_chordate_orders-0.md | 333 +++++++ ...List_of_clinically_important_bacteria-0.md | 261 ++++++ ...ist_of_elephant_species_by_population-0.md | 20 + ..._endemic_species_of_Clipperton_Island-0.md | 26 + .../wiki/List_of_enzymes-0.md | 209 +++++ .../wiki/List_of_enzymes-1.md | 223 +++++ .../wiki/List_of_enzymes-2.md | 244 +++++ ..._of_even-toed_ungulates_by_population-0.md | 30 + .../List_of_genetically_modified_crops-0.md | 63 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-0.md | 91 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-1.md | 40 + ...tats_of_principal_importance_in_Wales-0.md | 96 ++ .../wiki/List_of_herbaria-0.md | 50 ++ .../wiki/List_of_herbaria_in_Europe-0.md | 97 ++ .../List_of_herbaria_in_North_America-0.md | 27 + .../wiki/List_of_herbaria_in_Turkey-0.md | 33 + .../wiki/List_of_honey_bee_pheromones-0.md | 51 ++ .../wiki/List_of_honey_bee_pheromones-1.md | 48 + .../wiki/List_of_human_blood_components-0.md | 18 + .../List_of_human_protein-coding_genes_1-0.md | 12 + .../List_of_human_protein-coding_genes_2-0.md | 12 + .../List_of_human_protein-coding_genes_3-0.md | 12 + .../List_of_human_protein-coding_genes_4-0.md | 12 + .../List_of_human_protein-coding_genes_5-0.md | 12 + .../List_of_human_protein-coding_genes_6-0.md | 12 + .../List_of_human_protein-coding_genes_7-0.md | 12 + .../List_of_human_protein-coding_genes_8-0.md | 12 + .../List_of_human_protein-coding_genes_9-0.md | 12 + .../List_of_human_transcription_factors-0.md | 22 + .../wiki/List_of_immune_cells-0.md | 14 + ..._of_the_National_Institutes_of_Health-0.md | 46 + .../wiki/List_of_interstitial_cells-0.md | 27 + .../List_of_longest-living_organisms-0.md | 25 + .../List_of_longest-living_organisms-1.md | 38 + .../List_of_longest-living_organisms-2.md | 37 + .../List_of_longest-living_organisms-3.md | 40 + .../List_of_longest-living_organisms-4.md | 56 ++ .../wiki/List_of_marine_ecoregions-0.md | 484 ++++++++++ .../List_of_marsupials_by_population-0.md | 42 + ..._microorganisms_tested_in_outer_space-0.md | 2 +- .../wiki/List_of_mitosporic_Ascomycota-0.md | 16 + .../wiki/List_of_model_organisms-0.md | 85 ++ .../wiki/List_of_model_organisms-1.md | 28 + .../wiki/List_of_model_organisms-2.md | 51 ++ .../wiki/List_of_model_organisms-3.md | 40 + .../wiki/List_of_neuroscience_databases-0.md | 26 + .../wiki/List_of_obsolete_taxa-0.md | 23 + ...t_of_odd-toed_ungulates_by_population-0.md | 21 + .../wiki/List_of_parasitic_organisms-0.md | 157 ++++ ...Evolving_Genes_and_Proteins_symposium-0.md | 2 +- .../wiki/List_of_plant_orders-0.md | 553 ++++++++++++ .../List_of_prehistoric_bryozoan_genera-0.md | 833 ++++++++++++++++++ .../List_of_prehistoric_bryozoan_genera-1.md | 783 ++++++++++++++++ .../wiki/List_of_primates_by_population-0.md | 26 + .../wiki/List_of_proteins-0.md | 135 +++ ...s_of_the_Cape_Peninsula_and_False_Bay-0.md | 83 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-1.md | 77 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-2.md | 70 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-3.md | 58 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-4.md | 73 ++ ...s_of_the_Cape_Peninsula_and_False_Bay-5.md | 118 +++ .../List_of_research_methods_in_biology-0.md | 44 + .../wiki/List_of_scattering_experiments-0.md | 50 ++ ...elective_estrogen_receptor_modulators-0.md | 31 + .../List_of_sequenced_animal_genomes-0.md | 165 ++++ .../List_of_sequenced_animal_genomes-1.md | 249 ++++++ .../List_of_sequenced_animal_genomes-2.md | 260 ++++++ .../List_of_sequenced_animal_genomes-3.md | 196 +++++ .../List_of_sequenced_animal_genomes-4.md | 221 +++++ .../List_of_sequenced_animal_genomes-5.md | 147 ++++ .../List_of_sequenced_archaeal_genomes-0.md | 100 +++ .../List_of_sequenced_bacterial_genomes-0.md | 135 +++ .../List_of_sequenced_eukaryotic_genomes-0.md | 61 ++ .../wiki/List_of_sequenced_fungi_genomes-0.md | 190 ++++ .../wiki/List_of_sequenced_fungi_genomes-1.md | 135 +++ .../wiki/List_of_sequenced_plant_genomes-0.md | 102 +++ .../wiki/List_of_sequenced_plastomes-0.md | 91 ++ .../List_of_sequenced_protist_genomes-0.md | 50 ++ .../wiki/Lists_of_human_genes-0.md | 38 + .../wiki/Lists_of_mammals_by_population-0.md | 75 ++ .../Lists_of_organisms_by_population-0.md | 95 ++ .../wiki/Lists_of_sequenced_genomes-0.md | 2 +- .../wiki/Outline_of_ants-0.md | 85 ++ .../wiki/Outline_of_biochemistry-0.md | 2 +- .../wiki/Outline_of_biology-0.md | 131 +++ .../wiki/Outline_of_biology-1.md | 158 ++++ .../wiki/Outline_of_biology-2.md | 34 + .../wiki/Outline_of_biology-3.md | 60 ++ .../wiki/Outline_of_cell_biology-0.md | 63 ++ .../wiki/Outline_of_cell_biology-1.md | 42 + .../wiki/Outline_of_cell_biology-2.md | 43 + .../wiki/Outline_of_cell_biology-3.md | 53 ++ .../wiki/Outline_of_cell_biology-4.md | 53 ++ .../wiki/Outline_of_cell_biology-5.md | 49 ++ .../wiki/Outline_of_neuroscience-0.md | 219 +++++ .../wiki/Taxonomy_of_Drosera-0.md | 108 +++ 201 files changed, 20480 insertions(+), 8 deletions(-) create mode 100644 data/en.wikipedia.org/wiki/Bibliography_of_biology-0.md create mode 100644 data/en.wikipedia.org/wiki/Bibliography_of_biology-1.md create mode 100644 data/en.wikipedia.org/wiki/Bibliography_of_biology-2.md create mode 100644 data/en.wikipedia.org/wiki/Index_of_evolutionary_biology_articles-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Accipitriformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Anseriformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Apodiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Bucerotiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Charadriiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Ciconiiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Columbiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Coraciiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Cuculiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-10.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-11.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-12.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-13.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-14.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-15.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-16.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-17.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-4.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-5.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-6.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-7.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-8.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-9.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-10.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-11.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-12.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-13.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-4.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-5.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-6.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-7.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-8.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-9.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-10.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-4.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-5.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-6.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-7.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-8.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-9.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-4.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_7)-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Falconiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Galliformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Gaviiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Gruiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Musophagiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_OBO_Foundry_ontologies-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Otidiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Passeriformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Pelecaniformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Phoenicopteriformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Piciformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Podicipediformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Procellariiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Psittaciformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Pterocliformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Sphenisciformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Struthioniformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Suliformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Tinamiformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_Trogoniformes_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_aging_processes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_anatomical_isthmi-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_animals_by_number_of_legs-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_animals_by_number_of_neurons-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_animals_that_produce_silk-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_bacterial_disulfide_oxidoreductases-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_biodiversity_databases-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_bioinformatics_institutions-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_biological_databases-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_birds_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_camouflage_methods-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_carnivorans_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_chordate_orders-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_clinically_important_bacteria-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_elephant_species_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_endemic_species_of_Clipperton_Island-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_enzymes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_enzymes-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_enzymes-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_even-toed_ungulates_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_genetically_modified_crops-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_habitats_of_principal_importance_in_Wales-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_herbaria-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_herbaria_in_Europe-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_herbaria_in_North_America-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_herbaria_in_Turkey-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_blood_components-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_1-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_2-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_3-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_4-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_5-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_6-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_7-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_8-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_9-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_human_transcription_factors-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_immune_cells-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_institutes_and_centers_of_the_National_Institutes_of_Health-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_interstitial_cells-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_longest-living_organisms-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_longest-living_organisms-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_longest-living_organisms-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_longest-living_organisms-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_longest-living_organisms-4.md create mode 100644 data/en.wikipedia.org/wiki/List_of_marine_ecoregions-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_marsupials_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_mitosporic_Ascomycota-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_model_organisms-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_model_organisms-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_model_organisms-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_model_organisms-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_neuroscience_databases-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_obsolete_taxa-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_odd-toed_ungulates_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_parasitic_organisms-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_plant_orders-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_primates_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_proteins-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-4.md create mode 100644 data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-5.md create mode 100644 data/en.wikipedia.org/wiki/List_of_research_methods_in_biology-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_scattering_experiments-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_selective_estrogen_receptor_modulators-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-2.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-3.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-4.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-5.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_archaeal_genomes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_bacterial_genomes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_eukaryotic_genomes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-1.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_plant_genomes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_plastomes-0.md create mode 100644 data/en.wikipedia.org/wiki/List_of_sequenced_protist_genomes-0.md create mode 100644 data/en.wikipedia.org/wiki/Lists_of_human_genes-0.md create mode 100644 data/en.wikipedia.org/wiki/Lists_of_mammals_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/Lists_of_organisms_by_population-0.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_ants-0.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_biology-0.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_biology-1.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_biology-2.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_biology-3.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_cell_biology-0.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_cell_biology-1.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_cell_biology-2.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_cell_biology-3.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_cell_biology-4.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_cell_biology-5.md create mode 100644 data/en.wikipedia.org/wiki/Outline_of_neuroscience-0.md create mode 100644 data/en.wikipedia.org/wiki/Taxonomy_of_Drosera-0.md diff --git a/_index.db b/_index.db index 163a0ff4998ba42964290d9b52f9612c765cc8f3..7da5856ef64143783d2087197884055bd77a8804 100644 GIT binary patch delta 645644 zcmb@v34D~*^*=n%GW(j$WDm(?Ap}UmWG8?^2(k$zFkw{*lVnH+CNp7X0tA;~P=nUC zLQ$XEst;NPw<=a;Tv|~pTIy1){k3(eYpq*VXtmYW%KJU{nVC!w{L_BkB=^aE?mc%q z_uO;OJ@?%EY~TCCg6(^6EZ9|GepIDu8d4>Gc2_oYkKVWL)+xGYjk6JE`|y5~>-(I} z*lAp1oNt^h?QZYLl0JCnf^2EYRT|TtV@>M&U$5=e=c-gS=G(1!iuvFDz>VZo{OkdZBFdDDJrYTacYj!?Roey=bq;d zn2lN$Cva93r{|{cdH&D@F91gmma40`@8ugT+|?P4o>Zg z1iSN*)ns_XkYS>hQh%>z@ZnpOitsfb%`30GjSSTeUVDT zi6)WD|1P2B~K0~6EZeP$pq)R|~1_GKy5e+T%_0q^S{Fl+Ayb>n5 z!d~yjLcK+Gj1yfUPp@w%A209VCAireisa(u_jn0-hqB>)7Ty6*zo*xMm&fq3!IKH! z1Mv0x`uhDgyzIxz`e3NX0{@TU_nP4O0X#jyK-d8P2q#8e-N7Lp{1+nJ6B_n(_j@8f z{L>(;kHUJWMSfqnf501vghd2*02fCeDTi+^d_$%1oCQy$->GMqR`cwi$R`>*6!xw! zO5h;k*;tss4cglq=JMm0T*vR>qkA}!fv8=9V0R`6ZU?#&#YVg~ybR&R7wGX1g)MmN z!&{#>;0^gqcw3D(Z@|;-_ZjeZF5Xb%0Ui7^;qUfFH1IaS>j`*7cqejd9{)TY%Z00qR*BIAH;tGz}-7l^Cq3EUp4LjpM6yelxnt1$&+Qkw#M^d|Vt9k8D zrL`_yZG5*&_eTvkPb!(AE0#a4+s2!u?B%*#>4`#psT8f%Y3zL=&tU&>S8#n7(G;lA zk+bK;xutT{@glF657}SjtvgGn>frQn1~?;}DPB6&T)InsGrL1j+Z$VI8eR4E^-Ysq zu4yh;tTdJ-#eV)-xipx!yErcY%Iw`K%;CCsYC9}(ZHM(=pAzO)aSuq^S++ZL)_bgj z+ymT)(nGUsUllb913Yz4b#Q$(Xv8<@i-dfjwgGRrx_el1PJ1ewci$zgX|+w3cQ5@T z*B@-xebrN=VG{2BKZ zcffqed<{R}95J75=1fnSer#G`Dlz`qxZmhAPBwgOxYw}BP_O@7|B(Jd{n>g>_mpm@ zZlTVseOY^(Hlm%W)oWhU{8TfnnXf*k{-JuN_!seeVuSFiutS){|CZmz<*Teus(v7@ zSAC^As=8TtOxPhi?=9folsoV|J9@4d%SpAdI~3d!s1AEQTZn9_)scR0b&qGzTRrFv z_yXY}zo*(0=&fGw@rS+D-JaphRK0pUp@465 zFysl0;=Qw+wP1OC@{A+Hg2dGwsV%G*e4}Z=lm@!L(OW;0Zk>7L{AuYu+vE2Id_5k& zf4JH=Fc=I)Jb?(>))T?l^Ncpo<^FYpu#uPEczEFy$yk4+Z)|ZsFdW}Ein~v`xBkd9 z>F)X?k0`#&YL8sZd_vvqucbGq9+@70xB19%u5yB~bhPgM!BDR!;;qI%F#7a59FczC za^&+dl-bko0V@rCv+x7bv(t_^vnL5FM|1WJ1c%o9J$+s&W0k>P?EV$CDM{nqLp|P5 zF!GI7+$()F?Z|Ygz3#|L$7EskD7-HOGD(aCjr$(zGilS!Wi`?Zd&?$B#@otTva5vi z(%@-S6RxG*P479{UG8Voy9|Tg7ogz8NPc~Zvif^zBT>RIFBfAVJD`AU(F`!#nh=jSq2uc&TAh7*P5e19Y| z7@js|iZ>uVQLihN4#+ubd1jYWFvTsc_Bu}5Gu7slXTH?JXG_Q3x>9*Y%Nijw9+_?b z{!gP%s9IFpRO)Q;E%707tym!(7ap@7wccR$S*Ke~mbWaDrO%==|H2$KFEf{zJ~sWt zbgoHfe8PC4aiZZ}!*zzm20?$5ez9Jy`-N^uwT=G=|1f_MKa=OV!`u~^H|vD0x(e+d zg?jDH+O=AT<_675jX`~6t{5|;=Fpy$4?}#u)mXlpW(KuszAhCfeWpmgw4v_BW)Zb8;r<&kGHmy6L|r)D+C~Y)%f;lW=%Mj=j>tm&c!* zWe;&Qr4C6?NZJbd?)WOf5P#_l`*%61D(U89 z_GanLh3_B)n3ZPUKfOfy7PpOMPbZ~$QflQEmPvzO+VtbbaG#Ulo{;Wq&zUSazp_8V z@Yp&S>^(J}4@qyGk6I8G3R?qVF!588>|+V^0Zjgpyj;lU?K7oWf3sg&+&XrqKdBLEUu9lm`qcDO{L=6#>Ph13nC_?X7xFIdBkoqtjp9_Q#4slY zCH?jMK(2y|PG7(?aB5uqk&$kZ`*ghE4`8Clq}Y<2N@?&{&yJIK{jNjM##_(L*~^V$ zF}Hnod)M6HP@p#i5iSs6tlk@TSXqC00=@wV4TMZ(#FLcg_x6SD|4}HkGZgGQ9ea6M z;x5ipx>SCCwOPoLZv4VNReJoo_sZm1N6r(R^4Hs!3YPeVOL8vfBzZwjmAvc26@o>6 z^^Ws|BHkXBp13b>vb63wb1|>FdQ5#HSPFCvhJw8yzOJy(ztJ8~P~@;#KkihO#^NM| z8Oi=of*tIA)~wD9cp||8n%KG^F7^-j><5)94sYO82#34q?Er9=Cg?UH`UEmaBWM!c^X_m3BXnH`(dNYB16d&V1@F{Jk>R+=KlP z)WSWd2Kqk+B()#67b}gVK~mHKK_>_y=#<0ccjIwdY+4zE z|FnNR(vdULk$bQsk8^5;@2RG#Zcs_4!MqAyct)xl%v+>WzpLJlaerI#xCjj!ko$SiGMB=#>Zc3%~{Av z#W$3d$&b(P5cKu5j_FFSV~EpW9n;l@bxc=Bavjr!bxapzny|NPwrALp$GAe;LSro5 zIyfnot1p!wfBb6RBF&n5rCD0jmh(^P_##x|&GHUGBe~}1Xbhf+r`tnA`cFznkFG7c zQfrH@+{oj3Bai1Fe7u0B&<|COs;gA$CE}OjJ=WW-8?7alH!OGa z*9s+;fTh~}SMyEch5S78D$|#yCr!hqI^*As2aKzX;|#wwZ0CMrm}}7MpVDvDR&tB= zO~QlFv3r{e&VoqBui&uNU)ZDi1Wj&F>q8x-$alYC+hKQEUHNAxYK^IjkAo{$Q}Ti<5!~VsYwZ6{&;h6!}+CN|-`y{@^tdiuUC>x zd6~5P*XUGNE`)gLrWe!|(hIY4R+D&tyX5)8K0&_w+D>7L6l={{a%QEr*pHtX;8gpu zGXre4f12Q(pds*1ulK*?o%v^0PLutUGXre2f1CzbczQx@uuD(8tt)5!oGHJ#yHl{n z_dS%iMmu6F9I=fXu@xP(6?3kr=1EnPYQLbl-1@9WZSA$@TaM^#mJ8I+Sj^^!%p1)$ zremhKdWXpmLHz%W-!abQ%GGBXzA*gE5HZy0-`C%uU!!;EUe;|@8^q_t3q_j$_6vU% zZWDS1C;u8R^K1A*?zh@4-1VGC`-oPfIV*j}lEyiW6BJhO+>oia27A4JF#0}-A>o0r zL-Kq)zg(i2EMFuTh6V})pfwC?9_|T7JP!Hhzg7!n3?LI6C*bY!_JD=g)b@8tbHLajb&LQPkc?Pm&EdELYg;T(;78{epM$b^T&JD6C)A+}ms!jXbFu^LJ*c3-;cHkpXlS=EVkRyD1&(o@_< z8nvVn5<3`)wbYDiWigcw`V;XMRb>j4)=`wJvW`lJyCr_XEoJBM0;p-vi(gbo&)!;g z&KR9?vSMReLkrThTsjNJG-Xufki?M2{nIIehnH_Cy`G=6^OoDn;L72~!&SgdfUAU? z2uJag;i}-O;cDQfz`5XR;p*bI+*aTHVbxsKqbloR>owN3R?hN*<$B8nmOQT3{3`cb z?nmamT(7xT^{BbR^as=Rs((n8yBe-iIE(8!wb4QYEGgAHG859}OZ6sm+Nf}trJE;L zl}X#}?M5}`N{5jtD5YIrK5Nn`+b;G8l%Y#`$_K7~mDle)y1N0c5v~cY8Ez_E3*0og z>2NdP&VoA|ZYJC;xYqd5-Lvan=iZfs!M3w_)ko5-!M07({ex|FwEd;=1)78)?+f&L zw}P0YH-7WmZ0VJ)ZFWtkrc7AC%Wnn0u`y4_Nm>9s2|871l-8+19Dn8f&@r zZF$y{Ekc9*^|3j^tec)_5ys1BwNB+elP;V+uU^_UdtMPeH1T_8&)a5jRUf)y`}Xaz z9&F1U`7V6hG3VDfm=8o*lgWJ8qpLA8A1AF^Jg+WlUBUh68iE!q4XQfk2cpdX$6OsFx`JfW#K4U&?C2}7!pB}z9;frqH zjy*;0_bgBg-*e1|Ei&#&=2OG>5c8oq+&!!c*lOo)Wj^d%azA1|6wK{nJ}P*G`KaKF zn2!n$F&`D&&wNzw+BM8e1$QzZ6}*u7sNh-5M+G-AAMnUkF(2^Al`Fp)+=0qFsPGYF>C#)F+e{Cw|9tMvFHSS_Q+K8=7rWoyo1nw!V0!Jy7v`EqT z1C|yjXxzelKtbaW^ECqpjSH9;IB3jbKH#9y%6z~}AjJV-SgWFJ`|5*R1evkef{dnwaysL}r zuFzeeb80`;KB2u{yGgr1TcY_$^N{8;%`#1~`fuvP*zVk@K3kn3PWiKV52Uhc;SJ$R zVYM)k|B^q#U(fsa7G96}_FnFCZW?D&y{bBZ?!=Gu#&xUDmtsF&T_a7GRc2?`q}A0z?d)#mi66ejb_F+P*KJ^|3MV-u@a~5t?l#+`_?BC3 zc0QWEt2aP$AGY)oa^L7YQ{P#8MsRhVt}}wG?VOT;YiC>6r!CmkSyL@skeYc1QsQT| zCnbK4R@2p4Ej@SR>RRd1eYWX*XO;Ay8&@|=Q})~LlYF<^mPl{zw^fQXVamt9{2N~- zy?48OSDLJ9F>ris#<9?ymvI+5BxPah&iM;YUKh&@34E*ZJEd zozvrwU*`0bV2Pny2tCh%e{&Ar_Jp+i@7mJ1?Y^#U;2~um_0DLy2d+CFE$`Ve84N-- zhkr^1Q;{;^OW`-dWx@(!JpV8LDeH^YyR0MDHp>T=hb&iGx-2c&_k6*8gZU!!0`oZ2 z-%PS;qp8VcHy$(IWL#scGn_CSHr!+wFibVr_3!BK)<^Zr^y773=$_Txq}!yM1FhtT z+K03w+D>h$<~_zOIy5Cw^#|(5)Hka8!7lXTOX8*6Zq<*tE-qK~=LKTSo}xbJrT$0j zhlb8hl}eD4f+_5-yq-``f3>2q6KOMB;uemx^X?mD)8fnc^P~^IxW6zurRo2t^6NX@ z|3gmEQyFs9buRlKvN}~xwVg}9J*Va~wk~mXcC?GJ;zUnLcU-sn2j9-XyQS~kw0dM* z`uc@72uAlglKh2tKPlPd)sx18j@ju*f*RaUIE6M=2kF3q{2Wc^JhH8j*4-H&UpnRd zW?@r`lGvIgeH$d1N1prfbn^x1_F(NWYEBgGoS1GA0Rz5%tbs@)P~9CG4sHv20@cha zEX^>bwsY=(oyOI9&e&?e%!l@W>C)rBgeMnlkXSHj5xp3|%FqC(gk4`pe>6{~N+q1fH%rr2V+W1N4 zsBu45A++=I_NJvmNx6G>i!d~r@i%vXlF4}YFXH#^S>4Qy?cOn)KuOpl_s_@RF?|;( z38QsCx=f6X=cTUY-(AFawn;75uAW?#ZWA*IV;oQqI_wlPy{mJ!wDP9a^-}M(tEEFL10W_*E>fV-0ST&bML6kDSI2qGY;m0Uk_|EN-N7eP@>Z7 zx__N88Zs-zYg9S{R07A9dCby_tA7IPf?K>=xqU$mHm%RS#k+vVtS1`x9G_hz9lO<= z8UNL--aiOZ#*1M<{%np}axJ*n$eX*Bo&CKf9*ul#bq}wJA9Z?8z)BJ}4)SB43Y^wV z8lpK+H+e%I`|E59lz)K;9dC|F$LcMmJHLOI7j8XVA6!424{ih8MmRs*09*hr2sa3~ z2`&T|hKs-r!EJ`y694{PTMZ`^qow-hnx?6)dRIfjXesZ?6;jC+*^?#t#8vj4pWHbN zw+-$>xQpN}hPwnV3b!3D2Dbz5Qn<_DE{7X|+X;6C+?8wVV!)*G#R;zb9px{i}OZCnYiyr|9I@GYeefmRQmY$4_&o+myXky ztMujSxw~5ncUE?M7w&s---o*zZWr8cxF5jnfx8CoTDa@rB)A{KT@UvoxF5sa0CywY zO>i>YUbvg#Zh`v=+^ul8!R>?F4|hA<9dLKT-350y+)v@|fx8#(0Nj0WKZCm;?g6+5 z;SR#Z;U0o}8150cN8x@B_Y1hk;*}kTUj8&{xmRUUx2n{w)_1K>Tkp005bK^E>jGm9@lif9MN8CT`yyT)gh>bWois7V!q7=ad%vc=o7Dl>2B4S55> zUMN-r2u1eOcugowHU@Y_wmVc<JmUInF>C7MLEpqMfTl!u6#iYQ`%l=m=%cFI9?C)(+Eq4Amraw+au_MTZdB_p$hYOF&JQtpgKoa zYFPPH8Q#qCUaHw55$6{8WUuH<)Gaza^@~oAKk5%XP|h0zJ;ObIY&iD%JV>VDc!4vl z_l6++CYlU<=NZa$)`t1K-tXC*LIojcxx>zJ(SD`!o9FX}F-<0<>*jON=qXLv!I?Sr z#sGHXl?1WzoJg_*-e9Z92b2nMs|1cP1VYi8GY!VfteCz*u zhjT<6NT7?YDl_vUYy~KQ5M9oj$Lv=l7$vU+{ZZurF}Z*@^kdHk+nNyLl&~E+Iw3Sf z^kLw3b76CIoB?FpcA-6i%deQe!OS~ z%gD+!+AJ2c!)&*i4e{1%4+r#^kX7Sk@!sqBujG5J(}fi~)g6z+JpuP5+%MstimN*g zpO{(0t7Vn-9kqOG0zwBa4eAWEXob8U{#ve1ZhLc; zaQ0cmd$JLJkpRwfOFnlQ0i7lAjdihoUh4eJ1t^u50;7Q8ner%L^osKF!o{|tLM8@bPF4hosgM*bJT_J()XJI! zQgX#pjb5v2c>hU}JUyr!t8>P~6v9l>pHff@2dYr#X&a=u)YoPfyig=@lx>Fp5=oyq2 zPd$E3a14&U(JakC*+VOGv4yE3SaK~A5D;Z!6fu=2id4c3qFSwGP6s$GGS-SwQKv!8 zs759hrDQ?nqgn)I#4op*$}y<*YOM}`CbLXEd3OX^0ST$}8DGs+&=aQuaoau0eGa3@PoU8W2WA4J9CKP$TfCAd!R-@+(mo zK~zB#L={1cQ~;%?8c)2^pV=QG3mdBvZfrB9%&i12J`1bL{q2 z7>ku*fv>HDA0skbjDp87Z?^~@!vH!Li4bp?*FQsqe8b{{A|x9Y7%LOOX>MNywql6k zyj=_Yn49LibPlJ$)7-HNVu!VKg|1So(}PNC5rUa)x-K6l(x_ylEEqQ=QqfVWQt3RU zMAT?8XYvem`-dSCVJ^k&L-8>uZ^qFwEY1_=hzJI(sL_Ocejg?>1u8>O_w)xhV`^cE zbb_XD$Ojb%-ce$vpwVf^q|XpUUlcaKi09S3HXIqo&hAzvb%&NW(=-doM=``iFp3DdUg3q(*plXTi&{<=j5ywuGze9qYc*T~ zUv*kR8-ZLIN%h9rf@!GNr`Xz#hE@ui&8S+qU&+87<*kr3L!^ovMG8u5<4t6hpR}%3 zpxb$kuczPdOCa+?ttP#1Ht}lz(4aSg$f#y)XJ5jrgCLe9MPcmugW+%x{jcP`Mi2*J z>!rL@^QK`azS8=MaBkC@AZex(A%)K1#9mJiLVq&9 zLl6%p0~L`E0$YOM&*DYAC0f(KYl1@|SnMnLTd)SfQCRj$c*zvBpod-`L{$YFT26;9 z^}{U>GUUPC+y1fnlFFs#GN}D5^0mdlJNui>Bdx zTOiT2rJQafNFQT8SrI!ZF&tJZhI*TMEojBN!LvolejdbH&qhKtB8LTa1cu~^YE+e=ypO9;6^DuvpOfJp+ToN)Mrk zsaSe$OO2UwLA@0yN|5F~pK9kpydunJ>D2Qx1Wxl|!-ykQWAG2lM^NvZ&U3i$xJLICTgtKFM5icnwUgN0H#-g2_tgpFkl&l2jfGeSp&mG0gN&$n z1Fuo+&uIPy*Wpq5O+&PDqRR3jh}#1ekmxI|puzb!jQd3DLQn}i&)Ay)DA5WaaHW## zz(z5U5}?p$20;3uB5$_hV_D^OpSrEWL6ZuUQ zG()`!3a5t5;&c&+3!Y6wiKd=U48#i#l59IKXa@#-fsHIb6bTU>vkkHXzguP0YNKc? z4yUIY*9>)t2Zn}9Yle7Ta1hC%A4t>y+&ARiOh<7M03O?@g&^)5gtnr8IGn_9Bd6Um zguYL)ixN(|%?oiRkYLg?1pysRWnlbo)re_L$`vg}gAsowi`{H88nUx()(o35Bimxj zGCNH6ESuS4$;mc45M<5GvRW-RtIeF9Z86)-j*Lv3)ojYJTQba68(uQ3j_gdc&0@_2 zj3v`xG1;-Ewb(N(R-+l`9;_KPc3r03mYZqGv1MeKGVN9Xnlr5UmtjKA8AzRxff6j4 znf45u=_V|I$6dF*bYgts-ot;K85K8T+w?A#Xcrz8dITf?Dt{Nwk>75;$l75ow|oIb z<4-I>%R4@n^*fgC1+58pbqsEJk4Tg^l`*EzSO#hbtPJOq2 zI?OBnpt~36$k*x`v1oh;7OT6p{WwdWqxn?xj7HXM(X?wOs82-Ie^B469#LPQZcrP= zcf?1o{eEr4iHmHSl(Rqu28xYr=eyZL%7L|^6Z;Ue7ZbQ=Y4Pr_C(j4k`>`q4dw zX7^{DO=VCvl1`Ii-q<8l-Jf%_{~t-lrf6~h1G};lrQ`1(-YiXc=Www|r;+8OE!XoC zG*h&+dB2S59-O}Rz{Tabcb^qTf z;i8O^(=u#!|L&B4C&M+lUpgbWM)z;O4KA9xaiPKe;B3;#RWZ@z1jsnib z7o?ka_oN;4PwpG@?gtLl-c`VL^J8zaNIxo`gw?q3CmhLtIw5dnhaUN90oTNh96LO6 z?CFtX&m27VD;(3(U99RQ>8Jf|EhkDdxra3eKSnr=c&yw;(M8YnERgis(1&Ca&NG1 zuohYVW%)fWPr1ahz>;l##~e3bVQw=QnEq~h*7TDG(}gCtsnGbL@gd_jy~^muRS91h zo-uqETg&NoPg6xkmDcR(0ZtR3AT<$MM=|Xz>FNeoVAHIM1;{R5t>mFl} zJ64QI6HXyFp1xLTaF9sP2oAz-0xrr7a!*@ull$*ylwqU$Z)XJ8;66SUZjAJl){=Vn zv9W;Z(o-5-o%_?%&y{I#m;wKJstlvJ%?Pbehjf2(D!^~Rx!fP09xhD|Y;nK;EpX9M znxE=^?^^&z;hNolfxMrUg2VbnGX42*%^1VH zzSQkD$+?4fKO{~2^Wi~}rljlcGc`!{pB$E@U%h>JsYoZNrQGWdPAzo*V08GdukIVY z1SgqIp*ubnB6WjM5`uRhl;n2~H%qop4Ki9%{&M)=(r^B9c#2ThSTHi{$i7*>J{C2o9#Pe)whQK;aIYC}F!vhQLTq@_aDhRi ze^!5)YP){Axk~p>-9g=;u0;E~>CfiZw0lhlv_0B9&4W0mq*C9GOV?f#hfOxIUU&s} zK;CE?5SsaS_}jUK{Ca*OZe`qS{gHL9RcCq9QVdEO`y)NjfvXv|8w>UFE_;VyHrap5 z?NJ#Nb2oM!h4h>6>-CPr(SJJkowys%e!p_Q>+y4oZPLBbYOPx52-`>4$ytd7Ud$C{ zn~ZO(=*}m)3}%XS^IUtmwEd;etn&9}U&rfs)f>{T2lFPECXEYEd&XO>oYA~4U^mIu z{0c!I@8t_G(TiwN4ZEgDgxR52;^YS9nwC23$^3U0Fcc_fI8kv!wukm;p#JUhZiRZw z$1Y`b`{eZO7E zYlYUFZb6LgFM@8(FOr6H?`m$O4sQciJcj3ynyyvDL;byfAp-1z81CQViS6^@Wu>T< zyPH-C%c4a98_v!|SPNMSEbhl+w#Z{wY~Nza!6*tt*r>Z@oMHpvszUsdOo}mRwZ3ia zLa^ArODJF#)a}@XfceZCyzbDDRl^Q789~G*H;H^G7~5||YWukaY!<|~9^DzqitQ^$ zSR>CveXEq{5Y_UU?{x@;a^45+LPc~IfmfU9sp6rV_H^T_0hqDCzJi%$)We9RH@0sn zvYAWUf)Ubn@0&~Tb!5wROO67UBdY0km!8-@vSA5m6A0Y59&dGM<$#wk7+b_$N){e` zA+=QBOL{`LR>b9wiG;;!4UPcg3~+3}i^?bxbOR_6S0KX1rxPJN)(Tu8wvYA~mkB&s z{$vwelPKUay4XJIuZ@BhT1uGAz_e*1-WOp*$j`2GjqRU|cQ4g2hvT-y_AZTbmtTUn zF0%D#q%K;k#$(cAJjU^A4_yL?n&2%@`)@4QQph42bluV<>>t1pF|jg2B-O0g)mj5oXom7S;XT zL)eAbS3p25B0q?BjR#N^)CeRNz&i;#WNgyxBl?PEi8`z&U}a7ePF+zOD}h2cxWyma zUqt{~jes4l*nX5Hd}0`&e$ zk<-s%A$yR+_Vb1er!AYz?mq}CUSnl+A4Wr%PL`NbQ03p ziI`T{@hHl|W3r6^d9{eE4^Rbys1$gzlw@X9nM9#JMqc^sIi5YIinO^}m1(BvL6~ZA zu{QF~709R#420({oys*+_*qo3GKU6F`9{>DjVq9|K57>xMjc2{OyqJ-2_Dl3E_N=x zm(XK^;zQrfj)|#I7L|Aa-qwH07|MgHlMelj*Ak3mWU;mRR9O%!aLI3?zT+FzI`mY3 z5VsA-_7lp&yg(**`*PvGh!W3f#iM}eWYEI6vb|Bxo`y-Fx&jd!D5x@)MUzKmGalK5 zix~Et@SH^%1{ea%<$k1T<&5$W&@(1@`u<7iyNTmW2?%3Mj0c6zL!un74Y z844Zr-boLJ9LCyK((53>Y$D$hY#e~;i;CIhzAgkUq}i)pt;S9@_$|m%eh{^JlT*w0 zqBgkjSpEuAM_!cJ(=4jhG(yq2RH=(8%PHimpb`pM=5went%a;cq5ur!%%4PX3+b_d zf?GNXx`RhtM{WiscT&I%21NifYS=qHdg+k?vChVgFNk4FjpNo7Qj)XfYp1Ug%Az&! zS6AXOjo2ABxxhrrC@0*{O;(>tUs1}(A`%Z&!PJ_2$|z)HT5-x4mL)|m3L>@Eq{tEKXC`FRZ@_ST7l>9j~-c779t1@DjXz$f{pu&iC2 zMvRWLab%)AoG@3I3 zW+~3K=NoLx9GMnNuE}gNXBkZnV}Z?TG?}c142v;4%euxqeaECcQ$|@dwjk4b={d0_ zmI>y*j9JF~@iv@8SMkD5&ET_e&%r$p_X6B+;Euw*2=`mKm*9Q}_kVD|hx-HEAK_kx zdj;-QxYywR1ot}J8*p#Jy#@C++&gj2;Ge(#)F7x9s`LZey{d&$hSNCX(4AK-5>{vr zd1~M0pXYWC_}+#4OMJlho>XCI#AzU0a`-R)d0d?To>vO*dT%q&{e|5)cW68Auz!-1 zHr3louX}p6C|~?q3$K-)xG)b_k>WBs3765$NQm+4Uohb4TDy?3^WHu0!MzXn0o;dh zAHn?K3W2&sx7@U21h$UbWn2*@!E;zcN2= zzS7)b&M^JPbiK)Isx*FVe84ztoQ0F9M+{dRIt_XH-{~d&I(>!iQ{4l)ZMsE2&B)_) zQY{X|((xj-^k(mPHP1bxT&+h3j-+4R>TRWSL>1Bnk*}?MW`Ppd(U7Z-yKeJdgj+S~ z8omSV3&8TOo*|g|%&@e3ZD4{lt}`z;{?R_~ZjN0nD0dwBA>^4)GhXC#`OFPc>ucc( z`3Ct)K1X`^c5jGXp3Xp|UDpihAIQ8Rd)txHUoz%N~qc<&K z2G`R?)i0bXt>r01^~)E(2h_4h-=^W09Ko4#f5?qYTd05WmQR*SUgYiy8M_^H9(@6wu zqA4van*@YX*r5u2B#cj`Ocsd(M4;Hd%>WqELT=g@KycVX;_OMJxLqoh*6BAi_ z4P}yepb$;ewTXk}s3x{#S|vUQ!D%urmHFNRn}e}_wsO%&?IZCyN+z}NBhmOol5+Ihwbd*es360anmJBl{m&2ruf^#S@T^w`Gk>1LdJ5n5FCOmG!Ahw-6Di!&4zbb2UQ7%q6lcB$2wLA z9X(gBp=Wb9VY->X{LGYo5`kUFl8vY5>^e4EMax7DtlGjLA|?}`1Ea_8Zd!b5%@IYm+G8vD zRRSMO3>&{y;B#Q@w2v+MtIAP9tkE{2w5KET&A?7Br;~sF{SM5uL{&MB$ZUF^vW(al zq2|$mSyVye1y)KRYA1X}wESTUcC5uPLiZ6_meL}qi!D7wn)J&i;895^nnq}M8SnJBK0~>nzASkD>f@u`WiH8Jp$15vJULEqm z!joxIT2YG}ta-mglF|~!b*8elZEhQ4ob_l}3j|_thjn3o$r9!7bDo#{^F3 zBaUF3ZnBH|A%75)0fXIu3PrR$m9_-Qdy9TLT|G^pzGib}nK2z_H7jjt7y$I?bT8suw{WOkGT7KRajsScKc zA*}spATsY&pSB87I=2JX+c@irTRP3N#R= z8*w|fsV!{lJqY~?>3|VlNqL*(e z=w*dqEiN$vlq=M#%|?wnwl3RTI^Jl}SS)tIic=&S%x631sHf93vBQqfEpb`)ZC0DD zNSNNXnAL;lex{T%WxWpCMny*w%Or~0k-=scH~De30G^lDkdzSHR7i;4(Zgf%j@4Hf z9rjEJLRgw|CUfybYm;TIrlinNZeacy%Wm{m)=rL(dW0(^gM0J zTEPb1T@|Q|;Sxy7yqM?iS5%rY6G6* z6j~{ge}b@RAd@)O12~;-<)MLX=Dt|Y1d7TqW*W>H27|_s zo#DtZTy^3EcQqV$=)?)0Q|~nh+@Q+*f%Xn=Fb>hUo2&mWa8Z%DF_u-ld{1+8EW^Cm zT(D86Pi`fi>Iy=6*V1i#4Z9CH|Ma)dOWcONxltwF**)x3?qhTY*ED_l1yEXfrfT&hRh{eg|rt zEKeUU`DFPx!(xAMOITWZ{eyY+fW|o!Ft<}C3gfn>KyM-yC87c-VZP+O_9?4eH@`^8 z;D@@kw*Xk(UA4&l;6%0RjEQ?j1>v+Nu+8o7~N-~rb#aE-?OEj{0lSB3wr^!9(g418wNsqon*0&Z8|7cot2l=x@v1j zYecUNKxDu(h|9qzvMylB{obt!{5t*6TZEmmN3;o9@-fpPUKFYQQmu7#)rl_)(=qH%|zk)GN+#P)UkJ*e!A5YK_IggAv>TXqL-?NpW z1gEO#=2$14uws=+*4*Qd;GjJ497=Xf*g4=Cc6NJ##-5EJ$w&|c92!8il3&4d%Fkb8 z5p*-CcN8i>AJAvxym-SMI-q9Ob5t3R--$c5`iL$V!J~7%J&|yYyc9H%Q%K!~Y(Tal zFKs5F3D|MM5f2cXeEgAOp@2?q0Es@J+}TT=iajsPcGPo;{MQc!dgvm3YG@UsCuZdz z@efxKRJRwH@deSov(9p^?8lWXC-(xvTY<>L2XLshNjy3$y+vE;+5%^r2j_*@fgD^Z zgSw#JZ79l+Z)9wu{`71jOhyRR_&ArVvD1am9W_pK;pUK*<_7u2;`4-@wWnf0 zr?}DeyVJ3&km-$Ci`)0~G{=m@#=PHTV<%tnDwSN7KP5L&25#UV`=Jf_#oxcph028;;PQ2xC0TC*H^~8$e3Cs~F<&`2}`5J>nc33JpS94JX(D zB_Jji8O9kQbPBP?}|7v=y6AXh-6=1xW>866CNCP_FyDz^kNvLH!4NdSVn>xo%3-(#XF4K&{@xR zLoD)p>5Y|up^%0TN{X?71709pg+*<_C{q{#D0NFeMjjFMFi>WI2EqP` z;f1m311jwa(uhD_$UEZgiGqLNqT#R?XHLS--XYp`SJH#ZYMd**7~LTy1ME2{=s;p{ z&j7{~@hnQ09LtpN08VBRYr}=lz)_-|Z60hfh1dIsPi|S1x|+)AruxyQl#?+O3U<+vBH^HXA~R%l1*Qe{5J4Vs`kX9xP-<4hbT#IT{3qOL>$XdKoFy-}Kuynggf(1{z| zHUiTNFx{d0P{mLnqdDBT$5Pce-Gk5#0J%yqdr|VE#w8g-l24?tvIVqE)Q=W{*0z8m zs}h4`6&(jngnRqYtAu`<7{Z?Q#Efv7I3c3ocpo$o_{e4l*1qJ&_d0+&FSvsz;-UJE zwhXnC-+K5c-^93hZGwxR%qBN}lZ7|dG&DEWPL*H0w_V7dnB?J<@N^e!UzQo$Uw$Yc zEfW5ZGtn&2P*dM9wXvyLdU4~^+44?A6x?JJIL+0X0|JMKNDnnVH1yEYLq`uiJq+9- z%>g6#^}UdIpH%7BY2M(T#Lcr0a5dk_jqNY9Esqw@yn0jfg)~nrPoF1}7kek}^_GtB zyQ?Mxr~Jl#J4tT+H72LUsbKUpeNt%w&9nrH`L&b<4TVcFe}nHchUOtk!$9yUvoemI z;VYH_^c4hwu(WQz#<6m=s6?LAoUO1b_Vp;QL+Ei56KGOT@B)t#O$Vqka5o35DgPnx zs@`N0K+4vuPVhz1Do_MW71-po-iL2#(zJtftV5}R0&$$UDe@Q^z+9wMkVX(hH!OCE zI&r8MGTCMin-C~!v_Q-`kW&^AGN`5$iAyFy*}Y6?kFtQFFtG(3Cv--JAWV&c#y5ZP zVH^w@y4Ph)`H-;!8&gGw>C_-qF@Xe_I}V~PIM|NU!w61git&_?Hv!4YCl2Mugg5{m z6JYJ`rf)<}a0WN~=$kL$WMZd3*bS!YVgHki1alIq4@Q?Lfhy30vBy3;;_Ms7tvcyZ z>pc(_fC-pe!ZL^JlaAkhw_`p&a0&4r%Lfv2iGzoN;6kY!+4Z~Iydf%ES(w1iNTCv} zen=ps4=bRPr0q8@&x#KCdKF2KL@$!=AtBP;2>?lE2}FYz4uLU4L`0jEnHWrABl;gT zfMFsIFs8aBQ7?i=bI!$_=Icum6C)ui2@QvdX)qu_B9#w}UjimPh^0cJL;TS5V3r#W z1xM+Sl9DpUiHjUq`UL4ErfT9~VVG50HIaJDi?rPJHc(GWPPFH(%94MZBor!X*Jn3sH%H*%S?q}4gcizO?# zKU-8l=)wH&MTFFL(bIX+bG8C=_@XyWT96z=v_ioBU?`qeo^v61RMS_nG18p9IH}y{ zb4}F+vzu7-DL=pPy@J^O65G5@#kJS9G!IaR&4UJhC_*!(l<}RXv!t%i zzf;IQIUwJ%$09hS=Nmo7@d?XTw%EnFC#)yUCOS?>k?u5P(UpE0Z z6G9Df^2FK{>r|=rakhl{H`sI?}yus({ zSyOxvhUM0K-sTlfr(tEq!H(L^gfw_RG_OJp=sph?*A&49v ztZyK2lekZok6DB_0k-FaEOLQNb8ba)nw6X$68XmPJfl0xc^amY*oS zCC$tAx*5JmOMq2;;!3Y{j59k||2`DSglU|-wg$AzrE^~jed zXvk(b60Ur%q6#bY&A8cOkW>{4az|I+?xAj)i(rWvM%Uu&>b+jf`Z!8Nw>|Wxs7qS1 zaD29OdC&E>>o#&~Y5UXy-8!%~1qySFhswhRxoq?#6mJTBDS0v+CA18HhJ@Wu5;hbA z;PRM~y%0heo`UEZ5?DZ+QtL(Av&*Qb&^2I6XbuxRHei*ByJ#?;2fBgK)*fkA!Ky5# z_kaB)3rE)L%^TfkKiC@Z{nE7r$e5 z0!a!O4%3|pX#pTjEcYTnbCn$Z;ZZ)zma0aL^Bl~$1FXX`lG+w0zA5Xa4>L-w1*;sH zSlQC@s0J%DR3sHHEwe70rtpFXx-3GL5dx~Krn$bhxusURc~W(*e4E}XWJ+IKWsM{{ zh4Mp{gC_2^d(RP6`6^?h=)=FXpDPx|_Sa_mV)(fARRhg2D{&v+=ycJO{sG&>F@ak4 zX2v+WdW+L7&TTf*`T7xV*088M6u2wq!XhsefmS_Fz7A`-U;Bc5} zQmL_mL1wtz1`0APRK3tqg~9As;wy0M>c(Q)m81njiA%=l%Gzx~ zdz*7*Fy!xb&W3y!buOZ&S7Ig3Xt=hqrgkDItS8tPfKU~7*11y4+LQ4E3S}C)Io=*f zjS#>fCNx$#7c6gEGKKPH)7}F5AQR*X&?WH4Gz4@zGya$!uQjcnEHhG2k`PM7jshVU z;XmC_LbZpV^^~F?heU~@q!-VEu$SyAd?=U5bR|;(P_%O_^MR&>>6;W?DI3wqo;JS- zMU3-#AcR76h+x73JD^oNRi9L)lsD7kVq?nN%hZEz<%@Y))VJTD5viozm?Q6+zEn_8 zVZ!uS@?)rHtxVlFodS@){^9o)Fxt*ar{C0x1^K>Tb_x!C$vgi9yVa3;3QxGjCxS0Nsf+EQvZ z=v0W8RyiR}_^FRET0BD#`Mc=~vc5AN*-qOjM|KqCm(;W;tDLyOOCkS$Pf~-O)E{pe zf}RiaBaL)ulTrhYc0(X~r45lZCP54*F)KnM!Llc@CW_Lc2w(UFZ=&{WQAYjAHDN4< zRu$k_AnHCWdBIzh{TIUDSVoBKgMQ#F4Xp{G0s8KmzM3j1^HAV$b!)#r4|mRhqa-?D zcp@qMwqTMERY~{FyFE|ZRd}w^3NDe(7o^AL-JTtFR)RN8WZiLU_K{qmDcdE=@J|&~ z1x3^rh{uq`i7R4*M4=MG3zj;xHdVA;qnm5c?a%^&J{srj^Dcl^67+)AjDHvm3fwJS zXAMlz2VB|kXUZ$mNUf>b!bp<{6Y9PVBnl?hkw8>{ZWqEW zU!+T8z#R(k80uRG500#aTHhj)5qMpCCj%xmW?f8jjWl`X)supjct6%mW?rn zn6WgL6zf6vPpm>n~Q7?*v+{K z`F~$kcTdk~Ml#v#Z7YN(clVfWG>Y7?PNjc1QtTbbM}wSmAwY(ga= zDL_%v86Q0yhdT#Qhd^AI7zvPXcPP@>8e$+~3?ErEM2vAT{?-OeDsW1O-e8-O1JIcvkM|dHDH=NaYyqoQ(8;OGL7S4E&3kG&GQ; zlOhR^M+qQ2EdJscHLE9tXfqvem$M>M{F+JnYHkdT)=LqC(op6nS)f(f|05DnC-qc< zCX!fHD63)aq0bx=U1l2uKTRCPI^H$58X6C*7O>ofCbf46o4iD*dJhjpz?2~g58?Pd z4B;5u+I)k=3grR2CejSmAvyW@2n5|VYZl@xK?E~qp1;0i##vRFF>$g)vj9Z1SY1;? zLo8~XezBmk^k7DAYf|4g9Ppg+)E6qRrC@#bf-6v`y#R&$SGDEu*fM#tu5{m|wz&PC zw&o;dwtZ=tO^B1$92X(J10ESN+`0G3A#|q2GSd`-gCvAdX0}C-T%Cr^I`k~v7*RZh z{tN4ZDVgV)=TOCRt}FS4hc^b%!!amh8xk=U8h|DJ**C$uL`W5V8^d1tAf| zp`m8Y63}*7gDx6?ji{suQ@(_u48tHmFimvDd9VpRW(XTo^R$=DFx?WilMPJ0^tZY) z-{|<(PG1rllzx!RA#s9&DG6*|9%@2H!|4-IkhRhJ4;u@%2)nL0J^|ERNq0EU!a)uJka%8?dn5-6nK&!sv70#f7u-h9 zE7?EjR->TimlsKnS0Fi_Q7QS{h&}!&6qDm~a-m4d1a1E~(NW=AGUg1~F3t z1xEyyKv7%zL6-RBcrughp_G$SA=qMCC70f;2%ZW13sd7PSqpW`Lfb*ZMpz~ajbRe<6o7e&c*8k_DhlNp z{v~T=&fJ2nqjP4~SjgF#Q>sm7v>@I4qoIbD46UN$gE$ff4*>JD_qwL2#~mQJpHwvB zx#JynzAZwo14~U{iw;n&yJKNJljxfwMDj2s9*W?2%&F4LDL3-4 zjc0Er6P;E;vnKV;Wmm%>^uMA1BaBIfqop}y%=)^P*4D-*I-(=s%WI`{j%+6ASf*-umTukO+o%);4Y zYh8U~q#>IeR&EL&(a0P>SB@lhSrE#!|GFujM6{6 zRy!wM0~(~n;h*6wuWah$bdfl?ZE9?4h?+$%JGIdGUeO}i=vj87&~HTm6uQnPfX zY_Ro7DSzB62CbpBF51xCQg79N_o?~Dch6QW6YJ`#*9kUc#6MKLtnT%_lsa*%AD*O* z&8r()>KMeyrk^WM%`=v~>!I3+z=wQ2phuz}^{@9eM@^dQnxdeTCUa1)gkn_G1hz*< z248a9wsrz(wer)sMNx|VVFX2gjkZj)P}N2ShzvydG$MCuxvP;-kNTzG1h zvE-8hz+@rs9IS0%QaH%z%0!kj?z;7fg)?MnyY&f4F!goO)|SRbt7(B#6~;M#sjLkG zteK!xsdN7Y9_WD#fg7nMH>^=-o6#Oy>RK_;>RZjOnR}{S@;)l0g?*<5U1dxTlrJ&r zf2ZlCQ=jd8`>#cHVoi16qYV+OxRO(4vZw36?}s zj1$H~OO1|KH3SDSjUxug&rlTGlk;%oh(>SA;4E+D;~2_yDVU#N##3JmufBJnA67jYq<7x5QImnzV?b z5RpQZ1w<{MWxpYB9nwOcbU?Z0GI&cDYqjAHT`9s(&%q#KQX)D7<7O@(j?q@2{3pXf4lF1B8`LIfG=0bCsy=S^$x9`% zz(o`vCD|kp_z0H%FeNkzgGIr$?+~eOSqS(9fkJPfsKxJ3E^_;dLI~FcV6L{}*`6R` zHlTMAn#PBJ-N1apU%G$(D&O3qd2=g+N)>M4h&Mo#R@L5;Zc;?P?2Md=g z^YF*~dT)j9zhIVoiFg($DB4jn7w+#colpX0C0;LrhZQU;URvZSPAV0+xn=3BN>3U5 zY4O{u!17q}RLs@AN)dh`;#j%(p%*q+Y8nh>QMq1|NR#flLGb#uS*I3vXnP2;H6M2fCG~-Uk7hR z_j2m(5y1>e(sAJtycDrvU{WFL<<@*-;@F=v(hQxbdZe|LoCiaUFe%u(`0g?|Hp6G;m3q=K*>2Y3m%_T(D z6R*zk=zXID_~W7i5TSpvn$_J@Fv{9ru(l%1rbLwhK8bK-8mv8JnQzkcKB#F>20l2s zT=k41I#S>0Rg{<0D0r0DM4koNUYHsVcx7#1w0w zLv?N0YBK6>e&Sq9xst!;hQ6t22~G$zPrt3LP1xGPl^uG#Ztox`ZYH;?SL2* zMO*;V>t(=M`7zYG*qzjl#LdNIomxaqt-uJd<_F3c@Om>Aj2^5xATj|zaiQjhxiyE4 zylkuP9}}A@OfR!T7ic=%`|y3vhHEquwqT;wy3TVG5E%cwDyn-15;Px>6`jSoi>!hc zR5jR(xLsWnVRGkHR3H5VdU@)5uMc@z;U;mU4}m5YPn1gKnY^6V4Mw$iU>6&K5{q! zs2S1Juo}d{cNZ)r)1+{~pG6ASp!bq=AVX)Npbh{M2xiT`Y*rCZsw=_qtp)i`Y61*v znNEDWQ|nbsNOT1ob~)$fTtFEza1?L&yzc%4^z-tsfX9vFaYm^U1g>a4v>$5eAw1_w zmz>;)A%fCG4opjd8XW4MfM$9~b}*@EQz1XbUz;_brFcbt`qUT9Lcmta3T(k@%?EQo z_&@-BN6ewHh(k99GB$^5iCRSJNBpLtE-ZQphMZ!*w)+BLT@YZ>-F0a}R(Gu_q2s^E zevywfiDMM=@68?$&fM)Wn?NgJ7EMXYq=pHe7=t4o=Ykb-Og*@>`osM|Wu*0+1=3*Uz z{>+B5@(msaQjbjsAU+Mx zEORQ&(cR-Xut2foCCe2rEUNlpC}MtQx$ZUXt4x-+PVtYxEE`<{moGljyP=5PuPJ6Yc-ymnN{(3yBCh-^5odd8s0*!gkHu zBf^(q)JY(PWIy2YkfiZ4Nn|Y$UtnHs&621VL>Nfeh9UT$-8o?dgu^xlElUcC;u4+F z3mGd~6neGp8}6e|1m`cAvm3!&(Q-cLC$0cAZ$J1TD{w7X41BC$YYnnTzqHPGdy7Io zKpV?Z7IS{3>IKojD-6UZXiZUllEuMfKu(uyAU*Y1t3{P2+CAQ?Nc3`vMyI{#lU>0J( zg_8owHjp(6fmPDP7)iN03PanxP#oo0km1?M9#&F(EmKOwyN`P5dR8}y%gkjZ!cwSLdT3%5&yQn-Es32 z+<^5Y#g`g>=^?ojsAFK>j0TVy z7b2265j&%-5NeL{4ebZa!`%bb_#LSUM~v%6lv&9Q?e?iJ9)uz_YjCu{A9azIx(MvO zVbQX^ZT(7^C-C2nmEv5fOR^OlLpU8FzOmY3D@Axw6LWtai@a85^d4yt<<%cizU;p$-^bAS7pU=E^p$#wk9SA-p|M zg|O^|TvctJTGgx?z^84v7l(>4E`l9l-_X$su=_#wjoBUifH;(efkBO-aFePzQTzGKMQE#x{v+!0=qC*)vAA zx*Pg+8cxApG>jxH*t1IDfYaX98rY_~2n=A&(%32|dBh|wZOSB|4ja4BR}^Y)G_o zG^3%>dNg!~SFcLH3)5wp!X#>hE|A6cV@^7M*}E}X*nv)pK# z=*{2SSl<*$DToI*ds9Y8CPz@Z`qHwyuAe-4O{rLY-oJ9D)yF7p-zgWL(kXRFJ^0go z+U)7p9@ME7h!=1_g7RcAL0|avAoHQ<2;uK7Fd@J?~IJT%cCZXaq3wSxDIQahbh zRjf`~Z-P_6psPQ;UtFb?{s?Qxh;-M`(9A3*X-;BM11w&HABoMQHHrnnZ`DzBZplKIuWLE*6M~*k{P{`E~ZsB$?};3OTlz-76ZFF(WS7@ zi!?uTI-Ivck@~FOK^>axmy@ArWSVy|(|7<4mxiJKP}4IXn*Pe zG>7rtbe$E6C9^6QtBb~JLotge4<-h&3&$L9nC8nMv5etI16!K~@JO2MB9YvElmuOK zB7yku3A&aX1(uNc(ab)r-U0Gs7EBc>N?7B;0bX+{#kLdE4VpuS; z=pT!8zW$AZyb@jA6R?&|!1^;kHAKO;rjk!I-wR0^MXa``QfqE1kwg-m%Ar83(4W&o z*JM$7Iu6tkwP<=6nndtR7#gEet$F5u)TD@944}C#R@YFQ+Ih+MRlp&nc}6rXA!Cii zENG}}X%H2J*AV7!OTJD(AAnZ66QKRx3BZ)Fa(SsO=Hw@_WL;w&xJhem>-TT`7^Zty z-)Q)me+Yx)g4Jda61iS6F&UiIhaUG+=Kj)f|eW1(3{l}NLZ<{-^Qnx{M#ny;ugCjZS<@A|0A zcZcsX@2|WMcsslv&u2U%o@)0C?t9z^-ShPy>z{RfwD?@{TZ>l~y^KI+cNQHeiWGSZ zUqlerV}%zL{G{OC0vwwJzZv}7U{|m@@T=nHRJ4n<3FE|pt_8-#^H}`l;h(VHqK&G?mmj_(mMYqCiyBG|t-A$Kn?HZoz6%$}v_3niB`h6< zDoe7|?$L1HprKs8uw3nYU#ei+E$V*b<==gLL2^~oW__~U@mBX=7#p^6_nyC?q+}Sl zGNXy`!T3Zv24KVP-G4z*xk`%d?wr1)WG~_%#u4aHfbWdLdYcPquA-v5cTHc^d6yK~ zz0)qKjS3TNmjA*|uixGA=w0vL_hv;y@ZZ$;F26;sNDcq=UUk8lLzms6cB}eYeNvJ4 zjTfKOR-9SC`4;uKsxu6;ap0!ktVo>$^+a@r4(8wUjQY=iSx*Jtyk9F-JMT_SZb6C0 zm%sL(WuA3ci?aTVI~S>)h7o%IzK+y8w%(#%QCX)QunEXvDK&ZdhS}=wEyo_2uN-@1 z0n$RGMM#U0LP$%Hs*si=k?N3EA=M*AkfKO2qz0r$ zq$Z?hq!y%Bq}50lAzh5L2I&%{OOe(hwIQuTYDZd+v;pZdq>V_MkTxS-jXETNO7ctNL@(XND1Y! zM-D0auvgV5U4`5APsi`luGec%Y??fIZOKl+k=?)7-0t}EDBGe&d?Z|#z0---7(4$X zP?^2aiCRiFs&cRzY!iZ&P}M*-fPimrc0>kd!7dY4L2&-(?ti;rEfWL)vS8A=z{t#4 z40_CZ~S`QUio6l#ZQsFHU=TN{Oukuz#le4kQN_4+#&O8$?=yNV6kP z{v?}O2MGe0WyF$rUEhKD02@Fc(AT&GsC~0EJr#lJK0+rrU;B#i3 zk`uxKtlRPJX*+`(jr?7gl%tydd;}v3cqTX?6DEyYGx!+-02GTpaKWxLMdzHu8^QQe zP{ih9#vzJeWSKWql#UU7J zPK4uK*rV-8T3^UTuiQPz3UKFSy#~R@RC9D*R~?E?5)HBdz{ zaN%f}+Qo2FxMu3iSsmJiBVcjx3(f%qH|WOb#Ay2u(m}5q-fL2YL(0SV0mESTw7mhz zRqbfRs;5b_(H6&>a;K4#WTFvl2<>k~BMt&e)*rttRW z9BogR9|O^)UlHUUX$eQU5!*54#das(h=I=Jn{<5a>u+obw>M6CCF2cH+;$_Lx?@fD zzA9QXRhtSZoW^LZAr(QG@mc*4S=VskS%X2a`5O2D*k~u{U8_B;<-5Haf)F;so5|gfp7(h(+Pj zBo#zS{1s~TaWq6obLp;)KcTFfw+I`y1pTx zc?@9f1wag$!8Rxmh@LS5M`vN-D?L$%4&ek0_99S^qsmx;u!PaY3U&h$Y6BjvhH`75 zVm4gJhSx1zt0av&)Sb}Q(61}p9tU*D zU}z&@Xbfdv=cTWExaUtZ+{fyBlw z^+-pMjv`GU-GKBaq&FkI1?jEIWA#ZzFY&3K7hQhC^WtX_Meb{!mA4|W#x_Z0;Tec5 z75Rc@9v5fJv60-A7C9eEJ0wCr2y7ogXi#it9#sAnX)W~)P+Ix_2BodZLun9v9Y;W% zDD9iVJ2uIQM;AkJZj_VSA~~1~^gZdLnzp=3o3eKx?AO+k&7+HB_ikt&B5cEEA8av& zgXRQxzEo8MZS|GAn^&Yh`%6I771BFqy|^0>*QZYZKvOCNriFQra|;I_IEOKB2>*Et ziveP5q!su(kRdw7)?s;Q9pMlAhsFpFB)s2=iG+h>6oO?`%zcEoz(jq+$?daKOXmMj zU8vQC)*IK&+q)o1_jt=W*~Zy{g`hNF2WByWc-Whf`ZVGO&ON|Tz@6wWHi$q9{4FxI zHq-;F2MZ(a3A`ohdqWQYPk}@wJj#I$J{U6Y`{O{-MQuP{grfr?Cg2Gi9?DZJXUl|Nzx@?B_4bXXUiss@ z)!DQPKwcsgj3i7(jIO;LHRj$ zmt>&u>W8C0APn>&$G+OCda%co-U|3h}3~`7ZFa(Ul+t+$0j*~Umtfg-xL94((h2xl`WW*0i z=RkW7LPHDqDu_?wxOZ=!w`e zpyGA*!BZbNYvhu|M-~~uuL(EVk2@yNuklDxyuwo#>Huc0zy~&-``4cp8h<)A@HNn=5Q{Vi>!qj)> z9a00^K#)Y|2eb(W6ZQ|e+F;!ja3(mYiFYAy7eg%}t_O@v$wGxUO{xv}$ra0C;Av;D z-h~7#ZkvCj@u}gfi{T@Gq;Z>8w3(I7`5I#K*p~h#Fh3v-1VXb_bVg$ZII_M2oKc|K z#u>5>FYMxhvhX~WIDc$&=0I7cS%7rn2wJ>>)fJ2vYPX!dlltX%UQjCifEZvDfpvXG z|0VG`M)Ae*LgSJrV^_MtZu^FehX?1+GOqYStfBzpVk6!eJ6G(RZQK+HE-Vw-Oi1dk zQC7`({0p(#0t_jPF@&go(D?ayN0rf*I#5wc3k@4in%!ZX8|#>D_&z*dY&=r#^BF%i zHWpO@Q31$z1Gca)Myt*t{fi=(re51}MhOPc(Pq}v;7WvQPmS*Qsv4Ua<9Cs&-+A5S z$;D#g7(M31@!QbhkvkBsqD1>9V1e%X{TB;TU+?71S#`NT2!s}~``BO{IOLvn0We_z zFDN!0f)?yQX$u%1hEf#yE1A1^mzFP2x9bR%||*pqYCz;Mp!+4A_}Qi?j@>qHYg zG$uOo+}|9Z>KgtlT|M(p=$yVfc zM?zqs7}2k}8GJf`>~F@6{nfir9I7q!u#2k~3rO31r(D;K|r@h}&?vkvDAuowqu zlw;?=+PLU_Pt0G%x@^K|A;QfttjI?tTb8i{C>n%zK(&l+!v2SUrgkPk)TyD%G-Yn_ zHu7|vR9B};2RgJlM#s=q6^F$4O^_Ap1NfN%2)GvTigoW0)(;?X@$ndlQ4E&&t0%!x zA^i~si_alkquq3wfiz%pyUF)nQNErJuZQFWL700D{<#scgn&aD7k_jBy^|s;AJFn_ zbYcL50#`DMEL+*eHEU8s3!X#RI|e;smtu~JUc{z}s5+Px8!=4ai~T4G=>qA$(cl z_zfEZ&<9|zAR&uinBm*R2tsx=AGJXxPFGW&9*Df#xNde}@wS{|MhRDD9DQ-$s+oDG z@#mrY-N*H{w#J9#$<}Aw5#}~;>U`Q6%Q7- z7tbmBIcx}wqT!+~Mav6cEBtohrwZ>a94Xvf7%KQ}!B+}S79?G-xSm%3zTk?2FdY59 z6}%r-1uenC!1n^547@#XAkYx-`(N;X+<%+@8h@j|%=b&*mwX@cz1g?RSM7bx`*rV! zy*GOIdRKV<=sCC7^Ks9;o+F-C_kX!R>rT42yH~kO^jGw+>JRJh(EIe&dZG3!?Mdws z?H27yty!y7f31E)y&LujVdW>v2b4FU{_?*S+D_FBVu3AqYSFwZb#`gP?zOq@`(nE< zb-9##)YRD*E7dh;2Hv+=+ocrc%BnT)ZhQ3a{8jT6eSvn7YJB#$iP>sP)1$u)RJAF3 zz1F3s9`n>`E7ctV<8(pQ@AQS*8a4IG=3l6DjNJuQm*^L2dsSno;_Vk0pYv9Q^;KG2 zHI9F&_QFS>E3A4c`K|Hgs!y?v3+-==$O^zJ1#VCc2})G z_Ur@j4S7&ehIQBTuFjPE#+TI(c$8(X7kpQxK8io!({wPA+P>`}rCn=Sd6oGqwsK$U z_~grK)tPtTdcvcuO~r3}S-n_1zU<5c_dsc=;+X zU*qNL%9+~_e?vL)L^6O$*5ta)ReZWQQCwB@E!Y^XD}1%^{ldEF0|i$XR0O{m{F`8V zPPOV8)WymVl!ugVOzUUNiOqjbZ1o!-dG?~E0;X!7jfiBfrVJu0zKEuBa!G6zOc42De%U2=Ba`_SC>;fXse8KHE zLjC2QM~`n?e4T2P>>XTcJo|x(`Nr^vlckRqwkYYY|4yw^ zOB#&HIjBAJXFy|NlLlD63V?7~@6Snh85c>r!$P^TIIyr#%3`BUxm?y_pLEdlkvT)(Xp)We7h)9aI$k%EHZYkpS^Nkx*#X+ z6)LpQc>KN}%TiWCp2x-@KbRHvyd$F(3*!1@yAl6g`3mF4Fus(+$mqj^GbEC{)B#``;@!i zy`cER#kUnlii?V#)Sg!T$~V-nDj)I`YjwWw1}g*qsx&LbsVniyf_c74y(aMCz|p{- zKqOG^|C;}#|1JJ2{1Ja?>Yd0iTsr0|TCE*%xvDo{E#g1MjeEM5t4#^xkSHS@;A-VnE9EWWUoj-87)QiZ#Q}3&Kw_4L2z4+%? zUfs^O^M|AAe8}ahyJESvLruMyx>Z?{dc&^gmBWPve7gt27D@`HIv$>{?C~_#eGhq! z(BGF-d+R%WF4wI8OvU#-q=Zs8c0RAH3l_P2=xg=1(;#vJSuKA_~Vg=rq zR~XXT)s%Ak2LX;!zic?QefRT96oaa_7(X0tU!#RbyHcfB@Sgi+*K*_GpFg=+i>_Ll zS^ye&M)!Tmb%7v%8#EcH~N3_555lt#b%(h^l^nmoA<`SxgP#LBls)sxNj^`qu%Yc;hA zl@djGG_@Hu5ZD*%HFd0a@+4jD$5gtDw&PcmrZw_Sk)uGT)96A?ZL!{|($rS#GsQ## zIk|~hJfcqGomDCun`BvavQFamJX8W+s=^C(F)GnKc~Ssll*q#A<^Cp}jS+VNn}9Yl z^Qc?FwW&na0Hutl$alT?7(XzesZrF7Zm#QmxU6B1UCUyUqPy3z8?RPb7GK<~a&Y(y z7g1Mejz6|EPPxfdv1lXEZ8-Xi*kUz%J7yc`9iC9>6BB?x6N z$Glk#wD@_67_Pld0Fv?Pvw~G~tCA%J!4`M0s?2?9dC(p3l$Og5;ENk%^Z9eDY!QEA zm@qh^xP+`1?+(jq@#loB6Mo)QENjG{bL|SwRg}5A(I^fGi-_6vxoNdspPSa%^|@(>U7wrw+V#2VK)R21P0mTz2vu$Y{fVMc zXG{kEycw88?Cb?VbMVb6*$}vFQE>&)q0Cy`Tx!?iX0!fkM!@ zD4lU_B*6DueI=pu-lDEFp|W(O_?PSOyNm_*S)v^of68yY;x z*KSUF6d%z67(m%9=^CvJCJ{#`gejV3g=sz`x)|LY%s+Pns7@GZ;&0TqEO^sSH9(aH zysU2kY=i9FKGjd-Qelr}zIdqzkRdFE$P<&7DPGf^2Y1i|n}N$Qa z5bLbZ-@G8;vs{;ukCUKua#p~D(=Vu;%{O}k0n`6awh+Z90)?^G^BaxH zSG5eQoovs1xQR4M7h2)&4J({JI2b||MdL(-!r`t1$M8J=<~g;nF_5R@I5>wwmEokR zEQ9`y&w1`5ev7t<6Ehm^Nkd8nngq%>6_R|e1!<*D1uxo6)+&baXWDkA=Kv7{rcAhWOtk3!^ zZI%Hk)zu55U6|YgoM4(dMnDGAPBv@?>15PPM%Vtz?RnczijZRrVuV>QhB?|al_X#^ zNk1}>KZpXHmOLx8J{F2LS&7Tj6lm1WXPw zFU0CJbpWmLqrouFgc0NHJn~`)QH5@-Imzx39&Eri0|yrD7l_93v+H27-pkiLiXeWV{C{TtE` zk$!~qW2B!T{S@hCq@N-EJJQdQeu4B$q+cPug7hlVe<1xQ(yx(z14Gr{D(-r>cf{o# zp_OW{xAug8^5k{GO7;Dgqg6gsqu6^-Z&vEcvc#rXO*nP-_WN+y20rUFhK^aTR&cJT zh_Z=LG4TALP2Tn}qob2(#KA8j1tPQ}O@&Z~$SyD@ghjqQrpED}#Si6k6iBM$dN0ng zhenfGIY7%OK)5`cIkGZ0-X`9=$hzC zGQ%qT=*PNgKZDJpXtzny@@3E_47W0?pY?svrCBx|x8Zx{XlYhf@F!ufDwnB5)T-Vm;~Ix~zOPIu@;e~svF zDn}vE5IS6PA@ds;cALu3#E~TOF=q~XqkzKB0b92FnpvIwvpGHYD2~jSeKSIewrz~0 z-%3(I8KE!9itT8IoZcB#rrQ(C6>bG+&yb@xbHBhTnx19h{g?$7VwTu`5!~z=v&Gh` zA-hMQCYa65Lo<|44#DPxK(l%J4TCRTRl=xuMt9kaiULUY5TGxUi7<_pfl<{x^Gg^! zc(h^KB=VO``9Q3#g8m#ebyA(9|0y4koU=#P!B;T=PBz?`j}5QSfj~y<3ejp5(gqa> z*f{pF8(_2t2NKw4B!&Hj{V@R@26vbtP#is1U>^>NUx=W#A77eQ9o!!;lKabvnZeO) zVqz8$TW8qH6y6#hNa91-S!WJq_0}+1B20tX)uxOm1O-HDK`Cg<{{6dQcW5bfL?kB& zWZY*R1Pn4P*~d_C1PT-(m0?a_UAA?~(q1^j}DSMEVobYe;`q-af1z8&;51Bn?SNawB<=yhuJIKT-fG zh*W@7h*X4Bj8uYDid2SFj#Pm(3#k%mHqsoVxk&Sn<|8dYT8Oj=X)#g=X$ex5`q=PN zRq03;zRPvc^>bI@TMDmKA1|C=@N&UF7TgB7ihIrIu{DY$3yU)4r#Gze>`$GNq z`nU9t>BscT^(DGqw7qDV_M-Mr+P&J1+O=Av>*s}kEc}!FsHSKu!Clq;mB zPP-z*jN@>cRXj|T4eX;)OMU;u1IacbpVGXO;Fqdi5iAh=tb8~BRyC-n`1n}a)*($vLxTI2q<@__q2sb2iP&8_@;Sf9N6#KuZg zv)~g({M|oZnp*pXI<4Gz?OWOckLx2i{Ck%X+2^ZDJ#zaBt=QxHJ&w=HjmVPPrN&E3 ze!)uMkiI$S8Gnam? zRb8a2#qGwqeIHnAJn-q+dTQm;H5%|(ZwXxJ@?EUG3AsJ{jnZ?Y7Z~+_sI2t3Ud6%S zAB_{g`0P^Sj*lHEI#cq^R`qIqewk~ID7+V?pWUNRt`xPzSSe@4$@>yS*ozMy;PS*+ zmk>RM1`oiRnJ3`oe?Ydi(prFVS&Tpbu6&kW(CNBV+CSh#K2Xm7+@ep;Hd~K3ew{k| zuY0xS#$7|3-9}--f-?8paCg<+udJ^!UaV;dq(1-cR`s2#tI4=7R#J7}Q~UJPTfWn( z7LbB|WGJ05ZFqQe?i~E7)WPbaDz)fBw>Iav`@5|wE~|ODh?k3bS;NaEyj;r5T3*_C zS;tE|FY9^Pz{_R4Y~*DVFPnL}oR=-UY~^JeFWY(9!Al1(J9*i~OD8Y8dD+9u6};@_ zEWf9mp)$J$jf0~`gs}P zWssL4UWR$Oj+YT$MtK?IWt^Amc{#$%QT2@byA$f4zlxYCqb~oW`e7y2_Q)%0^wCf# z*q}sj#RiKC%5{_vDr2)WU=j=?AHoE~8=jjz8|uJgKj?yr7h; zeTmeY?)bI3$g-{#-lDrqG#@%x_w_)fP8TycM_>zSiyB#Zq!>XNgm#=T`{X+SKZgnb zK>ArH?Tl%64HH^fpb7i2MuP!q>TKQH)ruyHJNW-HqNmeJwRf=Zx^a<@w=>O^$AEJs ztCYHS-haTfkTqax>+iua4A8DqZHVl=GL<~@8ja~W%h;U=d}DQI>h#0kP-puaRyP9s zw>yE5mdkK z+Ti+xQhZFm!F{Q$Nqq15l zas9~k85e+-9(|yrt3lOqGn@u;G63ZCySX%Wq%p`S?f2|RQdShg_T3jP)3&5D2zC^P zbx;VD?&9SHFYn~#ZeH%;lr)r0Gq6;qjH} zZVK(9kom>oS7=QV69Mw9R0@l2!Dt*h66{%_7|5rC2lOQ*d|TmfoiIXSnn#xhd0uY1 z?N7mDx0WR&sem~OM+u&|3XM3vJ54#*bmHWt4-T}f;4~SbBcf&ohpae}qNW|$b09{V z#~FwQzZxA3y(*7A@;3u}PI16GZ6<6w37E^%Fa$EksTj9od3q)p<9U_?e|4HBQ8^T? zg?`pL`sEf~=$@u~3EMTQJDfcaUvnXCguD8Z@ZKPhO|HJNi2{S2T?Diw_OR#ZR{K?R z+%1P&Y`<~%YS*O^7#u*5o%z&1SryNGumBS}N z6x12QgBRnN1KrY@7o?H#y#@hWYJLx=mHnYyn5@=u20jL|v8Pn#e3)h)3Je}N@c?KC zi+J86TufL&JPjZodHQ6MaWcmdpEY-Kjpa+L=ni!*cG7n+niy#}(d%cOH zc{`6_t7Ipj6Z=@}dp(RYOvD)2lrf?_9CJ2c0~@dqe!1Z`bVUHLi#k)XOKRN^cd0^q{orYB7F|&^GHu1J&E)b(if2a8R==H ze?j^p(wC6FjPwlBSCF1XI*0UCq^}`;9qAiL-&7xajPWXIxKF-SVmM z+cj7{mL(>O7w`J5xN32+_W1NBRLmsTv1XKQT9T<1!$9Bppu( z*f9)b0}MMh<6^UfZB1OpXoq!>GpprXh*x_0p_YV$r2S@HXm4*HJXfuwH)2r1hz60e z5Z6w)mruwj?gtZzLY#y`Wy()OKr>$Xbm?qmG`02*4=MAKybPNXWBVYs?O*l2`+oKoEoy`aXb4I5)_ zbnzTf>yC_y3K{3t?3tCcMh+4XJ<#{kD_1e|*sOPAYNsg&=%dXburS7_Dr{-RD5MvEg8RrBNv-hA2_jMv_E z=VmcAD;%@RjB<>i=BGaoznwti>KMSuBeAB&)VYUuXq81n>1k|jKO=AJnLOEAHZVDR z@!s3Ynu0FOYVw@px zIcXh}++-261W|xT{NG^_)~v$6AnZ_A5-#G1>Me19Fa_joQn=Olj43U^g3?qzg>k}n z*_`1Li^n3tTsnvSe>*2yVxI%v~iUJi!kSj;@zC;*!&@=I*s5e*9~vN&KAtkkhUCWl6# zf8^pe(*hZ3t+y+IiI8prEP*3j1djA#UnVF2QOJ`7fwE{Gc)Vjoy#n_|tyB?@tWGxVOqu2m*Wf!_YpoJZ^>y-XH zT1<0ZoZu6c%t1ucEaa#wbS*G*AZE_y#wWXj_h+A5|CQHJbX>!nZ54QiHy06)ynI?Gm~ypf8kk z-U5P*lTw0+4KsA>yVusL?YG`Nm77F{rrc< z2O-gffHTq`s$LHeh5o()L|TIY(*szyzM4=t1dE)p(9prr#KsYjRH&_I1vV)*!UR1|WA!N5#Rid5*^x2v-gk=8UO9YAxiZ|;o` zgf@@DuN4A=EU_IRmHi<0fgzkLfa){qBdP?2$VBQ33sFafSdtpKSPK7u_MDm#)Y zIdhMCNqM>ha`13OQfX*uX%alVu*YV)7W=-hWU=Rrr~Y~M&&6I>%;mer72}p;MeSV| zOr9JT=6LTbom)fn-+-BWPSGmP<|bJ-~DbA(9|q{+UzL|q8sXJFMk zYT9H-JG~uYL6V)eJr8EW!0;4vJ!o@a9(EdP2g}wfDa`nUl?Khm?EB_z?67I*1bsrJ zwjqo+rP))4iBp80281}m7D;Zpe5HThVWA*nJmK&vt3gVd9Pu6y{&rW~~wxa;VYZqO$-_Ziio zWgHbB_QVpw$LzK=LJ1;tS~!~+1C649tQym7ZiWJqGnBxt?ZsXqt7hn1VhRBQ4rjyT zaBRt}IJ$XiPoP(EBsWCjNe>8guIN_S2xDv!YZV5*nI+}wQ>qX1kplIEwsl-qVN?S0 zJyB`XP}DZY0|}zH_^R`9x}w7J{d5?o<21+2tR-#8@Mi93=nFhMM3}ZAIR3=#*Q@&m zuZIf@P18(6BT_B(a#Q+_wqwtnu0`d?AlRaUPHLs?`E;WUH7P1!*$zShYT99nHqaPX zP7O=VmXF$|Ehb$`y8lTQSsg{ynl=CA9D*@yChbtEMm8WQBKMr3ITq-0nl{HET=Y(W zd!q_NX-moM+F;lKlQm;Dj9^BtTn)ph35Fo~l;93i$b>fJ7>V`aL$rmJm2vbxhSB78 z&MsP?gK3}x8sr?<8Xm#IWs{UW3=J3tsEo)GGrP9|Bd`&ck`^Cz8bhK~IR)~TYWBMQ znP>#ZH=?%H5!iRLU1*m0A`jFZ`9M8pKCoR!KF9oPz;MWFL4ys+BGZr+mBTn#lQT~a zi~^}bpu`ef{a^y;IWXLuxB=@iHXrEj$8-Vjd1UE2^ zQDKltFkA@mp#(0F#dpDAS%BHEr>_Ogmqm6Or^EjV;uuDI5QXg$Vd19R-!xfGkn23Pkg9;E^qcIo^Q!@s*^&GEB z4kC)h^pr2n{FXTqs0%2>eChSPg%NCTN5sm+A>jlF!r=6t+Nkt*#Jc7rFfL-wCS%U+ zZphKV&CZ?!lg!GL6qFs>>@12>7g0q=89pKO#&PUnxzos9McWb?eTadXkpi+vElH1~ zj2RHcI-YZY(+v@hE^QdqksfR|vB{X)b6ZT4dDe<13xi;6j^4C?C!<3CJ>S+^MMR~1 zoIM~{I_D`RBAbt+9t~NQ!1*7Y;Ba0{qHf5@3&IjbtxrsiQO#Ymv)4g_ouu+ki^}ti zf&HBN^|pTWJJ@=1otU8+<>l`GYKI#E{kTRp`x3_QTP+$Lm_=p?MLJ9uTw2?ts&=^Zs zH0*kL+YKLUQ9;ek(3d?dK*w%ZyzRwS0O0Wxyr~WKvj)17?BkzqMAZ=QDSCGzG0a<@ zK7>6S-k94Y1_;n0j#Vev@H`IuBd&Yqdi^y0Hpf}gg64*kkDP9val9)ANbw`QFGw8xReS~rsgjOVH6e)8 zL&P@mVKo4YUrI(ej^y{f1LJTDwkl;(p9bA53(}!r6g{KCZ5%h;Zi39pN5e48W1d37 z(PI1A#ZVS}glUHv%0{~N33L8=$49R3yIypH;uiW{zN*Suu2Ujleiig5Dy6VwUF{PD ztBMJzivb7IkYBf|p^(~C^$7n_3daW_V1ZHDU(ihkpt$Ma&oNLuM-rek$tn5|LBsmO zrAbh{m<*_Z$#^iCklC$DV)0JUSXtCj_X9`C=P&dHz3@ya^!W+`KCdqj@E72X0fL2ju{t$?J*v3%uUq(x5Mh zH-NGf^ahIyd_KP~;4eeL0WZozHoWC6^8<&;>+^Zfd~w5mZFS(d`&ZvqA9nxhJ8H=p z_p?_hOJU*KIeGF*)50||!)_^Jl=jqC=iDttYVP~^&t`~ck0blN+!#gawT`Xmm^`6| zN}A5<=LOLM`_5hmPKz*fJ&0p^`Sxhik`u5=fU%j_Dm?S?FwTW0IPrz`1P%lsm0{rl z3*vHXWyKN?0|T5e^aD9u#IqMhUU_n3&9`M0;7oH%gM}KxGBpptJ&^H`bAAW{f%8Mc z6`SFp^Lz<1LQYkTRqrO44+sxNG%T6(gODWBS#svU=D}Gd{1$DG<*O6+63~W9Cswom zqV|m1lGUx)QP7GoE=(%(7MSG>ZS|+sosns}lP=M{6NrH@5g$m>EU&r=5Ds|1p<2q9)z;gXCZ5rH7&_L5n(&J70%l-sSwYq>2dW6h z62t8LTx^=pVLUCjW$6e`I}edR_xRIydJI8V`0;#Az=#S2?LjNxcD{_JHq@FpXe#vN zw4FoH)Ob<^UCn`40U;WDMi|i%x9aEw45oof#roI=ewNbJB5P_3V32veG`oY*%oKng zl!?*g+^{Q?tgnM=Qd+I%c?H9o@k%`dn45O4IBd)H6%4PO&z$80ym*zv*tMv zTdcZ(`A~12nLRK4(*)J-9l0BUy(zXhgW-005=8Z97Q@1@?uX5jfcn@Jy9VT$lv6Ui zH7sXktO=#cd)Y5@!0l;nQt6a0V6YJq9-toaFh&d-Du^D4Yf67LC@16yIthi!5^Dgd z@Xq_P!=v8$zVmgAKlEn@VN;&~P|1$m7$6Mm2s(jggxO-rY4Ty<={znFeT2PMo}RIE z-&S2f;RxZGxn`}}8b+ic>F4jTFdj`NR&^&}p-aR#(V5jyb3%cJ37X;bZ1)i;BqCQ2 zVRzo22BZ?0UU|laKrB{%L|v6&FPDLMw_+Y<4RqeTIkJMF06T``0aQ7(?k}@(y&!K$ zwqRKyJs~}>x;(Gaz2+yL+IIr=WKd{oQ~ONWBVTywSkCa$P|`BI^mYuEWe`H7IL9%o z@GUo0s@O~+-ilDGLT@EK@X=iv+9haPRvTyMJS`NzRK4K%25K6{=CEwQ%^sEyDF{e~ zt#oeBor`O}Z9z_UZT*!|7N{W&1CpfOTgGFIx-i2R8i6TKF?f7hO_o$sE6O>D7-!~J zE$ENzGQkF7h%<~h3zE6WMq%FfBn6~M0wGwfGBUDo#g@kj2|yp^&Vnf{59US_VMkpu z%R%qTQ#b5do#j+ox)4+eoxFelE)mntcxCWybCbei6b5PW5P?t_g9Ecbpg~eP%!CF2 zR2~nk0S#c8@k988%14+-4nPV;%d4ZcBpFwm}lMCOx3(uejWfw*smDB9ei8) z43z*GT3`O}d>6<9Bxpg1X|Oj|G>HrPAzjuhEGTohumY^44@YTkfB$^(1>7mHF>@-L<^BmfQ$6!C4V}&$dN%kqfS~#cLBu+ z^Q+19DCVppB?!B?JS0j9g6GP8fJe(m##Gaejw7yIR*j@)7VH6&o2OY>^y{cIMnFK} z@FP}L^RNI40u9KNH6eLyZM{hs6t)W|0|eR=ZYdd~$>VIowaAAv(T6zShBPzLKbXMz zx$trT)|*|?jH0=y?>1pNk_2Bx?@jO=5bF*si4H*$oQ_vwM69=8|H~LE>S}H7M|eE$ z3v%{>fKYSh#ttigW{jX?%YmsfZP6G`?xz5B1-b_>pQd2WD>+9b0kGu8JT=A;LvJ_K z3q+!EVBzFvnLOwQ(}t@6C*KUSAcjc=JRB4%!Q}GsbDnsM*wbVaqB8)pJ^?#=NPgJU zl5|Oz4sv^g#g=#)?(jF7=+DSz=fe20uGIO4Ejc^9{u-OEGYG9A_7^L-FUWs39F!8s z?Jm#llt7Z6@H{V zBaloC+OZ=;0)tjs&O1S9DNpl7p1D}~!va5cs@%+M2sG}%W4RWUURsM=#k~qwFtiItABO8+> zM1W{bgMi)5*>+3`3Ce5A*S2$Qqj0&+`3~is=GqoC+70m%RyIuAEPX*XErhIbeDfXC|*dy5icdP9lWP& zuOI+(y99qtSe>BZ^sbz?mp}p%)H+u#I(f^+kS1^p0XS$f-8}S4k)zATJPhON$0G%-c6%4j_(~JxC7LFl3IuUNIjnu=cx@!n@#N&!MEj()*t0VO_FqsoR zqR7&WIk20m+-asB4S`hwWbF`=Z4uzbIj%mr;hZJg}wGEUR zCCjI7Rj4n8Pj!AqKodZ494waf7KD|YlW_|;hVxkqXetQ1W{6&JmjFd4MpNA{ep8JK zYq<-jNFP%{<-mX%>zg7eF#)JR78~{{6)0t{RmwNE(PHj3PI_%BS)13ksQ0_q?2Rbw|d@f`kNZjy8 zpBTm&o!nZ9C*+sTC+&`B=tAf|iJOshzJkdywHzVS!{_s0M(JQy;CVf!bFiuT3|$#_ zd<0~U2%4kVHaTvBoXu$-qw)b#S*!uOW#)@R#fGDY!z0jG)}&2(L}Ox&p=!ujqvMH; zOk)2pGJxJeSlsss*iu_!77r<*#JLU4s0xoqwkIv)CixlYGlh42*92G&0+)lKTiO6w z5_%QpoBb0M9iacn{W)~6qmhv&D$>oxJYBu@qF0il7X+@yU`AD%P?gLNbczWhyG@*m zIKBZ&Xu`P)^bI#;wh`lG8A7Eyi^m@3UDFI!HV%W6BQv^I97)19I;%$M5``Q9UzUU* z!i|mr7pE0dDdmdIn+2@^`bB(OEbmjZZO))5uI*DR$kjW?UC?dUc-Qy3fnnN03T|T;wh5Y*jg%mg|~v;3Mo$Iak`8oq#^f94#wrQp_u7UdtRl-MLoY zsaZ+E8C25@A{Y;w(~f%$sr_RhIY)K4*ditZ*u!`d2Pw`cIeVCj|0z?{`4)LZ_Uv>% zr)Yyvxsa{Jym8DcYy1ToI)OFv%{*@Ha}G(ym~c-|u9rD$xwuWG5UykGblL3}Mj_ZE z92CAogJ2|~_K35?xN`AX?wn$)U=jsaCyADVH4e~6);r;0%#I__2(`ynwKt+LxM0u& z!`SubJx#{iq~iH28hU$z$M;O09Fd0JLo+T?k^k`L^3qa1pijR%MPi}#z*!(nboR=` zokj+2@&-YUCJ;*i(iG0T)0V~QGAx=wZuB@v+h$L%`+bZ<_C~OaM!B{Hl;(7GYu2w8=KKFGL+{7Tzj4M zZ{;~Owtn(_9zgB6dQU9PWNb<5$mBo)Dvi#aqS?9ooF)w05@TUhC|_kj70${4N~c!T zf13X1(LxsUU^ij>GD~`WlO;yf3V^pBaHF#ry-=Q6%t6dTSxAt|E|U<(w~`>9R9&*p|_v1|Tk31EEQG6l7UCi(DWftDY#!`srBu(3Z5MXOB_? z!%R787lnbPIl3?X!DPs?*cM*|3FXXY`Iv}Iobh>bIs1=uJezf7bO{BZt(^S$A49^t zR{q?@n-UZAV{l;ICS2GMoC(Elh1o~yTI>`5GOwy>z{lOe$2z{NB4~;4PM7aaD$j5B z)gD7oyAHAbzI(|G>u)5dmvkhzm$Xx9UKf={gK@zGx_TLsh?pbsE||$s;4>*7n?#=S z$}HUPqn7Pb^P+k$v0zzAi8 zoAizzF(klO?Gr{Gqs!BgDPP2p$?9Q%t+yNRF9z(!f8v#M=lm98TH4Cx_ zl~Y_=LQv5R?S8&t;`bcXY68AOt;F`{qiI{joZ>i43gHqRs)oH|Iv|xWRmqH7CT&>K zgp~ah>Io92ILyp`CXRljDTuV4l9~efaS)GicxD_c+gL?D0)03EF{eBS831jiKg@x} zNhbEG*(G4qw}zp6fx(Vt<1{4?2HNsj%~1yqDU_R_0#tg+yBxQz;Za1YL&%<7&oNuY z$q?S8QX7iVtTvJXTZB3FA*Q0OB(*-Fn%@#>d=u+D#6U?d``XR_FQ_7QI0fQE2sQ{=OLyQo)Cp`pz z0y&)s*GNdbc&L3-c*mx{%%Uy7@>DB3cGq{+$L@MTb%)NlLmyBc@vPi9c`_lE#0NTO zSQ4Z8^`_C9+rhUTS>rj!dkPbbZrxK!2zYJ*4v4WjpLyr(IY)K>KXY#$9>;aviK4oydS9^<+#28pkO0_N z8Vf~91VM_VD2gBnirUEr&;UVVA+eBzWUEzhGIktqN*r~zFD)hWhL~g$OIhsXn|!f7 zv1Z1eyd=uJOx8(aPcr@{<0RuOFY9~re!p|8s=I*(NPGU6CsNJss=J{5+*l+_1at80p!68oVp}$3&DpD3k($&| zZ@nCK^_QdutFR_T7-1OfWz^)9%GSxda&gz&3!67h`7B})=S9RaQCs{64;|4~c&Kz& zOb1*_&8A-1y-2Z@8MyGd0%^ne4X)B`iU?6f#;XL@P{7rn(6}|tl-Is9Sla-TimFa+cPHSlJ%&!?4}SK) zCUZk@!pYuEo*O?wXk~?(%HDFfH&l!W$f+(70clNl4xUKFWW)9y71(!AO1jfdbkq{l zJ9p(sYuj`sBs}@iwpQ>hCL<4VxV$Z!PoX(8anlIxRT*z$B5`-38j2(k()QwEzZvQ- zzQpXol(XHNvEGzs#iEFLKv#@PHAC8}SN2J0L(?EqH+u#7=*kvAf^x1qj&dA!yXmNZ zVACR$T5$dr7->VzJa7Vn13Rz^@5ptR04H>r1E*T3tqEsL`52LISN9hX1gW66o z2srhY4FnILyw8+@J=Z;Jm!|-|UBbZc`JPM(MG+{$@CV)vvp}aRp45N!(;d@`m_THh z5;q578YGtZ-x(-#dA0*E6CxaIU$H2_UH|&zDYz z>oD2CB2;8@{N+Y7Xa{{bXk3(XC8@yXI#x1?>1SZCM&*-K zZCv3o&bT$W?(Jk|UO9$;tA^m*y2YbpF%qxt#;T>N*!AeIM+YKrMf~Agp>Kqa20s$` z?Le#lp6}oL8ok%epEv!+v-(%`U7k_x7qnQ_l2_Au5qeU69M|~G{dkezE_wWTmf+Xg ziyo~DaR~7BjLvUX!~MI3%wJyA59HtaWVIQ~E{tJ&kYPx+(dC7k`7YyccNRXidsGiZ z%U|V3e)fa4jr~W`eMfrxx!(2-^c+g1j-*o7{`+_G??3z8UX?FilJDtx0ErZSWF)EY zQ7`M(zq~pGPRLsy{Zf5BO9t>vs;{TdDY@bPa!F%-cINyqe7CnF4onfZ=_fH43UB@9I@*{Ny4%D~uiTBLC z@>9ppg7(38-IimgHPD+*r|gyo?=R%v4lN#tAv>Xj^utuUJVxhPNx#*Y8#``>>U~@dIyeSxLHB zNgCcx1F3YETglABR`T{>=)pAWE!KqKV1xbL{Y6H*`H(dg5-a-FMC&Qmf;o{MD6Qp2 zX)W6}9o_u9pZ{xHnr)t_@b0UN&g{dj>A`{ifpn1vrb}zuV&de#y5Qe(c;M4&&zmlo zqx<^$+$o;Ae?8y)Uz+#kf4w;r2xspAEnLEnEUXm1`SV}%q{|;AZ;a^mggzi}Q%Q8rYVF>pUdd#8tR&Vb6=}x8t1Y^RtEb|Ne@;uXeFQfcl~s*B|q{@+k!f5jj9k+v}gs*7Ctm=_jLjN+UCC6``Ntp zPViuSo%?TpKJ(MT9pZqy@m1IV(_Smx!zOKDV4$blEo`DCFpE7YhTc4EFcCtY3S7tYTrkn-|vW7M2?9?Ca}-=d;_*OvS=*oqRKz^%M(J zk-6RFr}qA}iiLG=URbvj)(ZYg*=K9JWxR>zs~WEI|BY|e8#8`bZ__?oHB9vJj=|MA zYb~6(Y1Qq%+|h3(7*pbAF{XqH+F8D&*fBiw+ADnr9w@2%O8R5A0^|1H0M#z;5<#?54dO<=_3a<6HK!cU><7-%c-k z9@xvC2lle(fxYb6*h_mkd|)qo*7ef=?ewzyfxYa0U@yC+m%Up|%w!JR#vBnnQ)&DiP04Y}-Vfw2{P^b@ zp4g(NT_wZ$39q&0t)92G?SAgfQ~g#Qh3&jQfctdWd(c_t|M1s-qrUK`(<6HS#@$0} z{^U2lUYCC+^Cx@rE$y+|BNAq7i0U>Rj1;&f)O%lh{d$wvdH31|<*6M+VNdfI$RE^(|P2 zL3v3uo|&Cr1`5=aBL1Z;QXKE3niTr989NEE3rnb)zx5rTOy<<9EUxy>Our&Tlqa~) zG?krB4qwkM!5e$}=KLL%5bkRT2�#B~N55RZr=|0KFr-%5Mbj7+0e>4tT}&q!p6j z!T{7t<8=I^SZGf&z zl`TyYkA6@A5ns5y&R?5<-tel_`L2(DBB>e#%t_!kF4(0My{qB3GKC#S7QPDHOmjd^ z$VX-YQC*U)h*-1KCb@=TYeA=yC)69(t-d;}r+yt+Oin`W03MKB7pHSH(o7(&#HW#m z6TrhHoTbdQk^zL1t^J~$PAWZ!1Vw#0uVOS7mfb5cG!af@PRTDjU_N&xiTIo6PcZP-^S zAI?2?jKchm)1JV!br07yxtO{{l1LU{D}(Zj$tPf;5rsPSeioe0WUd8dTrl#d}Q1bf_% z7x?X>yydqGx`)*qWi^L={5)l7-6$=HuZg%v>$C13N4m?pr^`v#>@jlvsnnvK?U?TA zL!+b!ukPtb3x-(G2>|9^x9&fN+)EzzYZ%}9bUn?Sk|Jy{-A>&z;N)r1J%dg)F;hdr z(@f%(Hc6ht9u1w%v8+zjCVAY1MqmVlT)WYTe(V0@%o$gOKaS+D8tjZbH8l2-i5E=` zpM7zUo?`!)?v7N(3TAarH(JK=IPS;Cqomk17LyagA14`K^sp>uJmcZu@EgVfRZ;!g zr|D2_s=<3%Qu67OGN32%Z9ztyG&-Sq(rCd6d_C#Dp42>jc*vBanr9G=VY>#jpq4@T zXt{B_@Yc`1sMqc0_e<=HaSd-Z!#XVggpbOz=T)j4M>QJZBlDmqK%m^~I7&@h_s^i% z$NfJ1#A3wXNMc1ip@|7N;ZVBFtf;Py=wA3DLARjt9QK%))|nX$6iRsBV@zV++v9M? zYutr=vsq)G$2*n7z47a4Icr<+cxN*7u2JRA>lzASmmc3|;I+)7XV}u-06zy0k@!b- zzS6$`q;-Er0ipb>GY|4yEAF4V^8eJ`uXGRVExFxo`FFndA2wjZmiVys(?@@_=;Hxl zj{OOjbOenZ`#*h|FmQ0?#Cf*~l^cyBV3)JWYP$w0ub?eyP3vo^Lj{M2n6O)o z53RCJTg#g2;2sfc$@c8uw6XLDWFbyZVQ?hE91YlrJq(<-B9qgwW-~50$!?kJJ~K-Q zE@H3>zN76S1B{Jzeo(^qU@X>24=cbkFnkWLztmE!OtLxKWz;cctG;)C8xxQI&6_u#{sOQ#XJ$HVUqrjgoUjF3khQ0<<4I-v>up^IZP2O?>>F+5 zHyZg-mUGWdIpmc%C>5Cxyayb~O58)g?1w90llwz8Q5JsB(eeINWK#{sDIlRio|xm##f!3{|n5lI!_4 zVc?;#$r1w4Faje39!{K^&~-M`_9vmcP~{rHf14Dj=Ihqef_|etK>LL!-U$^M(7xz_ z;VOTI(5jfGaGBvy+T&QcMc~Ix<~t_aCT)GNd@TBKQ)tsSm2CS|$LvZGS}$4pW6L&f zEx#+R@VN&!(RO-Kl9}GFrJZ$|1s-wjPb)keJC5WzMOI8R2)o^Z}*a>rdEAf^MozcWCwf;hDI6BW{7CP=!RO6acUTNO@U z*D@9;@kq^flv1Unvo3v06We_PAx@NgFtZPIfQ7IF7!sUjN+*5m@VTP%b#c}1?RLQs zzhx)RgXMlRrAppNltw6B`-iH)_vl~O{^92mwcpUp4_&v`8VX++jp$9)N{2c&Ge18e zC=bw6Hh=vEy<5GwDle`Q{sAvimyzSDPEtl!${X$Xr7ISmB)RBwObi^Fev z8jf%5KYLR={iMEozqM8$AD-Ra@jX-h)6^Xgml*2cSCc>d(H}Xe)Zt#`W>e_;@ymLH zS2^7juJybC&`6L0Iwi*shX^+e8pEiHlZ?khUotq?(Qy!pH^u;>udAB@ajT%{MNAb; zJzUbkn>iQli>U_81jc(Jf1n>w`ZB^!az4s8i`TQ+rS>Fz>k9Aw@Nau+hoNqj zleknVtcF5v;@Yv4WZ!vpPpozqu-&+WTgIcH9QK@rp{S-ceNQk{LUfy^D7U!6M}eS+Pg3sV$^d zLy7#kMYvx(;k+>);Yf{`exO`tjQ20u`&$_(Gi|alP94X-9lVYMi8KR^nk$Z1X*-}M zn4DxvEId*Q_!I4($&A6!Fd;Jm_84#il$xlC{@3)UZs(;dlQL&=vwtD3>ZF-k4eBA}XRD@wesJmEM^m3l`pt|FKCc(eT|!}dT2a5?d| z)x;mibd!7Oe2O((yjGH#Da1a&L*M7?{~%@Bm2#OzH^&Y{rhpgl z&1~V_=SK9y38x^({V|*W>R*1j!F^1&qE}?LFm!N4-;r~YyU*bvf7))dj2<-QnK6i? z>-GpDKjKc%t^naq!jm+j9ui&z=+cA)r+@_k1{dHJBOSSkdp|*BQml=gJOspS0DM5m z)XY-h{Xk5s&98ocQ*|NtQ{U_HZT4ltu?JQfKeUxzwJWFffF%|A7SJiZ?%(f4AwE z8uF1#v0wxHjPy3wF#RkibK%18H|sTEM({t@PbeGFVF+G?bmMBEBGJNvhp8c}?Kohi zMY!9P5JET;0ah&BN*Gt&lKx)=&5zgRYz|i|ls%waitLeI zN%D3sEKa;qfrnj#Jw48{L<#eR45us{msA8Y+DPokUTz(WnY#)OofuBC|Fzs?gKmFVk)gq(<1FC_7`NWVAI%~ zaV`b+^$p@a@EJ$ezJ)@O>{#ij$(WwYNm1RYRC_9w>bNzH=md@!#o&n~gP{wQ$F*5Z zVi1yh72G+YP_lU)AQ&dB-cEki z7H4oaP>~J7))B^f#?ZtT4Mb8k43u!N-BPE!BDpg#fMfkscYY%fDQ+F@`EUN*Uu?^< z1x~pXy9-I&L4&^uwluUyIi$zN2`4W(DuAOZCJ{fF5o~baz96^Hp1?_C9wz=NXDTDmjCN8ryyF$WigHb!t(2U{!)@4BF3i%%Q%tK(z&AFKA%)nnI}OvL2gN)pNhL zN#&C~Zk1KOv2Mx!@HPJ$>W|!%nxBvjJ5Hq=d;Jg<%Xa_a>-`MtomY-Wb8rxu`S!bv zBPa7eY~4+!l15$2zvHRVPi5!w)@SzhiMMo(J>^Tir3+UvHVwg|Gj#slKMdEOaaeR> zgP6;f9<)C(Y^@pbp_{u8{lJ0#DQ-%KwBo%|!ZqdJ|Iyz@Y)Uv(8w77Ey!|_W>}dcT zKYuI|c4rtuWeP{tBTz{7AbfT!v=7{&iQ0J%9vT9}jXovE!136gDMKUyfgH$k^+uui ztSb(e^I9>%X${2G5(V%gqE}zW;R%}+2}%XPD1_~9Ti*~MTrnrn66iNY)iH7&N3=?% z>lK(!r-1IxzKsR+tgjl4KoNjtgz>AidfZ^!m>bve%B#0?i$a^T6oKhrNi8i02ybo4 zQ==ma;z7{0!-g_eYzfUtb<{;dGyZT}@@e^2S~O@>iN1aAa0$LqW{#CA zN^Kll1o*}-iC%3qew~=h9LJ`RKk@5gcKkx|SNR|!ly`DybcD&C&YZQsDazwj=O9Rm zKD)Zc;+rmzV`DS=ldWFGV};MBf6r5&Q;E(ZgbmEFilV}c{k#EKp@0Fm({wL`SC}xS zDn&BF_>GLGGc)tl$b!}wD|INeoyt=oV>fC>NF&H?V$54Y*-J1N(@we~>v@ zuvE@h(85#9!wL++ZU@A36s%jrF0~wlMZH&Whf*{3tTtsBqc;lW;~}9I1Vip zQ8%_5P-txT=mL*9@KbqE*^oZ#$x^v!ph?ITTBTzbdP``4J3Ok2b`z? zMVx;bVay)kc9v2ylO!KZEIoE2np%O$41+pMIK#BwLAX}PLXQhtAK~pdE$=Ig5Zm4- zig+$EyJTJ2a0qbj?1)Rbv-*^5{XKdRoBw`eXO(}K?;A$JSTIL?pYyHy&f$vcfARj5 zcg1_c8#8y9e`5Z!`L>yh{eJ8xW3R=|$CA-+8h;!8*U_nHSLClFpNqU=?2I&rf6@4r z@ay3dVSngXLZ1qah8lyvAN;}Kv%&hn{}uS2Kxibe+y7tvzu^D4e-!78`}(0#!)o(5 za12EiN(Xk49dsat>V!ZI*id!k&;7T=fm~{|uU&t^&4RsPcBKQDh_HXa3XKzW=_=hd zy6fQ+r$%=k)UUWDGt@a$-B8@Xg3mpwtp2&aRGJ>%qfLADv&FQtv&*n=x~ZH*+j{hA zH<8laivW{OtKgoq^TtLiV!6{(nOW2VvzIiul+%!KPL zIr!h(!xMVQT&34VMuQKTsi(A4fnug>lO1Z1D^k7G(lzQY=Grn->CJ#qU;fX({@(Tc z)gO%yes1|E_1(|w zDbJ;6@~?m6z5j0P(a(4apLzQ{?wnux@SE3;x8y$N__+4M$Mp<7Mc1~&g|OPH@yL%l zdI@?$ad@uQ8p&;K8texzn7hmiwQ$pWitdhUE%?@`;STy+E82&(NjM(*b$=ib5AeSr zg3J368$O^TAiVqt1{1*m{{)aIhXkQeKnrVHulUfS!x#QUdd-KR)-HD$RLb{I^>7B28G=K$N(3<*|J&+G$ODtOXCzk`VsqpMV~b z&yXI98o@9fVJ$Rcdl1k07ahUhocf2Ke&*&U{>nT1p%+E6DeSZl-=caTW`vD^;WNA_ z6OOJ%#AljeziCDc(-$zkK3|RDHFPsz`uskS+3z<@Bc{smqVazG@AC($eY!6f2nQko zxSMJj8O-NB8vNYZJa+)s2Dl;GnhEfgh~`fWTIau@&=HMrvu6&sx@X;w5XZ{Mt>&(iQpo zgpN*F&x8A#dg*e#rn4DSI(?5{#n;t2@#SUtH(35XyO*6(%uddOkr&&nee&~w zd{z;jVRf4asjYj#1IW3P&a9(8d<;u&n0I}l2*&-1^MieY-*%;?L<92Qg1a2 z+b4Z(;n&B+Z(7ROg?u@%ie$ekpN~o*XXJZ7eS}AL;iE}PlI&gJ3ygmpPgC^Q-YX>w zSwr-*UhBleYaXp%2_w{aw_i$Ykx3)z_0k3brdF z-u7z;*o8;MuU;Cnw@K>k({gyR3W4rgF)>U8WF^6!vt+oE)olGDSuu_q03->u6k81Qi8*A~5QhNed&B zRlA=_!Y@bA-8o?xkp(f~6SDC61m4FnD=?QtCkwr>c{(uYZRI_!l&};G#7)M zfeSET^d!EcK+LHm%hHs<#zXKhF5QT{K1=EhT5+L;T5_%mb#BX(TD?irUarCL2W8ix zL@J6nLVP0GC7xDGD%YF~!EMZyvqmKIA%0p@Qk*Q*t5+!k&#G0A@056YmTg!KAC%;` znS51~@Ao9@S)DTQ5ON;pDkn3JneRy&Sz}fo<@Z%h@&j+!3)8yw7mYh)noxk_?;P*jS-dusmWScbY!&R6? zO%0tp63LmzunxCFx?AIzewh8T|CTK}WI_vS3D%_^*R7p?>>Kcs&3fL#g|(xa*3ufS ze>4&cG={wpLXZ{s*XxVmFG#|sP!Jg5NYL=PGrXD;JP>RPhl9KKMf@!81Iw5!n50iP zKM{sN8rE{V@Guap3q0=+=m+DN!Z%P(3^E7JGrXaoAIF9;cC*;*hD`2ggZ>~sC@%Q} z|Cs@=FKBxF!qlxgYUzJ@f4$H$62nB_9}Zz#>v>mqk2r(7Og#aDZ4wR+y&E3IM*;d+>4!-(P9ntZ)3 zCFE+z(AG?rL%GJuJLM_e3!*nKd3_;wV4sI9P|SA2r)fN91hipA^D0-V!gi3o%- z77d)`$UQ-27k*eR+E4h_KSBz{wpvfjx$EjdjKA@z-)h_H+CjPc#oFF!D7`=2@@lH8J;6 z)?2S=ALfX^P=gPQ1LOpF1pCh>%Egl$M0EsMx4--kFDo8m`X_E z>Ldp91IWE1)AIv-@0B_E0S;;{PHP07>YYpV7KOPH-W&YT^s^v!+TdzWbsR;YjBun1+CPtWr^^55+8t=* zZfGr^zz#_l!`2T5Y{OPyonfo1E|gNxK>1_Akw!7`Qk&OWioIQ9dmVp(V>?J33NIb}k_o1!rR?pMq7Y=f8J9o&RQ zzy!CdiZubHr>v&dVn!$K2a=Rk>(mOhliSM@^*fyjadDc+2wQd%z*Jpj7C4vzQZT`l zT7u+JFYIS1k7{P=omeSaaW^3c^zp3p(QYd8!`#IXWbT`d#SKazC^S5oy|FZrMWPmX2*G?5Xj1n#=d!R-;Snk4!-P^C+i_;!x|_5B9&>&8ce zgYeZuizU)V8W&17w3*?wRmXBnDDDHBC8JM-@Gkm_e7zOOJP6~QvhOmk1pErXzZ~I; z6JrntI>a%v+cYHhFO*EP9gI|^rsdJ%EuTfPg?6{Wv8(uyLzX;M`12n@xZPZFN~ytz z;RW$u?ZmK5L&L3X66)4#JHx)=b{<-}apc8lBXs5cCtQqSj2%Sgaf-8tUy@<&(JLmW zl2lC5k9$y{pi17=)l>4TrypK-i%V#pM8>Ib<&+H8TbiY-J6$&9EVc(Y#*6g8;{=m7 zu(NXav81gC0g^nw0DG~70NEnhM)N5k%1Wr|+T9>0Zf2$RIYrh=v_u2dy<{eJjD{#s zX3i)_2<5GN(GBcnNew~Q+uY^rN zSRFV{c62$H;xNT<#ctgcQ{`@yBHf@aY;t8ovyriTFua`6Lon{+?!}#D%=$_bSyFXk z*oUvr7cP7`qW6oJ#lslD(zg3Wi2`5$L>czbs##}(a0MtZWwDVp6Jz6gi-8tZJKLDZ|o>;1Qh4qbM zU=4(czs>dlrSsC_3hJCaQa0t!m&*^C^>ATmEqk7mDGM1Qg3~t7KeddwhYC3R#JNl7 zOO~1Sl7Rx-F|yLfOrqH+pmX|3ZLy>?Bm7l!*ON~Voj637d;B|ch-;)101aLZ_Em=R z=CvZFvlt8GZ=P(VBwcs%H0*-*y)36h>{;wtP2s@VFI;C^XJ?XS#Ioh9h!KFa&=L+w zcF_^hO0@HBT7ui~Htages*MX$^wB*52H+gr!yy)x)tuAQY1q1U^}8ivA~H2@6#yTH z5wIce$}^EZhe|p=fXHjOW~kz6xC@GEEil8eVBl)zW(oKnYspivq_cSwWsKr>r@KFS z4!6uUPk>p9ReT&?HRXw%ONdfUXD`O++$p)tx~`pkKQK@xtoaC%RIYDt7KE?dsfals zfFuVlhSH-7^_TD)c1pYs?Syo429z-3Pj#HyI^x#=HVV`9N2-v$y9eyJLnLUgvmLPRg@ z#;V&@u~(x1DcTzO!SMeKUk-g=@Na_W0zc;e3xC@8aqn+>yUdRpe`8$IKd(RHIS176 zx~kj6=o~bx04CyA@aXh*SjzOskT1})MNq6Z9lzg2ZK;Bv9%}*Cz^p& zcb5a~9AC>@-}M`N@^Agep75LBRli@p7%U+_^mcnwJ*w{pLI-m657;QFH`c=W+3la( zoBtovw}U&Ji#1oVkG^Vqg%IHzEO<5l&C`FqGynTv{;TZ|o3{2Ve^n!O_IIXxdIozP zz~-v85HWD~k7asb4WeTBgwacNg^rbga7%hn2yuZl{&;wZi)gd-Xl} zHh9P7q>dO=2h$!!-YM1yR9qn_0Wz$blsa` zVTi=nmm27ChM{-O%-{aymc0TvylsABqGM?uxX5sNmLMkUiU!)ce~U!LS^$xp9spvy z&60c9jQm%lyVMZHakO8)1<#;$g_99BzAKiAV|i~^PoD$d-M6Oy5LABcP1!qHTwmLw z)$s5NY}-6hu?9d!^z}mJWVbrC=E=W3@w2V@PyNi4Sw92Z2&_j}?TbU@qsS^YOHnKz zD`{$=tKaFt{xwYk1mxdZ@dpwaoQ&=OU21L}SvGlDEH%}c>H!qA!*qMssuZm`SoMtR z2%miWCPeuZdp$5@)>VG*%(WEsMNq=^IFn+>{apUSlpWI`7>EDZRrrrxb^ON^@^!U1 zmX*IyFxdS^QvIF1eO-OsPJu`7zn0Im|I}VNgRy-T_dlp;erqKXs8>Gn97+|Qh=Oq@n@?2# z@y`5K32y()Uqck3bdaZSu&dXheZ&0^*nt_|`P?>dr04_($y*qDb5!3SFLjN>)0zDH z@9eb0Go%sbx(9&+oVgji|Edad06`w`i<_KVPH@`!T~-1_V;5E;M=T$_|4P33=Yn>C zgL*-PSLbfqiS8<#=`-AS>}&Z0PD!5o_ww(rwYR9tS-?v}0E@!g_g~QWnR4?gfBv6;vi>Z{ z?c8@QLEZLLMXG$K@bL+#oi!D!s>en=D_(RhhfU}g?B4YVXZ>yYO0lZ?+uS=>cC0FZ znRUp~)J7)YW^R!}2-`BzLhux~@$_j2z!K#P0*1*j@S6X(8qI1O>#G>fs_;IdST+3b zh+=hVsB#o5DAnkT3rFb{s4u7FPLtblbuAW119YCoH8m*Ho<2W%5`j?VLH_NpEY)DE zi(6)P+%_zG?y&6TJ@Tq*!K zW_^Qj|80C}ftHHtaljZT>f&bTG_ek#D#vYHyc4+FvTg!C#;vv(LA_(VQni4PDNDl9 zwvR4~X2hF=1_vX8SFpEy8bw2`XP-@rTIHlm4MFKBCp-b@$_k-gVLfNL1-JuO!eC&M zB1?k*oy!22LBjJHbwN`Fp2XD~Wj5i-sxrpkrxkr;pA#3F*Obu3 zA!v%hjiO`g;1AG#ipxf_bp-Gwyh?P*j%jSG9Z;a;6;Xvf>pTVmB_Q}H^i5)HLC{xH zymbf=MLF7{94=P*P^%o+dAdNxacWAbq_MNP<%16-o!l)cSCgxPAcsykm7*Z`dud5j z=V0gUAmdTPw?u0Wt#uVDZyg?08cJ0I<&U~PV*|WVoiq<6&V(Sf0Sy5V+z)Ql3G? zB`t-iT30!;2;toNOGzh`qui=k0EL5M5SR4Qm32%&{!_H1@B*cPvBrk3rxVmW;ERcA zS=uIHFoDRakOn+au{E2}vb#OkM{rb*+ARRZNU`hrj8V1aLd!faWMf&WP%jwh1lAFl z5!wZ>hY9aYF9DNc%myQZ{G3>ZeQKVP&+c)m9oITbFf?827m25swi4xv#efT4-UhL4 zu3@NI7?}k;)JCfV(c0FHAo!19m`g+zd;o31U%&b@HY={o@a`SyR&f}x+>K)GP`d_@ z45mieaA9#3%mxsHke&bn@Z6m%+|K?_L}BGFmVi#SevMbrog2Nln+^RPcNq$WM7mCe zUoW(%ZY8j4f#|3R$y6c9lQ5rf`vr!>Bl{<;ma^4anl99QqSKR*F!9_$ z(_%@<07Y=?$?jrLa35#x24FNwYEe}bbHE;a@yyew)cSX_rZabYz)gSd3Zn|PZqyg>SLlPGkZUd(qz9PJ@ z#Ns7*H3}|OOB;H0tU6 z$Y1Kd^?QT93VQ=^BSU4$g~09QTZ7VzSDs(Gw$Jlv|3SdJ=VXWQ0}alZRC6xumFJdV zPqIZ>e=fx?q0+guZ^OA1-05s1u%gRZYZ1|1?L(=YJNw#g*@Fx5*rwa?RmcTowEv|5 z%4g=53jZ0W&(Qyl)92JCr%$*X9g)BX6i372ebI4VnXrx%6o4mAdsB;~Ozdo|o=`g? zW!I$by<_R((?j`lKYpws*E+!h*VVeIYAeGGBW=SGgoCkTY4Bpk=pEu`aBSI66Nd5!Nv!_BLxwKXxnj z{$aBuSfuQQSj|Ru6sr+{@wR9kH!*Z!!Et-5R9#1MkdM^IZ&o|^C>h5WWz$5UY3X_` z3w3cD2`j-&`6?~r2^vq$gVOnZiayjK%QT!EmYFeCzn6L}*sj z?FQsUu@O9GNYb37wY$!0HnbOG=fG7HJ9%q%?Z#|ru{q{&WwvPPOg@EeBOE^opJWh4 zFF*7He?Cz0K>MIY>p=OkQ?_Ucl9j%{D)6?xAO5UOdf&(Hz+1O^+=}cz_vuW(6(Cg0 zc=3>1Zd~YaV3rEEza#HS)mOAE%;txJBMm@?Ej3HH08PY}eR3Hi1t2frc!`lz!43fu zkq~)sf4#U2Zyq3)J^Pavn)BbY?@C>6Au9?E=5$_t+z?5Oy^)HV=&; z!o^@}X34!Y4<_dr`wDi)OIDmoj?84)6IgT~$NnFiJ}9ncp!x(m-*uXH z0$>tzb1TW`;LiXOFvK!3a@gv#VES3K8ujM24}Y#MXA`NL0C+^PBBbXG8tgz3!Z`x@ zfT~#}6xxAtN`sOppM?(1WM0Xxs8W%V5LCqAM8`nITj270Vz0#b_6X1(e42aZOLAqG zQ)4IRF!tI->fFVs6s%wQyjI(2ga6sEUeL`!5zpW&`7b;euDO$}24ld@-o$2}IMT}nd9*P9s(v!;*jIAa( ztB4goDIcn^SHOc@Xh+pZO;$EDdU84Ms|2Jow7287^Sa;IGW_Gf;qPeg92TzEM))!D^$ z_#rTMD(h+C{i`qP4VTNaxze%}z{334^VZsKTi~`i0=MW6rnM_hg3|;KdNzZ34iL;4%q?I@!lLbr_$}tY2ghY%=cvq*K}kW{3AE#Scv2oyljMpT$B%m?6R( zysRf62H2t(6^w96zi2y0A%afPo_rD<5B3=byMrZ(?k)5xAwJSNvEZnlZch#aPcqy}TQD7aaXHINTfvv7TZnqv|AN(y4xynxcKDhsv3sxQ)X0vrFi zDID|WCkwYGU;xa)`PCT;4gp6%V!;WyrqN4wZURFk6z6ILy&D#urMp>-4zUr(rWaTs zz2FeaO5j%DVXu11nJX}V=oI!*jQocpmsBJ+{~$k|2J6o71T3FAvh3KR*6FHa`s z!9XNV;8?mAVs*rcs?A}7GCH~y9dO_( z$@Yro4pFlAU|@tK74Kwe1q2e!U_=;3*X_|;U$Q*x(KU{eP&ThRJ24xjldD5< zihyr`*D4bw2~0JtNBqg8bmJ5z5s=Kx43t|FD^QwbCjh+(%_>(DwVA=BcbE?2iT)Gf zesQ)E=b@c~@<=ysObw|2uqdqXl!Rq!*5C?MIR7ivp1S-$E;j`7Q=fdb_kTsqu9MD{ z#jM)tex)k#1^p}7>HdOO^w;N;ap*HS>M>p5ObEI7zmy)l$4;yqAOQ0coLN`6JFe-iu8o0yb}hTN}G zL%KW$C)V+4M01^kII}lxczOedQgWhQdMD756?ioTN8u0F&g*;gxq4l5OZYN*Q!3%)q5gnd8V9_a@8vGRtc|FN{r>CP zl~+ehMu8h=>{yVj@YTg<_1gT`|M*5EXKy#DIGjQk&Wz0^FMa7J=DuXXes%{CthhLZ zD*|1q?z9c^JPeRB!Tmo6Pj#vbxcK0f2||hj<(aM$m~O3I>E0e>H~~>Z=bLFvlLc(; zFp!fOgtZ;dVCe8~vThL)7y#j|=hfC-y)AsPsYmW*w!A+p(3xH*4Pn+%E~%n@T|@i?HX8-;r=*Zh%l0YLgzb0CoeBfK(i37o<$= zmmo92kFz$Gy`XG!1%s3smqy9(h!tJQPf0NynweR4_NMuF|L%`#3a{V%h{u0Okn_(k zA|f5uX7+-ICQ^#Wd5BaPA$Ue(bMr%;UvJ9EejocZCFSvo9pfo$3RDK)aB|sQ!0vW= zipw5SK@H9>*lxI3qv28l2fXp+#RE9XIZ;`KL0RDSEP#%=3XkFX9k(uuAEz>Va5TjJ z9=Pg4XDk+Ed0eEENU^YVV>AlQjeq1B$mhEJUQ-E^pSl{=x9{mc(hJjLcW+P1_D;JA z$0884L|Q1ZvpuDM>=A42l*A_azC>AUlKeYoni>kxk3O&O@j<52PMf!GoN4H^e=Lru zhib~e=O4}*(k)=a6Y~v&2~W?3LNl;sY6_2B|6NZY-*oRIk&6@{au}0vB{+!4ID;v% z%p|EWvu%qAn+Q3e)(t0ML*n2{R<3{RMH~oOz}Y5f_u+;Hfh9U8E_v7#-GLH@#3CfVpi+^Dg6#*1k7EI*iXgLd zJ_)B_M@sN2g<^{vt5`FUmGD(X@^6w+5~&a_%m%qLJADshUM%q5VM#M3iQMu!lUF3Z zgbb)V#xiHuPgx;8%7#x<2|M7fFy!5>=?O5a__Ja&fWy{OKKA(kQ5Pd^K$cNa<3LQ` z{^Z)Dc{-)%Z=Y$ZVPqx5BnPOKa0l_y-KTUsj6zx4jSL{#!yYJPSsekf=MAPV#m7UH-yt^pt8tlb|bHiPLU;7$-wI)noVM1o;lL=fx-uQuZYxB-wJ0K5=XxC=ydAUF?k7vex@ zFhf3X5Fj}CBG3yc3aAgnTe!`SUco4dvLP>8KEgQw)oq)$A4op2Aka7n06`ET-MZw1 zn>M=eQZutOc;iTW{!zos3D}0fA^#{bl?d=+Yp?DGwr~!(^iu%+DVJR z#7Mp?0PRnT@9>lvFAg3ZMs(;j) zXIGxI#w2?3S?fH1&Y!V#qDy3UFV<9Rr-j6z5&sj!5&R1RyZ_brf)VXFAu)h>0!Sm% zt1ykCSQZF*($E@=@7n=z7q+K?#2hE;Ny1m{x4JI*`2Em8FzgRl{eF+1y|<1E?oPD= zT@=s>Pyxt0uOV}jpj8mnWs$QErms+@zDvb8=b0YZvkE*&?16h419|c8AQ-iZc2y3WC_a~3V8ei z3%AeD-}OM*0H%gOiH#`?lbnrThu8hxA$M3XD$+cU=U3mAagm?<(L0y@1#0M7)!0S0 z?1R$S5crQ-1AKHzz6x;A@&&=%s|y4@{=H1FOX!$eYvzw3k0%Y#rDo*WMxYMjerOiR zdry%UkXFF_BQDxS>oNB2nw60*Ry{6N2=0iLuy&o6pD|YcvV84TO+%K;)(!H{tA_wj z6Y}_pJM+9R*XoP;9sv>+hGC7sB-UZSPw+tm0jAZ{hq)At#bVX|?FnG1#B3;)L;^S} z9yXUSK-L^fe*Q5`G`wr~r296|O zBXji*mT5lGcG3gB9*S&>Zr|>Y5t=2p7^yLjB?#$d#KPX2HGZZ~FS0*++y1BfnJ5;p z!gW4=Ywg()8>}m-mMu%NHOAGm>mEPD-y*97*v~72VleIDWRo;B*ci%%1GR~U6w6Nf zGyeTSHq^Khd4f#Z81Q)ErGIl75N*vU?3}KR1Njk6>keDK5X--;2d1%#VY@t+Ei!7G z;TQb|)<0{_i)3M4hgw*H!qlWWZXv<;smU3hJ6Sx(lkK_*-OMgre_h~1@EZK2;i0{v=LZ|t+hsE z-eH(HAdIg-F6QuaMGvA2Hp;guU^Qs!^V4(I{STt<)q`Fi+$eaNpAVv+o;C1(QHL!5lne9Hm?KPM~kyXh3OjrlvHNJzmr*_14 z?bAKe69UM?x1%C5qWlDCDUw)TtEZN9m}tUyzT8nOJq5(m^f>YSW?9K`6M&xt-4fYx zh`@gQMcA#A)@hFCP%Xi=tV_BN_IT-@;4W=%&<)tcK)*gDx@P#$9r{!j3p=c9OY#ed zQQAK15}C%^*mzjOoc6waAdyHmC99)&_jJQGg^OyBgw8Rz|0>>itrZHS+;Qu)x3ryU zpNZ>yS=Cl)`Jm~Up95u(dUb~a8`21#x!?3ECp5g{jJ^KYKCcFH*5e(PY>6j^E+E?z z$6Nf`icnJ)l4c@-8DN6UOl}5TAlPugiL}R*5QV;8e4H`8Du%HVf-w`3zHmNJj%6SZ z$7A)l$3KCGpkM~GgoM9n_-=uk*!qL{(XvQ2fKENx33p^Vy*ggXPx9Y!pUeR^Eoyi@ z;AwZ%dUUUfO{d1~GGk>bQ>1B5oZT&1LkCZsK&8odDJ`ey!+USjKSJ$4ho`KsOMWW|3WZ5d^*%_X`c9 zx(~L*$wp$?wQ;BlJ8SD6M?ZUFEF)hsjV$?4M*oM?QR(zRKY zeVZqMm})EYxXMs6)_{^$LWi{{2)4PTYZ)b@tY-{!3TNz+HiRh>qrDE;BQUgVI+u7de<;$H&yl5sjHcXbT$!)A#Vtp44g{U6qk!#@OZ8m;X_bkq1c5>T84B%&Eof=}V zo*+1)xC8=4p)@sAps|OE6IUGP( zHn51HB+{ZjZW>^Q#hm)t6E{3_vRVQTl3hD-R!00$cG%YqIZ$mKm#v%?@EUXrgwH3E zo%DGd>?I#+=`!>ld#QgclEC5nR;5=vyx!|MM3Y3tvd^&6-hd10W3Mi!y~QO6n{eyp zP^bpyjz}mF@%mXXa&rozndfzrzOHhh@HJT@p+t2slmI+l+&YNE3I0arLN$rlIphys zjT}v^9*NcD>JyEjXgpRM3Rg#KBZ=C^+C)4ZjW#7Bwf%L`>c;9|ye3u?tFNw!M#I>K zH&iELv1q(OKBK|-wz}%wkzla8F%}8dSBI*Tb&*J{Hd+^oCE|%hBvNy}J`s)8#A{<8 zh$2rUULR|SMh`}tx5sNx$>+7yC$!7HL;JDBs#`WS54dHMu6WBPUHO(x+PP(uCf*w( zq^R{Rgtj)2{5 zc(=2cs!Vm|0rM6?>J-u*Zh7?JmdE<{z=i`B56#A|2ftlEAj{S#E-9>HSupDtOLLor z{!2mVKfDOB@Y*es*!A*c5y)KaeH~-di>gMnyR=H-og936aFJ7|1~LE-)SqZ447vHYFs+-3eH;9r(Q7 z_H+kHZjYbKA#!EVc4#Geoiq+;6iER1B*)J?nFi}SX-Z@aEUm&CQj!*AbThEGW9k!yl~J;IhVmr)|&m&C`IdF>ll*Jz(u21}QK`1pg?D zOu4Sg-2}V4xi&9baeIk}G(-D2v`@A^)gg1T^gWF!IMTY~k^_s#TqsRcR>+Ah3MpYp zj7u3y%9XKu;u^PZxsr9Q)qbCoy4nz)9lmYr=cz0cSUvzZ3Hvi|eU{y@BhP?q7>Ua% zPL&4S56FmhlOAb7Q%v+ZxF)!(S5mG|sgl4OgY8}29rIYeCZHIhj%Ysr?thz94tDD= z;-o8F#7SXc?eFiebP*?Aa!1$m!_Vn$IbAFWMywf%7i`#GN$j5S;83&rBy`f;@~uvF zvw2scL3GJe1v^u?28`vE# z+=3>L+O>M!2OSI4XXpc!R~?2y`=(O!fdHbbIEojdzP&>AU^BLe)@iB_&srh=(_C9m zEv0p{_V7OZ&T0E<_p&7t_hkGedr}kb1DLs%?m5d6!qutaSR=EJoU3LJQ&H+Y~)Dx*?vg+OK z^?PFbqSR;k5Bh@JgM0VyHBe+IS`*WfCQ_KO(Dp~X-tDGY4ed3K6}Be5!_XJ9cd?;I zm3{1qd>ko2Hu&o?oIeTE4HJa6Yg-GA4J|DR9v*w1;%UZ;`8-rlaj0JwJ&K7W*1=GH z7_pH8>1(>d818BkOz7lO3G3016FjTMQI(}MKqpHzAy|q!vK^Q?IPc0V8ipl{jK>*u zjM~AqG{$B$X{Mkk$S*nPmE{r=Xh2W#D(Hx?QJ-;I5IS{%&FAo@)0V(}#QFGnpx9N~qsk zGIUYrQS-i&oN^JN6tX;|595ihV?H!{Pr>*RLN~qj3`C@v%LWED9FMkM<}}MSiU}Y> zF0b?OIBe;h_5P=$oVbrOO`9cx&1&MnHS@99`u6dgSY0F{(+6Al+hjor_ID4nTD6S^ z)LWv2z9M01*zOB#PkItDxG_CQRBc`&4B;+Gy+2T1;RjfrvOE4squF4=xjxqM z0b$a1eywI%wFmiCbY>#*&xuSAvV_4G#6TuOJk%VH#wfFQ_offhLgBOGv~|DrDs)~b zU{UwmFn=IihaUpi2ntn61%!mdRUv3{p#RqrYGAlHOO&Jon9~q#yrZU6Hr6X%L)kiL zidmHqS1^d9POJ4rE*I8okXYkOjx?&)jm69gelg}+-0-TP_euh8H@%CC^whB}NqtaI zVw6NeQj2*|F`EbSP!@zX5=uTg;;8TuD?~0G=k&Xx495wQ>j^GT{;t+wZFLtzF)ZjN zo$hbiN-!)qaKW@SWUacF7apd^(f>p2ME!P(WeA%c$Qk2aMzMbbXW$16oofgJJ%Gi; z7IKpVyUe~V%FxBZqBxr@p-iQ1pYzjLp}voJyzs5Vr3!mWq@i_0%RrnihKZWfeemDH zLgh@#&LEePJtXQ5JpjK=$YMCwDdpzD0Hr!-!Hma$Cj&fIxC$$}#+&hUz~jA#Nx6is za8)_v(O=0x%g^t3bc45JY)y2J0Y4+kKd}PH5^@+3?_}pi9<&D7v(-KZ(`u`cpp3Kv zZu212Gh{m&%j&K}a=={?g;J4x+3?+j^DLlYl@@cJ3tqcH#pX2a$zPtu?*?+sF$-Z} zFfVfqp26DcsU?0*mR&!`yTk9N^Db{Fq4i9m2TUk*X(VA)9e&R;29p&WZG(J0QyV<7 z-Dl$F5_>4!F?3@RXaGub-_Z4&GoX2!vRVySqH zYdX7gh^583<(UBg9YAR>m@=w-ei%wvaB(;kibF!JTsA0HS94H14^G#o)Y`&{FW5pu8Lux6{y}=(8V%qhbx&Sqp*YJLXO7 zI)qq>_>P57%!5xL!#2_?CNUJR)JcS;9h|af_>tfS*n4$%2i8xF|4zORw=q23EB+It z*mR#Lkn5Icxd{#W{_09l15;W^jz>`6@ zO>bCxu}1OYV-k2#JG9uCVUV401(0aEbf zMH#-!)b4UxUBLGi$=t>2JD=rPr8!+6(@k8-Spu;|p0v<3MVbB@lC54gy*VKNz%f*v zw~+oYI97OEc+@atPs&!oHo`g2aolH?>=e`d0LDa0o=L5eIGcss@YY&Z#Zn2aFCr< zmQS|vkP(>5syhit#d)*G@KK1sQ(n!5j%|1tt0Soqw&aUXShCs-?g2g+DIrC3x}dm^(PXs zL@*kQC913Ak%maTwy7>!8?VkGT4ACgx-D8;9f^fwp+sbRL&7=}sSbtX)y)WM6ssSK zMH1n73;vHHqEE0s7LHc$jYaDkcER=#i-hazLXluJ0z*S6)C9LG*eT-E@mO87;dD(T zyrVj_vnkvXi&jTr067#tSeK}7LVTX8D)A`%p}<>uGN9RRg#WV8oqR#>H52IbGlfZf z@6x&p!+-Rw{@9~hk9D7f`vBur{%Di-9ZUqSNOxQRB1>Xy_jr2K_ILQ53|K$94~h6@ zps`Ru8Og+t)^ZC&`r*G19ng*z{w?abs09nZjQ8nW2UExSUJOYuHFFq-_#r3i<9svZ zejMVr)5Q--=YB|H$tE8!GTkN4kzUy?T=dh*6>HbE)kb{Lb;Li+>4^FVze7ZbLaZo$ zL0Dkylh(!1#jDc4NM@=O_$>Xa65)v|OQlhzt<#p zZd!baOWV*qSb$X`RVqGBbOQw-1A?^jrPnNJ8Xn;z z;t&4~@-v5ju(v~d>?aIG?8pB;NypH{lFrQ~N#(<5Xx5W%6_VYDSjH@xm4u84{$*j# zpP*ryKKb8|bUqa9GjfLCi*6hX@H z3jxl8QTWjMeLfS`Lk6h!2O@Y7_WBVPD^x-V-5Wwxs)KA>$jGsH#4JM_;0G(ORDan5 z(#Y^K1F6Ao;IHaYNXWt$e1#dr28K-~V8<)?{H{N!Im-82I77@xs765<`wqW@9+ zU=n!oqG!5xgGI&6fG>i$Y+-a7QQAN({y-+i(!)c9dBu~k=?j?*;)ZZ;}6Es&2wIn|Z#{*22S^r$<|0`r z5DjUsFdy8EL;hUYAMr;~PXMm7bVFt_elLCn@FEn4YjVKLHZ$UxdI=l(81vU5jHwCF zRdi0?qt)SrzYf*0&G3{)4g@BYKX(7>z%Ga|NH(E^bTAUmfx;oQHw^v(At1}^>+u`$ zOwrPahE+<_eV{VpqjEUmkc~QpE@&M_1Y}|3K^YJQ|4UCmB-KSQiA*fc2eJ=lL@oc9bMOQ}%$o^eze z*4+8m$-#KxUL6_%yt7l}>_jToxps{QXy*@tljA#NVAOrYS8z~K;wb@nsLh~-Ap=tn ze)<9KNGHEjvG5j-9>A|N{I0qG$Gz~yK~fDvd>2q+3ZHiE$@TsY}f zfT)BhUW1}X^P>sK8UX(@#37j*MbTwGz|0}!iQ*Sx&IkFY3E~VBk&}>I3O)!&Ya}dr zXxyrS1F>e-={{jK29ynigKQ_>L1` z1c*x3j(ZD1FRnB6P>`T2kTY_*0izUGj`(P87((Yo97c?4!-v0E3!&^_}w>D*z|4dQtkx2-0dh5YRcFIVds2lSJ1M+%q1> z;9wy@GZ5D~66lNtLy#SJ4;|4S;m+_$9LBK?P4K|B($ZGYzWOXI zSfYKx@}X(>c=DU)9&h;u$+yIhY1yfZ)A=p#KCSu&K3Q!cp~tLUa<09}lrxgDnu%Vm zmB&)bYdkYvW~tA;%49F_V}u`1akH6wieJUB^fa@chGQ@O$-v_u&tH@>!zv4kP{-)! z`1>Lokh4ar`D2tHFY)7~G_v^?-&&?MC=TUG^ z9d#JDkMYp=q?q648MkzGFN4nif0VrmbX@6m9>}*)6U#H>SrRXj zEIAXOnb;ZooH$P6`M&#J0R<9lx7kwRz5o6Da{v3^|K9IzoMX`~JZWYPzCY$WMAxtb zSz#=VZlLom_zq9x@HES(yKvx)sFx)vO+qB9d4v3a{xKrd(dF|-R+xWc>s8uisVupkLb)+dL6}GtvY*FIl6jR*m z;Q_6{NtA-z+T}t*@U~fdeL^arGHh7}#BVNgI^5ye_O7`LAF}pkqs)rSY|0hJp5xD5 zSUxBh%tIg@*x~r=c8goy8S@ao+quhxyP2q9+HnToW=S^(u;1cEerEV|PI{nyR_YOQ zCdNL6HwX_ZWGH#{c$$Ls5yrnlQE>h(JY8qlLm5Jj5L8Angg>U`SPF)EA#Ewv`48P3?nm0ZVmB7R-?5|{tm$b#{7pROCU}%TNXwlM z>y?-Ll*9bq*^I#3a!GcCQjUj>3~d3!sF~v*@ycAPhfZg?5Bq$P z+`V|n7sop|$FO~TZP>L7|Fit}6s;!Pgd=SCE_Vn_%6n$MjXCc3bU}3$w-1ojZOj(oeEDphDiHVs=}f zJ9bO^zpccNepzj`&Of{jJcciQ|5fcz6xI5N-*a2T0F|Oj|j#Ip1n1N)>E(3QHc=wvS0=pGIAFKN%u5lwAE2J~pA^MaW*-<)c z?I`UrNZpVoD-rmFhlmtvblOpmwc3B%EA1r5_Ep>8+nua%o5pm`TUX(uof-0H3ksQa z4m#x~o$&K^vXgC2rcR;fIttlH>UOq+rQp(rxxpe0e=2+`|7b?xtH)B_zN7W5f2IDr z@%6Eq@0PBAkp6jH(Imk7qc40}4Xc`A%^ts{RSa`Zw4cRTrXmz?Uw^=rafhk$b#1d+CFG`LAv(|9Dy1Z+$=VsZvf@Km7ynl7bQa8;ocVMzrE*&TEZX z(ok@9m@5hK5$~4U)5kEKyPbNkXTnf7t<%0F!p+(JE8gS%yBVfW% zVNtS?#^ZIv0Mf(4teKZhtXZd&^!LvzUpt_{q7s|xXLyfS$Bw(&!yjJIbWp5U!zCW3 z?6I*WNoj7msZv(n=GJjfId5)U#mi9@MoIIT*(WIOBqdmHYldiRnfWEOD)(Gf=O!E> zR)eZ7q_HCJ;e%PHspF_ErKs0L_AigPpwTSl1cs-o59bIaa*T1087c_N#$7%icPmys zB6K%V6b23wW!_~I(i8Xz^Qv_UQSppBaqB8#?#ZU`Rz1F(!q2cvg#!ME zP0CBEVw~a~NwW)AZV=cCS*$l41@;dsZQ0=f`>L}97Bh0IlIP6mJo&lmwsKUJiOFQ?M<7B8pRuBxL)f+Dk|T5$WuzUF9Zg3FUVxRn{ToQ&)|fagja-I;*)?GBCquNpG{HEQJ5aI4@W0rJ4>)7fft+f=`7A8@!>2 zWk-h*vZBeYWqyGj^PCJz?qZ|_X5XQ5Z{?k-a!7+KOL6Olo#rV%hWClF0?x}5;sn&p zUnz-!5J9>Kcm(ru&22>Ry%Ab==`#ac~XI;Nk@>WI4EVBS5~Hzlyi3avjhQ zo(c+N8P2<$2zRe?!_OV!D89=XXO6qcYUb03*crNC0;^VeHkC5B+5=uhIEpa$!!V?_ zU_aC3dd_1%AAo@^$wsrArnbyr!taL}k)sX^7g_dBjwl&Nt${T&4;ltk$I~D)vwYoS z=ybB{17kK1)9PQfRmJ zW9Xy95#h!86FbDL?o?U7i}3c8nue;=FiV126&*gC8^V_zBO`B~Em4<1ow7($ch=2y zbkg$vFev}5PGxszitW>VOADJ|EH+a!=W@ZXAJB!&JX!rivKV+KdIYOI7*}HA2vOam zX_M(yC!;PM3M_9aztMp;-yE+B*RT#%N$V(z?9WmuYOFKNb&@0lAItJOu0v?Zkb=h; z+0jZ9cDeF`AJI~YZN6?j317eU`e~lB+p`fPnjO;_1~5N4?>MP$=qj#>W%X5P>J&~k zkJzX~p@a1bYm@2fkP8>}gZ1Tl0x5Dwu4?Q8Xq`a4T~;b3%VPb^R#^q#^& zG=P&tJP_DZiI~xd-*?m>!Ho`#G@`pB;ZP7l-Tr_-isMLmAQTM5{pmPlMDZwYVQ@X; z4F$~Qpzn+KzNw}T{OtGOUo#lhvR%7EwVtlI^b{}OP-|YSJQRvA2i*qUjWq{F8f-=T z@#&!7`e6)5LyL==in#aA-$Up-E}4X&%tAm;840;SZFX7z10s)FlPAG`_&U(^y}QGR z|CaT?j$G0XST7L1TM1b|Fne38{+aA04ff3V+`*&5g>m*2B)0^xGV|>Sdg`IBmTWTJ zrho~gR0N;r6ze7P(aWp*UhXBmE*D&r&>DH;3i3I7%bq8i_JHP@H()fV7|P3bmlG3lz2?X28Tp{coXg9<^AXL6&(SwslrJ-KNz=JDmBZY-~^EIc+h=9r}q zx&d-5xPYv36A*v!h≪Y3Ghtt?LsDvvcOg6kb+zZw6{a^eW4vgd7oW=o;ptnLmT? zP>orbg!vz}J@RLm{{U&3XKFTV;^w^|q4bQnUswmo&X1}gOlLDhEXN&`G-Fi#8q%~#H zV}-3WrDMNd7{}`rYwE%c0q}v$5BH!4Sq(Q#!Jz(S<}dIq$tlqxC%dbLYXPc>tOrQB zlACwAu)zx%et<~*t`P84r?8D}osSp~W^*N3;7G$Xi%ChAbE5(29eF+p{=&)ftx!qS zA@JKs^DMHz;WlP$jn73^`?N<4cJuc!nr2&Wz_Yz`| zddbJ-FR?0Px(47?=TMf=OIB%pBFrrb;(osZ!aRznM}BOm8#2_@*8Wqsw0$LD<2Rlw z=9o2$*IuQ<`ZD^u?>?vTBHw8Zx3BfcLXgxe}{$?e*vd64#W*I|n7gR$hGDv%l?|#Dt-iO+v!k4PB zrk@u+lbpdE<_+Q;%(`_t<*<416`ZG?S+;NH3bH3Lk%q$3#JtJ`ZPq_Q zwlyMl3mG6C^ONkbL;Q9Oid`^s6n%?f1{{JuG3J&$AN7bVLY|N4s`cB*rq;T8`j+;# z;<5fc-r9^_l)P+x8DZ@aD1|A(2oy)aPLrTzt$%~?L^h6$Pd_0YY?Q9{#;B@*%R!vJ zmZd8Av_Q?E4bt}!U7djE4T|Ni+Gh{Dx1i`w9j#f4TV*#fTO)&r^h~6y0dB*QAluN$ zT?+L0vx7mLcM{D*u0cih5ICl<%YPMrngaohD2nPdr4BR9bt7rp=Y! zu=b4J(x5y^p_fq2EQXYq2K=Zb-~OZb%|eS-Qi z;GZ{6Abx!v6tHlZ{pq0c(E+GHV5A^8)f5%~K^XnXAvPca*%rX)4`MQkroU_E*h4@k&98;iESdk!a8A<$jVMZiH4Z9 z_Cfrbs*YotOEY_|A3`nsS@#4iIAASg=FcPk0Jr4?exs=rsmsDwzj!zwTZJ;E467=#$o) zQ3f4k6NX6;!qa?5V!kCKnn+R*T#Ar-3zmK6URNFRP zJ#up4C+-Q7_3q0Y=%cuVRQe`L4XJm?4T84sQe%vp$TiM$zoA=q&hW?!8ixrg)HB}7 ztk1A3(_|x|j!LTvjLHGLtufzm<}h>uKQq=3BR!6L5nq+x7wYtfp+OX=I8_#CFS}ZH zz+V+gfaQ&bqNTVIjY8Ea2>ER|Tp12kM*aTkaIiM)4@A7a4s&;;(i`@-#N!pvO$x*y z)5SF^?(cDV>92syw=^8Vm0QRR1$KJ}coEdr-R=+U4lM^G!DyR55UvTD*GqlSa;oV8Z%Kn8O17>)OGs9KseqRV5&T=64h;e=;6D4cZEJE&bai8J{ z+~?CYr$*ofA8*JkY2hO`Gvyg4Nrv*gQIF{S$z6mp!EYxeE_itGQXqIu2pS_vZXQ8& z^AxThaTYi@svFot?TJZ#yb;?2HfZj_hj?1R$_BynU`k!-c9)Qz-Ln1@I;uWv0DTvf zabu3z0h>dIigJMuJP#=k08PPJ%0)p0>?|TBfVU!Qg?ZT(AY%YnAa$iTxX<6yHJHTN zyul6j*ar6zGjh--7I~7@j1IOA)Y<&7x!vi`Uc*gq6+nM9^TH6xv80?B4&cO*=7Qn2 z&Yr!cor^%>oNlDT83{>Aj3YS1ol``E zW;H3PunA+j;i6N3~ikW(zkNIZs4Fhz%_*kvf7wL%Yk%sAG@E+L%L5#@qR z0jzJ>%a|WFI4x^8JYsP}7Y8<7uEse7$13PQ17g%3(ltZ1PPr~=&E5~|kPaEUI;}Yb z9P^&AOp{A^9gl2ODi_S7 z7=G>=QGAOGh2sP5F7MMdT8YwWsB`6YSU{~HD?^=*cp!c?D>L3x1|EjYTHJ6Thcq`p z+&AMfAkB@lx#l|}+&D*BYc3LqO5tbSZdiTVJ@tsq>;eX$4ONtXg!FUR$2Pms>~*_= zwLq(Jh^3I_OQ9&aaknNsC%f7NmLBr&^_I|aFTMELr&M!~Hw@@aBrbBR2&o;)9A0Vl z`L-lp=+bd!k#u`$1zRXjPLx-H$i*3HA7~jX=-)ceM%_N=lx9bmMTD1nFaTOCcK=y1 zcsKL&2nU_;z{Cf$MDm(Jruy^kuIBeb;i@t`>8}r5GZ9m?dPx^h}x|A+J zeuVsG9U)&J8VN_SMnn?hvO3N|){>n4VaMc?Z(S9Ii>9*bQw?TxZ&_ zW;|PcW{sm3?IQySeyFLG!o0_iuzZ1C8@h}$yW@h6j<$ikag?AC=cLQ?iXaj2pVk+U zSE^%6pop}`18#^Q)5wWTRqnCNwX!~(+4Nff0!ez#xVZ>$IS&mNJY0Y>j=Av+ z-(QfQSk?_79kFw`Ej`h-NhIIkB5vsJ+H)oZc=YF#v;n3j1JO{ZawI|tz zq}c=CLU0N27}jhXD-41XFAiWf|5>WTz+oQr60}#u5($I$7TB-R_o^o*6yl)9WCtMu zH8*Ba$}CQ%I7^a*Ov^!${T?%WDGq~7Hh&sT^Hq1mC#;L8StDd)cA@5aIHu+;)UPR&buh1_pf}dt!Kb455c{(@sv~VW5Ymi z^Vocs^@OYlJWJvF7aX?Qa^)+6}v3FR|IZX%DHJZeAP-dOIfb*~tw7edO5GS~m-6VdT zBk|Imn>KQMyKf-*9Y7L6JpgR)IcA1kZi`h5G?VhT2v>2COQf5bvp0~57?SBE1`lm=#N`PZ*Q($IIJfT^xQOKZ9b|zcmWAYHS;lD=bJz_LLF~h2 z5}?*ZZ{R*6zFfow5;{*vK-5qH{AEA)=`I_e9DCevB16vFauI{>W8qy*+&{o?A&)b0 z{#MnC>PQkwg?MXjlhHcgK$fwQn|vcrb&axW19c_ZbL<#KD1bD~HUqpDP^?zVc>as4lHsRXH&m+)nR1_da)@H%m z0WPTE57?H!y$tB3Ay`&~BF*n6!l7s=6b_a_UB~Z_miZ#(W#Le`yaK8r!C*r;8cST* z7pMq@N)ajUZ}IIb^Iwmjj|PL~v1oN^JnAnkFMSY>w3Ho%a2^_Rp!}rjJVeuibn@fs??0Y6=8< zy}@cfjxYD>V}VFnBpe9+Yz80K9x^N0PUfl(ZDH~&F`SrGPlyjGGR5LC@TnHsx zaXAX2ig5F|;aPChMljQFa7=HAnpEzFat4f=FCyEO*N^SU7l!7X*B^!gt0(4*;%wyc z1-(imXjtXtw$@lI)>ISN>+^*bY<1NUPt+5tgpz7$q}uC=F`LeKg-4WNl~!CiGYHCr zo@3R+-iopqG$%T7QrQ=YhP{DE*c%Dg;TFYP84W|Xlis4}n8l`o9Wd!ylY6LR80e6! zqjpdhp^K9UdZ^0{xri$d1-aSxgQwP(msd^ec-JkhB}w6sh3$_A4-h7-%{|IXvWC~N z4Jt3lq@EJNtyx~{ww@tPmx1^%usKrD-OFM)n@^9$4)Eg4}9BV27=$)GcjNX|}FDLZf7J6=0skS~u&o%aP>+5ITN8+T4OVW%e zrvlh#1RSbjp}RzC)I*c2+=+%OHORQ%T0kwtm+hfrgXxl`GO1hqQRKl3EMJ*TZ} zh}i|@nEw|s_Z%E$UQKed#strf+~s65LLhZK!6J1%?tfrji}vvh1ySq@uwN*%B<;I@xzJC5juy+DAra(JoFFbCz0bA&Z9vErA=AvOX7u!v~zY8V$ zX}D~rt_sgvW(=An-$mVrvfhW&0K1!1ZYrlZSjIk{nVz|{#aZ4Q|JpI-<#Pmgl*?gue+nNXJWdX|tW!O= zwDV2IeUJw9&^ZK-3wI-%$zDk7!JTp4UADf6mNty-@f6ox zD3Tl}7&Y6?2T-drbTGsLZ-@6HWP;u^ULLb33G}(*75IaH!nNq5rPQXyZtU|O z_tqX5#$W$MQINlUFyf2cVuraPNGH08((Sz-8t!mSnx%0Otcgf0*8!GYc@lS3x%_6r zRqFC-Z31tRbF1hRb0tc{VE3&f?bT4fSJDIZ!J54taYJ-g<~6jUQKj<9Bld6=fo;q~ z5b@%mZyP}3D^zH&;%jb~N)_5P9`C`b5Sd>a2G%~*T6iYUt*B%P-$8~qc_%W7vl^H> zo)KxfU>^^mnNDJOS%u8S-5;IV?`z{8;|^w3K<&6o_g7qOoe=n+JqfcXe1hVG+=796 zyMdhSifk;=4?-8JsUQV)7jo-b~7wJtnyw+{k1mbm~|9SgNkMi_%CTA z1_{ek>nXyTp$VBoSW}i#wRRDeAMsIWcai1K9+DFkc~=;YKrr6JO6?KNt{W%u3}sjR zHVZ!Z1wRiom!Y}}*_DK&y?DM7WcVWq>9ySxL?q~nB*@5zEBGSm7e2`Z`+HbJw#tjeAGXYY-03my)>X5MOOi`B6aPxzK%}rReaV_L~6+H#^*VTYrV2q0!BG&-lR9zl!nZvNIU=> z)Icx+6Xxq>zMwC6D%2eCM}j`{tZyXd_s7Du(HLxpqW(~z(u?piK&FQMo$)|0(9jr( zL6HVlRlWnhvVae^%%O0^TNjN~Bim329Jy~#AQUwhVo<^Hg?v->fn)muVKa8ugfW#r zQVIywDqx|s_=Dt)&0^NWynT`8b{Wmil$rIq&lS?#JCd-%^KM zP{MKj__OGY8LPkYV^0Qf@c_?uGoFvzbLX_I>x-Yq@zT=&?7Fu5KZ^w^-<#<=XSAVL_0bj+W0~t*&+)r-zB;C9I&EMM785uc#cYbvamj=ss zTk+i6wx0e`qm1B_PH+OjiQWSEDuCyRP&zzeJHwezjBV2@-$Y-Pctj<|E!3oCFz zxQ1Klkifw{w0({Owh;(3i`YGE z$6^lh>HeaUyE@C$i;cyB9$*k0r9(uNF3%JxbrUAOi_O<~r zuPAb2`1q?$1d5_)oY<#LHWYj5W~8jsMSxM9CV(rvD!ozwz!RM>h1$OwgSenh_rjy! zreaI-m5c-_5%IPak>xN8{^8VWVfg;`Q6S_eFpxnUUaM{jV1${c3(3~hw?6lU-nQf> zn(GcxF_>8bs@iHVuQn@%u1(L2fOr#0ZEKWL=vM$QBUg9>2Dekh2qjuioE%P$UQd!) zfQ&_u9-VoLex8|Mh2+IamVG_lPRTF`+mgMWYIJm`bQqfA*>UXEHg;zL)>;&!FvMFE zbo*@U#zK2z^w;KQchSOwTzaRek#$xmMr{dPJj4WoUF?jAERk1gfI-_S=Ie!H_@+d@ z_gbS1OCkwh4m&UNZbIeSbCt4-*J|#dZnE;I`4*9~CH`39+vt;Ezyic8Bey`?05qlj zg3JmmaN=^4vCcRszNA0S9m4j-BrvUXYAHe^fSAl~%T%gGtW99(5>0<;0md~#&BV1` z5pC?rcG?64qw^ZLr=1N^SfNV~|C#jHvO_u2RdC?IeR{_Tn7nX4hnu4vQfE6cML~A9 zu+(-afs~^a4uac~oDj+TxD3P*ey50-p36kKLs>}yM???4*5*!V$Y*Z}=@wpE$5>du=a# z#X)%g{w{!n_ow=-Z`9w`%1^(tp%%fIYQ~S8F!Rr3C;rLvf9p>C=RX?Xvp)78HTMqN zF^-X+yd9%+PjfQab8*`Y2Ual$d1)Lo9Gj<5&7x_R;#Mxm<($&?z-;@B?oGp0+zcGd z?i|7C+0A`-9FFu7*sq|oG`j_;Ok^(Do^9*;6fub<^Ec&9I`7~kW?8(wW{}ku50N4m zu_LdQg|uTFtb{a9#B!~*b1qm40*mkfYq+?h&Dz?lQwh}-w)QjgKg63}(~#OuaDuPm*>Zxy6KuhS+hEiApwrg8YXyI<{&Ur4@6(ijUX zc6+b=LNdEUJPfgeU(O!OY^^pMzT81C=ao%zseo*5W0-RT`P9|Hq*z?Y0&N)T)8LN? zeft_AMrN1==aPlx`o`7Tjp0UxoXG+{eRHm1*vax?OUFjb^o609krym@r`lZ2P;G}~ zf18W0oyb==W`XTk18$wMGwrwzyD|Km;{@jqpeY^T>Zp|xhrXqTc_^|g z(SyM+%#@vT?ZN2dnv}-8JJqZQqkN7#7i8FA8s9|SdN9a6NoY8*6>Hg9e7^&7P zZOMX1icgG-;cC77DdS?y==Cf;k;G2$CSu)#VR3p9To5K$?|M2kcJS}IrS5(6mZ};w zu-0(g^_bdO`@q}X^*I+@!$dP?sQ%*T)&@);kIR`7ApP1$Ug%eigN;ciambqoyx;Wt zqyMX})B1eKS%Md4@Ea3=p9Hm_2?f~!pCOsVIrJdQaPmuwM|Sv0Pfw=lkll;_A4hClOs#*$Z z>%!0N)yjN*{rh|SJA1qOd-~VE^j8PUHY08u<5nFJp|_l3ij3j)MP|sj$;b_&bj4NSe2xC!AJhI3%0Hxm+}!I}WFvxR7@JOW*E{ zuRr{Ee;8=PIq&uMaJ&yCj^QfeVd6@LbLmjR3jgU_S{(K`bRv#9yV=3cYG6m(D+oH_ z2`nDY=FKcftqb1AkFCzaK4b=q@I0Iv1KhhKaT&@%aHRxh6VjY(52@#q>0D1dPgdB) zR=%-V>uZ1U9kn9N8lGOAN4{%Cwe5RjGS=3KZ#NbqGM2s7(%w%@Ye%<}US5TUOK~S1 z`oyF%Nr5bpu+!OjIBjP6>vvxKWqF_w(0cYpTVlOy?K`D=KIL$)|ITkH@%0bC-5HY+ zp51YT!4ED0oqXOVVu@q4U|60`j4tB}yCZQ7tT@ghWDEIv1-fN8xB;xx8KF@q{~*Yj zCPk60OF#an)fe;3(rBLCb zA&T$R&+B8~H#2B&9(#*654+c2J1h3WmsH=tK=1lj{?K1GS(wwLQW=t%Own=i2cH2y zG;SK^zWRk9Jv3mplUkVor`p`daC%0MEmMpO!RGt~Oo(TbGjsHBPt!)``Xs%sEFW&O z>(}BWxVv!w?q-6!TM0<%Zlq_e;Xl3r6~SpIHc825Y%s-z>^Y?oJF_f5+@}`CVJ>GM z=w{Q{Uf|{(T`ApZ6Mp0*Qd=xoPX13U!HpJ>Oly0{AHhUH9WVr&(4 zo=A*SVuG1x4=`x2Y)!L?^y((4bz&a-mt>lTFcIg=#N_JA8XGBrAnfU-Nxov!T)vrE zddys4UATz`%l=}mGfy*16BI+EH}H=7fe8U)hC}zf?AdU;KI(KW>3kYnE<0Ad6s-Tz z!=B3Qvc0({dbF+v|bpwe7ucvutaxP zSAS>XG%jEu17T6(@Cfp!rHo|2?y?7W8ji!TC1FIy0il~sEUzx&av(El4>o8^dRF|< zZ}IUVVl^ zo|)nSLHZx!2J~#>PE&UM{pap@mIJiI_%tG)C7@J5+Pg64a4Jyaq|gzXjR_p~FpX9h zok_&mmpE2Dyp$|r8ydqTOtkXj@K{?XD~_SIr~eajcT4fi}SNk1tkZziYhefU0%P#u{fUL8y#2kv6j6+D}!0!teyDxyc*os*lE)x2C1C$HeTY%%I$;goPn87l+ZJ-^L^5%Z)KW+ z$?7DGprsD?OAHFAoVO`Iv?rYBY3LThW6v=*rpxxej(d4Y)NXrQ=fJ^xF2GcLmL!nWjJrC>xnCgCl zs@fkNMp+BC0-HRqzye{beGlCRq|Z+a$!AOStv1aSw|ySqDe%|{uLA6&1;e036>rS` zxp)&lih=K|s)Noo@!AL2dO!?1QTkPV5__CItAW{$IRSw&_1r(oayFdO+-L;-h1&%z z7QA(TL{sdW#J_jGJaQF{$dU(*5kFq6)w1T9o1wU8a~c2-XJPify}Ae0lFY>P+}6ic z%`*iFW45R}9>c-=Y|;A@=!QZvH(`&1AAoo(h4Fu?dvNrbD4Jz!n_jr3@hyxD;D1t< zCe=GN1;(Z*>t|{SEQn_pma~PLs8x9zVsY1wewd5f*zP5(z1sz*|bOJpc3q_y` zpP@?y7Vr+-pHuwobkcjk#kFaPV4#cHl^}V=%_gq-W*3GhT&f2)Nv6V^Kg*FPX*de^J9jm`Z6{Z){a9 zta)%Qg0GVmx+$03BjRUI)?bN%%8K23W}Io7K{_kK zjKLtGutM-TXuz+{v?zt!6rf9YFHXa$kWgP%J_-}t;+n?vtOwFRoY=Oi8rMBIUkXJp zRJ9aiBJSY1v|1ld)3L)RE7sesM{B> zsD^!)+wTo=uWL#4xcd+%3$GdP#0X3r2v#)d0JcKv_9#<72=^M)F>I~cQx=EbA zj|y4|tOBT2*c%JKS9%Ndj&D_(2Xgrp_`7G1{!qt94(IffZ$q=`q|w#gl>(na3r+8& za2&VxqRv1IE&)0{kcZuYu-gYnQZNc&8g6lPvv7J6g8s_PBJBJM`nL9`>Zqztf@m{8 zz~0ftT^h^&7V0@8G@nloRM&kj5Oe`wUx0+*z=-BZsxs9(I}Xzpo+?md#yG7S^R`RA zTdJXzVEEO6GXX>{I%I+yAI4nJN|xZ(8fs2X zKBaD$&n^;nM=DUQxm7>j?!i{MG)Xyu{obpV0C^2nDx^N6A_8mdBmkDQIEj*Jkx)FmSYCvey=-9|{Q#4I z57|OT0p3lz8)cdGFh^LxCc}aOB_o}JC9H;fD-&#G+G(Y(!0hn}oG(csaFtWYd#|dY zW=?p6sxQn;JK5dNqG#qn(id3}WgNPzwcz0FUHQrIxDK3Nb*Rk$y@6Zl9W!*03~}>cL@ebCeMD7S;y@coWbP zE40L?>fix6>{tn>JQ{i#AVrxqr--Ch0!K>YGfR_&1ei*Q52{?4I-OeJaXN#MGm2UZQ;sQP|x)mG+-ofRYfVnY@QvB$u_JpKLDqpDt7IAm7wluv4-IT&i z?a{QwRcA4SBU`}`qrHW%elA$^zWlv zAjbxVJy5E8)_^F5Q^5>_F?%Ngx2%+4H^KqDP#iR!Cuk3Wd5K8qvGO?J=Akr+HwdBcFhY24NvJ_H`}(JDW4)~h;=Ozghc4Wb6zAHE{rA=L#% zDskW@t!vdvaN%TQD13AaGxw>12B`+DTOV%D|A^+LkfhKrlCVPcKyPka5U}tdH<&Ff zv-_$#U6|O7svoBTboaIdJ@!K44C__gPe^78Q=v@Nr?WFcn^5af#kB^u0&p(Uh&CuFIbfRtlTX9Aljq!VJ1dsR0 z9o(z4{=DlZE*fFm0H@eco8E&@am{PX-R{pINPxFYZ1C(&*kPPTjNLlPE)x`BH4pdT@kA}Ssqp@&CmN}BqZ{JACu*!; z`oS^S(7`i_a^2G+5X4VtKRVsOWJfeZw44Ygt1B8H7gq0s{#Mm}#W((K5is5-+R%TD*rUUMO5oQYg0NDF5LLh&s4;sR$w23#9>jt< zAC0=@RDzwrfk?Q-?{^IFRB2jPL4IrI#XRnT*wnp;t)RB?gug1$U5-3Ps}UVOgEjh# z+~5L9nH=4;^)5QRdVn&velCG({_No?XCLR)-gVnx8rV5po`B8?J*`#s z)iscQF?K^qj~$aP^SX^DFu|Ir?6r5;{5DzbuC@|z3tD3g}RFKT5h%Vt zNBMZ%#jb9&n^&z1GC6y!S5r{6Wkxxn8;~LrHR>I{*641W3D(di+otdIsw*NYRn(;| zpo%m*_I?LlI>i?@1w9W;I3R+7dcMVs>aEt^n_8z>FPB+2@w`XTtzSm&~d$aR8E z@m1pIXaLbFUAD~>2V);>(L8DF8+IL5;Q6fwr(isWUHYX3*;FzX>Em4fmLs38>7IfQ;t`>E1l{UO9Kb zx|Hv9yn$n`9nnfH*rWk38h~?$h*cNDf8~Ml^6=wG?0OI;X$=wBtVP5AI+W%O z1ppiU)epXA9K(;n9hR%V-NyV-m* za+1(hrCq_p<;Yi&l6=6+0W>`Em-74uK_Ao4qZP)@td}3HXeHLr~FmAgx z$PJh{fYPj8&|{LYiH8z0Nv!NhCi6BAk$F9)>99Y;S~$fZ>vxbz>0x~qtKCL&sUlYD z1ZEvO1=w&n(qZ1ejmSAT!vt#L7{U{5Nv}wjcj=1tm&oM4!A&k`-9C3yYso&t^PYVy zAud3@l;reP2+&srP=&xMwjjn?mztJspJ+q=N&YZnEG6tdfSqMGn!7>>dXJ?>NFtMD zKo_RaQfYM`P4Wl0Hl_ixhvyj`LXTder%LMG;5^fyd~_>-uR3|obMRsa3_;SAs&Nj_ zd2ZnQtzSXaC*J{w^bTH68g3|`LLUM-aWy_Nl!xYrHOfn(B%E(%&Gy>7kPWNDG$FTu z>>kDAXB)^Ai=aLm7S|eB_1Q@S=l+SC$&D5du`` zPD*z_pn#Kb_}p^?t?Vp{(a~EKcKa@!LeQmg%pG$C4ni>1a{J{*<3(EtfltC_%2fg@ zCny;U&p6H)W3c^2E60&%?u6R~K106Eyp1w!r)_}$^1#_H2?3m`0pFJ1)LwCc=M69u z9#32@*TmAyIL{EI#BrB<5*Bf|)v{+Vg0c-RjqAT6d6adzO#6Isd{Wr4%ZP<>qkhgPleUBdGVZoH$42xu+NJ%b#*k_O#A9*W?lU# zVNUaRkp?U$E;evDL`^+{f|cj&s!`Dw?Kyb&L0+w#A-6d<#4E@}obPz%X7U5FmIdwK zMK;*w@=+t3_yy8!Q>;;^ONXcgTmYx1xY-srYk-T!Xl@+k#V$bh7N7)!l_mzzimT*d z1_n6Le2}6u8`iYqHi9ag`f(CMl!N&|6nwk{b^UQhcq_cT z&^&;oh5m2G`adxXhg8F`R=#=Bahg*@+%K7Edw4DucIuwXcrtSzj-dr2xkm@EhF!r$ z7M+2cC>}h>`>dMX?6{Z5*>U%D1L8Au7>=w`4Q#=Mu|2E>UI90nBhbSQz={QCAFj>X z(22rWK4MSqF+7ldLDIzeBP+9uj1Uk9^zl`k!t-Qj8o_-+lr@{iSwYwX_{+2Tmtn@O z6U_cR?@KQj#_IASu8)Q9ud3Dw4wwa$5X;hqxW^3m!Uh#sM)ZL0=HLqFJ;|(+03f0y zmL_lxyEv?e@Se5}WYRXk#$(34>egV8XZsGzMZJc@!C&Jy@i?>Qb-_AmW*&0J{7sa0 z$Lk7F99mb%FHAST*B!p=N|QX%M7oW?G)82 z*F#5J9{|T{7$wdVpW)?{3xJ4Nv7Ey;*1Y))kdv62^N6!YSQJUYlA?rt%XOT_WgI?U zA^FO+lhRy=S9JU_J#biBENaW2A|9_BxH;AzVYZdG6Q~_6zKG=E65NX6YMaw&j=2XQ zH?Z+%rttZh)pX$|<|k>d9NCWRDuf$?R8uR2aW7)E!D*2V2*V*u$Tb>FV=$Ablc z7;Fe1=kAkhknMLCvixO8-vyfjScv~$3h>^A!C?Iwb6iNwOizuiy%boq`b%@S#Wt&9)WdjdzXZ?Obw%}MS z$wu3J9FON+tkft^iH#I>gn&v;zxSI>b(LVpg)f4Sh7=7fB+lxPK&kkBxmUS?1n&sT z1Skq*r}#8H%1LDjx0i%5VFBY@yk^kF zGw~|d^d(aAJGBf>=B5}j!jRmab`5|kW=UO8_nT#v11eV~SJl{U1(6;LUG9aaw||c@ z+pD;&2aqE-mvW$Y%fU8OhsP%e@l$U7FuwIR>Do2$n{|{;Ei6D&i}zjr)Up>E;HQ9pOr!uRIiwK(t@h74z-)hGH>aU4Oi_ zrnCajK7R~QchRb{NCkWshbtq#it>s8Y%>VT5v#P*O zUU7o`eqS^i354KSCrWg@Z~*upUNamumEDnh;i^EeDHx3d&ZjH{aF4c9Uqz&}ys7Mq z;keS3t-(>K5!iY0a907KU>p61Cq{U3qbLxoS4Q=uH~1=|Qife3H}tu)I&Mm6;0=Tx zbnk;eg-{s6Fe^zJZ2LUZO&RrrL^dX4d*1fgK#6DWhQo!eg2u*j@muiTjLasG{skw) z1A>d2y96EOw)uby^QGpIAtavL*1!MwWj=3F$ zH(a^NEfOgq4`kQoi((s@fvx3hpI*G;<75)`4S0r{d@h~(P_{o4^O9X3p7`I*L1r(O zqt3@_zd@o}!&Uq)*-5hsd?oZ}K(xt}0=5xN*r5veH`x4B>GgUckM`;PI0c_<Tr2xi`vipZ$TReIt3UPJ8kZqRQ9k7;-yJ!`Pdy7kI7ZhqMvdm0pL_zdHJhh?Pxo0TkxBg|I2g={4#YVCeONF7 zf{fP&>|gE$r3kMVjPF5`G~mNMuvrf1t%2pgim*yug9fOBW_%i@gS@lIqh&e~k$FC~ z{sD@rYsJL|wM7Jz_5>JT(JI7I*rR-ggz;?-CGdX3*5A8%Lu<1B7bHrJ8YNJ@D?0d2 zz_E_F3t(?0L>4SK^*G{#84+R&Og#r5%F%j^9P@d#w!KD$BT$ zd)$hkS-x~!A0Do@e79~uYCvw`7I)Qoqr{C(k8GIPhx0Yqt}6(BK@}&n#!c6Xw%3}y z@XCmwE*CcQ!uGMItK;b5BUq^y{gt60SbTCxWHm0FW^ACF1J;;5us~8}aJz58<>LV; z<*`lt@{XZkG=}kXje;RV+Ijf8B$ox-fU61c6C&nqha~nfT2OzJ+^L{Q_k)wd+>_5q zuz$RW6?w^_X5?{ek$`34f}*6zsTVEfj!dn{B?|M)?-dyGu(+s7t4|a&q?A(bn=HMc+-2B z>n(SPwWICIy~3j(Xu70 zh5P&bAbDx`-h}U}D&VPd;_9NXDgO}JPRf3Uo|mJ=6YvY>L4f5!iKk>Wjq3*3mYBBR z$SCp1@~p~z!_R9t7#!m`N5XLrfpM~|Ce*4YGYdzbLPj%>_uNC5KA-6YsGab8%LSEO zxk7x`tEL8>FVDSdPcN?Zn5IKFtnS@!!J{d_26?6?Bi{ymV>q0FWeeU}(m7l{P1;W5 z*q8fX;3tL48ZtSuvGZPB32q^Ed$a z5V0)*f9Y)BBd(Fhr#XnZ1}gmvi1?_g^w`Lpxqt`kBh(? zXIRVu)tw$sKYX}~C0faVUApyi=(W-;=wAVjQ|h|K774#W@-YUkOR;`8MZS4Kbgpssm2=nf3?TmR8#upXf|%d*DQecZs~w1=LE7kHA1f>SFmTXnzcFvm;k5*k>M1|SmM;vFiTubi(Zke-a8Clf3A%q|-i@A}VW0r71msz7mA+I~n zA@*}%&tnVXX0`+g8;tU7PhogJPW(Z$hIt-mAwIOt zfWH>!t`P2_eC3cD`@O+nu(A@khCY7;7f!KEQzBd&iQ&{!>21Ir5^kOXCcGnE@~J^%49;P*eP zvCd}mgZEqwyWHjn&tZFY!~EdIk9@rPZ52O%tbY9Q>UY%RRoX>m|HsDXzoSkoA1}QB z9W|nS{N5M7qkhBCOD1=DKfdz!zoUNTd%Meb{qnBR_254Z{FlIG|IhmV0>{cPc>ciC zTJqHWo9;5#xbe@8pngyLms(2ADu1Y4+4alBRQ#-N#`AaA%`bcRhF`&lO0B1V!CNEH zQLleW{nw6o8L$d)=Qh;W)t@Tdxs~MKS$}_hp~?E{f6x@ShxWNAfV!Jm|NLivz1I2_ z1eO#94uAI7OC^_{&c3dJzMfv^=B_4xXZ_ODt!C?2PmgIn>(Bn)e^ou}zhBzhR2<*} zBR!s8wv?%mR#u9t0MoC#zbn=4WYU>`dwuv}ta<%|wGvM`WNZ}8%&u)(39sA*!CJq! z^g%*mlFNR?Evt8-|ur+=`^$vvFEz5f0W{N>&NM8Zo{3%ZLx8S5K=eM8#~ zb!I2bYIt@?Ew32ZkL$_4q0YX+p1$58Cx`O2Nh|Aksob_IT|s7w0B0^Ss3EB{pIU>8C)Elc`I<{kk z&Fp)JI1Bp+2A%%z&ROd5C!r*hbva{i=PTSdSGIMs!!J4JNlFKip#ZR*{x_e|;7juE!9 z2e?spSKnY^Ztl&WUvKy&uRXf)F<3QyLIZaGzLj^XvumioucxqbTk_}Dzj5=Hoph+Frx9MI&mO9Rnz0z|`9@O12OO5MsF9d_x8fC)uZR7aT1*kmg@oEfjpw&C+;Jf~&J$r<~y zAJ}Sziz-Y%r-UpzzJMo~dA)i&)DF|??_4|RA2=<4wT4-C{wG)Q?_5L7Y*7!uoe`BG z_V*@RF}=@iP6u9oF0>^D1u!c>yAZxZJtHkpnYWLvER6y?5q$(rN_Z+?D$K1riBHOD zdq!a7fqS{BOT0C@1jLjT--_YOtY%rxIlyRUuwLw;Yug4K=}<5%nnJ3THE}( z4k~IF<~A4F>;l0gKY{cT4AZ8)80UR9QRj$%LK0$Oo=Yw)K^GS`svwepcE=>k7T*DG z)r7d1mycckq?#93oH&`VEyT$)xvjw$Moyd<+_`gznR)s6}0%MMmk{myAa`a$$ zaUD)iQ-Je%otpPx6t^mwed92;I%Jh_iA&HA#YAiqDG&6S27-s(Fed)1AW~+ zy;iEKMJub>ju6^i1l(f;zk2Vxs{VQS#7OUQSMN$wesituhv5I_Z1lEi)Q|jxXTVef zz*f7x1+4~+d&lkA`uqKV5?^0f8>lIkqO4nM17%jCk#d$l_%h@ydu*{vW*LxBPRa!2 z8x*w=&j`3r5U4_g%&*E$A$qNy_~oVU?v!q3#uoy>XraH zRWJzy`W6kjkYom)=WM*g@tJk&bKhGIoHhYWB8U_5)!?gZt7O5S0?Jfs&`t=HrsBu| zMF6@}YOw2-WC9(wx<~=dGV!CJ?(vxJs|kaZS+*5O3x!=c$0Cvd!{y2u*v z%ZMrpds#q7C1BZW19QRE3)V3V9|0yR4P7Si7#g+J-Gy8;>yhMQJaJ)kc=SZ#1UfP? zLN!jX9&<&-jIDot|KF6aFYNVt)_>$D|Hr;8#O44SMQ=&|q~>YZPb@EQW{bK4P3$}_ zk+y<%2;qQj4IjF7>qW4~9Dr2`PT0N37>C(eklmwEppWyJClWyhVNE6hNQI!GB1f3X zgI%4%0_M3^ZfMsRGhZt|EFCnLrUiFm1}JWiVKys?Kw#36DSHqA8(^kM27s~wus3Ex z#L;!Qs42C+WPDeRTfaIP*YvE7Lb?oK*NdBIW*r2=#$6k_fymGc^BCDQvLgt1f}0hP zWufK^gRCjwz5xk9fbJyzR%`7^gXA!l26i6Q+Hg}ki6^OFdg&p+(xx*>+;cCX+cCzS zu!f&q#%3ZV5s+>z3E!(|f&ke9%3#fUw0BI4S!;d&Kn-N2JS-Zl7NUY3CvMw3um#4T z6ma4g^O?iGg{>gHv6l0htat z<-{q+Y^Sbh^fdTb z=wD%s?qlqMg#rm0RSVH$;?iUV4^9WIo1?DYVk%`_u3S;$0SH02wZ(d#FCcUq{gsr7D0zAqLOPEOHutwy-ok z^9*KQc$rAA&Sp_I?wObQMT|?(KdAA%V}e9_bxeL}8w-qu#IeEy5y)sUTNE@-+FkSx zERjrclKa3K<}@yflSQviP+I#+I65CZGDZ{i+$<8Egv&$p(`E>WG|(fsoB)QyCKi8N z9f!4XQCS$4RgxKM;H@yKW#aUMc)WWMFsI_jaaacf7XmW_D%%s=VnO_X)Bh4+8l{iSGeElqf{WCw@BkvpY_`4t;0t!^b{8yVo#@Lz+({f;T>=yYwAWzgw*6%e zyn6<@7e`oJ&a6&CMdZyu4qw#bp)NsBA;m( z)vf{Oqv#2oDXxe_{izTt^J_DX^R@^&Db6gw?Q#ZZ$VqKwxb?ZM5L!s+Nbs{er*pm{ z6`17BekppskCg@E3N*MV@FDK;Fb9qUGYx_Pv{t4zM7E%5z{5zi!oGGPVLMB~UV6MU zF`30jlu}56ktu#2Us$2;`zxWCg1|GH2lKI9T>GLto@8b*t!K7p41YQp4Q#DTYx5a< zsApEQC~#ZA94ICI`*98ycj|ep{X(K`aZt#@Q$hdYLYSvh)x`1Dm6@%`=?UEa7u6J- zC2jI0Mi%9uc@l-Epu~v$OfQivVMD!6z=jywd>KoX9dVoE1Qhrbe z!V0tDm>}3XrGK_o04^a`z(62^^_9^It#AG4fBbE4*N*qQr19z3&s@CBwf^<@t*e#Y zTiflc`~XrG9lr!O)%DlATz~y5kxJ#yT^(Q81r1ygrCTF^izq$yQ(qZXI-{=~22*WG z>ucZl6Kd(J?g&!_VLCjIz{|`Hh#nFbhEKH9zXJY_wNs1@LrsDqEuqISt&S%oE)U3? zZc~;r0zzBx2nB~V_^*4gwS*(!>)PuIXaPeYi|CbAGmL~8pHA*v-f3SogoWKNei z-QBMx-k!Gjlx)`sA`ZuM28tg*9uT|R%x1yoktqJMsLfVDMo`f5MRTO8PHkG*58^e* z&K)Q9Pl!2I92KYaH$=@c*VeJN;@FUOI31a2<-r1u#GdV(yr?!1T)jCS7;BDQQFMr{ z#zD2{e+bemTdVt(_HK3wBv-bmy$~_kv)zdgePk7N(zb$l3n2Q2I~S5|wJ!(cNKsTj z5&6qi1$ZTRN}9v5{gZ1+A5NdXnvQ&XDN7Yz} z)z^_2JwL|&rvIZt-)(j{9Wjz@5smxPwH;H&0blw5se2RXNVc>*urebem&kolYL`;` zQc9IFwU%mCNwx3${;ITB+%t39?>t3iMBFXz{qKMO{eOLp z+cvb_%>g{}Z!zT)zSp)U-vR_!o^8Ge(DQM|x6|5E6iR_Q1nAk7yi>uJp7XOo@weaz z$^$;ubTB~_R}jvoZvdK17EnXKk~bCvP-Ieb&*pY0xD`2Mu;?FWML;ECNeXu+6Fwm* z1gPinu@nwzuxpU}(sdU5D4!fH2QxNny)jvUgiKpE)FT)xh1=U{+Y6i(r~FY1I^aQ-gXp-Gue|pz4KrknXY-qui1(S(w%AKSfC*$L=x;3VhDPY zZ$6L!4_nYjXInB?VTYBa#C(AQaPsGyPO<#rBd-*sAfNr&f7>A@QCr2u>21Wtw!xk0 z_>)^oanoqZ&ST8<$LRucMU9eRacZC6<^5Id^CVgRwwC(dMq|C#N+;2pz4w%_41taVsL0LWV2h{#PLUMRo&ZOb9@X0;wFk22KC+&wn9O zjOYi4|LaGNvh1Xl7YcMmzIIab77Qb3A@Yhq3V|Fhl&4&udL+g~!%Y}3k~>0_O-W+G zm~6Q&M2iquZhT}C5xFTpqg)ipmjBOkVX0AX; zbn^UQ@;cJnO^+eL19Eztp@^v&lIlfD6w|O1X#s?e&Ot8q9G~2s&uId=Qo(W|iw6d~ zhfSP8;Alt-?S8RekdljQL6!plLpqLbHzr7gef{7HfZ-$yx0PrCb48KEf|VV^iqyz8 zd<7O>)|~eho1flyQPK8DOwG+eCLbhyo;GmfOL=f* zB01`RHp&+4d5T`GY&fE11V&;Y{n;@lyprgFKqQE{Y3-O{Ys-Ax9n;y-n;(SincQ~( zQ9*`BXnzW~wn<{b@n<*+Mwedh|IME$%gXK-6;^KJbar%Fn}bXukd@#&3ShbaFEJMoD?7@fC#FH;s@a(AJSNgYADo~KSdsI^o>d&r&{5qQ zrzyr*5^yp#oopV2dBPf(_3)V~g*u3ugk}LVgPBr{F z{X?aCvucNKkD>cy3@mL4Z>(~)J20q=VFX4?EI)M>2{*TDUB!4A-?rb0Yn zip0~l&b;-nZYq1U53eIws`*L$eu1w36xF)-&=awq%_=bUb$ICknG{#fU3AcSLU(JU ziLWlvactQP{_C4?I%?+QeMfn%MsSePVcQk>qPPmS@OjYbhc6r4_vw9uh_9%9fR|q0 z!;uX?@6mhgVAR8ZF6guN3%owBv+|8%y-WPdJY{sFd*n)rvwVNCC(GbPgGs$bTze2A z33V>$ydH|P#$dC~8Yk=YQ|#w1-yD}ANN$4R3XkHPz{2tC5*M6^SGhii@<$IDd&DWT z+llyw;@o&&apYpt9Y%hJk%biotG;BcOIC&wr}q3gJ(w+z=6ZO7+L15ajt{2Mvv>mz zaV9IdR+s3X)xcPtmOE00esvG&a2hsa6Sv`EJpPF*N_RWFw?3H0cT`qg6)&wiaqB(G zb?Itiokt2?GU;e_UUiyZK&6&e#>crz*cf0}w-L;B*zz`Z2jMEL-#A+3(D5S>=rVr~ z6^dgFoADOHOu^gQ@(t|iH2(%~${QF{kFJG>t|r2Njh%2rJmjL&XhW7IE=g8|PeHFvss+RB90b z-CPEEwGGlW?_@K*<<^!^yI4WwY3NcI*Q*NC5;9Uw=LB4yhw$>UQ-NmQ`hAlQf70P? z^Bb7YV)O4|i~+xM3|(^^{i!UmP_7oCi^{GB?*eXgxNa`OrH*qOhqL#hluhH!i0sU| zDq<9m>O=^4i9`u^$>-y6bfshBgwr_>|3^+z36ee`1f#fupFm`v346kxnepGgsT_dE zC4@!r=Vb_l)gv&l(mlIvr&B(^O`8}&wlw<@!?VOJHSt3R#zFu$s zB%W6!RhVM|;<<*%v<2_>kE$FmIEG7gxZJ5W|0#+cb&G@U2an9iiz`Z1;s`$BvBK?z zY$a*zaeh*bxd$(khn$Z9n*)5}Mu4K}sYeSEhG7wyWk5GZyod~K*>c*xxz7v2SnhMF z=4G^UE2d06f-9wuzOqVr<%4pEQ#b!U-jq01hgtu*vr5YRYru8`f8n;doqdV?;yq{AfIlp5-9AjI2g8b=HTCrLgE69{2F3Z zk@x$2rnsPIfK3MiuksrYYKY^8z0sY;-Kon8gMF@_=bN~6_>QJhFoXCcc(yu*s8~n} zlaHT;&Z;y78b)lK5x%$liXSs!i)e-s!3#y2+0yDk1pp$Ore1;pl&czyt^iz?ODg=# zS5!?*RB)nl03oyNeJlt(-lqVq1f+JeA5Y5K)UjCvX|n3!+=D0Z2;9qgVr38!2XZHd zJ($Mrq(?Cw|K=t_vTH67i=dIM=kFnk6l5XB`olJyK4%cBPuIQPxPn-(pd%b#C&%KRAB3{*nd`2L33<>RuEJZ*_kI>%*1VEFxR~Y}%sN0UWh=E=a z*Wq_Gg_RIY)^gZyRaI!A5s-rC=&ep%O1N{n#b>n1%QO2hLH-ywxP*>4r7Bcs-Y;544wYYy)z95DNw9ux>~uHltIVVw+=v;O%IP z+?;8imBuJf*kT?{hRU<|l+h!kM+04C6*l;`K-e=i6f6mbRv(x7YW&s4<2?bR$sf~w z(NK1u&xhFmv1Z*LsOhcn`Qi8K^Xt_}2!Qbap_mSTSAP(TMI(lm>h)$Q}?V3i`WzF@$uDFrrXVBos$pfhckg1pR@C9@NWy$T$!U#$t(Z zBm|GwpfBvN4i$wCg%FG=j1eIEP-(zlCITquU+wb#yz{SqHWL5$&W<143v>~EWE53j z{n3G5BSO=hM;oR&2(MP)n6`)6pe)%SrdQ0gXasA)VRmUu0)OVjO3S1s| zsN`sNZU%;rG$Dbg2wb7{n4I^Px!A&c=R|NDe7BW_-F^-U=q&R9fVG{6LVIcn)(J=l zVHxv^B#0awSYchv@+8N#`I-Oy`<(FuPp78G_E|Epu{p4NGE7*-!K7dz&;3r0LvRJr zJ8TUhE+OU$(cm7H2mETpyQPhtp!dZE%vCzr8J)?%Lqj$!XcF<#xh7@LP`U zgnQo={PJa>^+I{u=I^xRsg^8)LhS_zEFUp_H5uneUor4M)FI$bp<0G>4n^V1i)5MY z>EP~4_jPwbSh);V_2sYs(uYMafAtqX)Uq(}qokr8Rx%6F>%%UIW=4<3$02is#UrHU z^R#ndLLR&orGB0jrxX$rL0Rtf-ZWCY4kBD4cho5IFEfDn6N0%3oa zY_^`jRAv#wKahjD;n(5&c%=WWWC-Nkp$aMMC-wh03c_R&abFvHTKJqr=9U2pJ)T z$ERss4+$vP!B^iUn?$D<*^MD^$4QrM!b#Wd070-LTgsgE-ZvW zSG>|^viZpJG}Lb}`Wl&fF#K$X1`DLBIeM(CP&xQX{al<(=dgP6~5Y{W7_oYO=xs;;oPputw7-de1+xk2P_#;a7UQCT7S zccC7|&ez7OqB|o(AZ{hSNBsqzd}J(LA5)M2U3Auh@F(`1CkB~aSMX8c`)~D8v2gK;XG<2QJmeNiaR>nlb3$w??DC( z<-NV+$!38+(BdO=NNUTfIUvD-hJawS#lZf+rR(1 zvECJ(Fe23#KON~c0z|kI8whuF8ID+6@$D~9{u6Jo;KdefJ6Q1QO~`gr+1zSvH?{fg z{6%ZZiBuuvE8>mBJn^ z8n`-71HWp)BTCg*4S2qLc>EmfPvt0wK`{+ z>r4{QU>~{RRI1BmVvq{{A!m{t|!x1%Kbd z-+#s5U*YesonQR)e{;Hi^>eNdmAYuJ=-{=`_gppBDD@xcF@ydKO35D4*jc)5(Oo0X zKazeVkOT_mX~Xl-KfFhIw1--fa?N4hIfiU;JVvrdYUNbbn3? ztnay;P&8OsBaWKyqjKFjH@xX7`N?PKnR7=#S}jjMn6uq!tn6@XD(ZI6(x-eFYMUBM zZFAJE0+gV^T0()tg+wal2Y1DYQ?!eKZ*+g**~;W*NvK({NofEqLhba+fLqEN$hPSfGy2hRe5+;yh1 zS@mjem}9{&3=2U8UEjRwM0D1*gD4*g9>KN6sKM2bEHOBlsgjhavAxg=Tk%&v=Wu*J z<#^$DK=ll5E%VFqU;cX01OWa?Ea*=E)Ocps<7lOJ$(~D6%&76nFcf|vVc8jG@NlOGBQW}E`SsGnbP4eh3?m@X z0Ib|ZP9n7RSkr(_7>t);vyFc0@7_|O;9rw?^+zOtK7dUW-=K22T3F>9yfD)l&9*PGnid4)<^Xml-+wg3LoBA3BL}PDF`J_w+Q1n!VMd;K;Tz{Z&$LJ4DkL zqa1b|4`Ezm4Y?1RdvN^Lzxv zKh*q*@&x(83$h&78Qrxqx`11w%LH(ML{=YiNpcG&@;v4h?f-kQBVj{UcHT%-Iv8^z zpAW-O*RZ=vgE+~hZ84bUgs_log5_u*;+PjISf#P630&KQM2)JPW zHmWsbX}!|Q34hy8$aDg~CsY+S{&U!-iBHXAf0y@h z+=pSRSmf>)8-F14J;>SbabuvreM>ob8)pmTRCWRiu@idga?Jp!XdA)&H2onXSf}U| zPSK9!2_Dzt}9xAdIQ98=`Xkq3AC2_GU zsD#D&5zgX}meEcGCzF+4){~E{e(ngcg%?=|s&!w55C0*9VzD>sgPjIbDC%_)uLJWQ zY4+>7-?t|cjrxKOzD}QB9d}gVd9fFD0=h5jM`njppejmHDS(Ht7w|`r&cH{54~D+x zPc%~Dbu?q7dUd(pilUXFP*F=mD87$R%OX*K5J9)YzHm6)=sg>%1YLuK4ql{*3PwZa z$c>=adSkkrG^_m)BHPsxuOGqevM@3(w3fN!@#LI&to%8vgC0NqX-Ig_!uJ?ig;={> z(cx)CUc;guF@f(YIKr*0As)e*E!=<|MBsC(%VKgM0>JHK-2tmF{#wpzPG&4+Qc)!5 zTY<@*Btk*>bszxlFJw=FxeOK?yJEFF;&uRAT*L?>gJRrqv(JKMlsxIeW2C&oX*N>Y zQAVn>>j`tamX)ujlrY|56^weGeCOX17#MVVPI9wz<=?HUudS55e~q`Db%zrD+!d?E zY|uz2vfM95!sBW5+{mzzhe%Jr9>q@7IBZt@n_Gzefdp~%DiZ*`freHiO+KANU42%h ztK|J)tcF`-;HX!J@i?M3AlemB@&mS2Jp~pu6YE5+NaUzN48RSeKSB7HS^lisyCU%_ z<NRL^mj^-p_8eiKyN(c z(^^@zw_&dh5CT-tjt#UAY%~)V?PCp}mnZ6zEXh2r*zKdL)`$eGY`` zSiR@>!XQe=&;3!OY5zbRi9GR*+yFS9#U$`tJE|9vSdNiuTVoc_8Q2aw9Zlwy-vO|` zRm?tJLej*D!I27?*Itr!yO|?owTroBVN+=hPko24i-{91^Gwgc3>6)U72FuJVGOu6 zn6-ccg(Yae`Ge@Bs^~PH7qi`4D(lqn%r7&)fOnObT`H^|(ZDR8Aq@vIJ#vr-zyX1X zrJ3W%C@$^7g4fd&uEebZ+A)E=X&FMR16RFP8WYw``yJ*#c!qpJ=Q*wGw05mfU5E!F zsE?m@cYvROL}hkjUCY!ntUGbGtw}$pRec#s8pgnsW02)lv*>q`$4aB9AYmTB@1!on zW0P_7E*?~tla-wzOx>(<%e=_E;o)e#S+s%}`dJQfoRa{q5D7wfc}$wVhqJs!GulPo zo{j;33=Ue7hc2<2>jrlQE)uRncAi!&3Ia2@*Uh z5 zh6p_hth9QK1hqM0#|~s?!W=QhV+8aey(T0xV>kDRyAhWZmwfFmewA~i3#yZx5V;8h zbU)%20ctoUU~!%i!OH56<3XJC|0wdQE{|HY}wty`v4R3wlVC&c8_>VYRdXAsICd(Z;T2YqN5CEyvS?@#?0k- zU)b_EC(XbKYHx#T)uEZaKh1SG%QuoVdhHQ^o=0jsB5}$mjH?zGF~#3+yM_Nk`_mo| zG%IkaC#}GDFXEtNpjNT?k7brtjWSJg6wRPM9Lc2l1r#`u#hD3TXYjb3V#TdM9d4`*qrf?^-$1D! z#qHyyi5UUUM~J11fHApUg%Q}Vc&td!f{gI?xuOZrfLQ}TtTu!^ZiWSrRpJw4Uq}rn zf}ubx7OTzfDKpL#MH8`dq!2~Q90Ml7m7#b^IE17&zC`R$RYg2n91X{iW+xagtMC_B z>a~erFcJ)gBjHdm)>IiPPE|z?RR;9(7;5N6VSl`+BvKkFjz{$B+DN!Do~StRmR^jM zIf*c`^yr~zw74-;qBr5DUXLOHsZTEn7Wrc}C9!BpJdPARBf%kmC>-&H{N=DH{?vzm z--bxrblv|;N41%}?{}!#3+6dt-C|(fl3?A6T^-O`5a|zK8iu$|Z(D99f=63~ zs;qF6&>%H`$KzUrmnor>w~Ky3_Uk7&MM{sAn9fQR?~>JSWP{7x52G&U!pgU@w;f+t zbddI_iju&Uw6jG7@!BGujc4P;Ty-V99+%(UMLhKqY^Rw|OC$??XN12i<=PC%Ex?Hw z`iS5p02YMkzJq8&<$oIfJYddoG5_pe+*177Wt5#WzlGnuS^8iRKR;68aJ9z#YQ`=X z@cAOWtM~$V9-9L6hC%UWyUfno+xWSgl#i$ZM65G#5kp#)q<^cI3H4JtnU-T^{d;-X zGEr+h$MdZJ~PHS_x0bjm24-CN%*{^EAxKqQN8Ujzz16&$P zaOu||0U8D~IgK01n7P-jn7@FQD`4Rwl6b*(Nai&I^fd{t69oq)fq2f{Vec@6ywHM)bPt(ioSx#PhkYP zn}@h(?F=7wsp`vrci`)lA*LC}VLZTx<&c^wzjaG#8=zLs;&b0oy?MnIo&=fTa8JBZ z(-1dNWPhx9NkiuEDJF?QQ(U!!W(w_8lshMpKvG!h1l*eN6~_7)Dy*JC+QHK(QROSfHcmw$Q9ra*1@kxY zvktO99SpFUCxuv;Lu+B4R;sO#b zdYUaElE26WNrQ2zDOv)&Ly}_wm;(pM!1)rhWBIyLR`emVj|&5}w;J8e5WP6V<{7+8 zW{Ep=F4!c!QzxU12Aam&NMiQ`J_;}187N^Ft8TEte7EZ2)woY2GC*O%YBEOoh<`Ha zQKN9{!{|!f#>0NMe)fQPwyy3vMc3Htca}~{)qT8MJ*w?Qzu1T56HYYMjBV`x1F=|Hqs%r$6uaYDXqgjH#+B`qm{05*KZf)kLad+aB zilqSmkxNAyvKSz7in^?-fPU_r}K101O|TOxF3H%X#|!N$=5umUC0kIC9ZIr>cbJeI_05OlIe z?dBEY{JOgH_!%}0v|HWQi{Gb;Sgy+*!tg5s2a%)?w;dYM=rZU*43qLkxG#Q)Dvd+p zTXzNm!ADlo#def?uBwxB4<0~X`&H32?4u)R4j;U83?=%U>c}XwpSI#=%>2P8*Okf) z$Xs}gkuZl_^b*p;K0!yT6^gR52x$zZ`-hy$*vLcF!i$?K+{*p{W2ke~n?H>P+Ol;h zGNi;Ahz&F}f<7Rg1B5IPV*zteWVEX4UI+ljY&|3&87JH-Id6z0c~|BGI+I-Ht7pnE z14~EGO>0zpV6oSi(f&JLf^MnefWsfBV@Op&WQqPDh1<9IojB`Z z5+v;NG+J7HsCgGg82T(LLzS<+k?g^GdgFcwj75^Ihb)&v#0S7rdr-t9t1|+n#i}Nz zm7w`Kx;g^wed4eEM2!atVfXoKz{6(((wZ%R5dtuydZv)o24@eCWm0fP42n9+@r58C zQ#FR71i5$!?-s+zM$OPWB*gihNBMQT-CO~_$CmOT206kWi2a=>tM}udGDyPs2&Pd-U{!AKOpjD29NtAq|akj@B#Ek13q~1l|=&~ z5cz&k`q6kG5=6GkKq3?gqIBc#-Vm~H>fzl{Js1r_5fcyj!l6hc5f9veD`G4Wh(*J2 z0}MthV|8#ZH17J)RzSZ6ufj<9@rA~LilS)B-xdm^6Xwti_|8%gHOUt8;zVJW(gyKq?uERl40N4NU6Xs=M0HR<3TEPI61i=8z%)ma<3a4bt z8h5*ZHyo~D5F1(KMgv4FO{cL9;vPuRolBshsLy*6a=HD4j+GOf)P(2-!$cmPWWEeN zC6A#s1C3(-@vkC}c|?#a1fmcvwe#&|v*gzx{3@YuyHVwt* zU@CbTb*tv=4_;R?*;?F{N%rmrmum^hTmV|@L})jvRFUV9P{-OkL9h|xJLTvsXCv1L z=eAr3pcd@h-g1wZ0$(v2t&Ys`0F+}-i8*0j#EX(1gGUzhKVXpfIL$Gpl!-$#LRIB_l5}r2hkE&Hn-PrOlvJ*xZlbm36oA`-}_t z5}#nPIDJ_(fEd^|1~vlbP1Zu(1$y_{PXA>D>^ar*5TYdb6`<>jn4CsPH8o~M0(KSx z_B~6qyFNx5?^z&lUG>5w62umJGoe$sh-UU^3R_GVk{~c}58Am1LPJ zdTjxZn^YYU*}<$K(lO>hxTJp7Z)JKw7{tl35!+qA+U0({Y{`yt0MbT?zpX3qp|z#f zdtL5@C)Vy=Z{Y%Yz>CsIVtoKb&v;cxQPJ~B(nA$qirGFYbG)F?_aGsp_zo_|xZ@{< z=;@Ha6}pRoAJ#_kc+dm!6}uB?8-e@(Z(=^%`;OvWspf)fCAqM*lkB=&bI;@ZkvJtU zH-Dz72)K>5c!ZyZh}5k34P=qd##z4Bk6AbT^)44;_)zVWqo6JkljX(a7&e!LpFW7M zh5ks8ULEc|?wr;^63$QaD|-dSw$ysu05?#|2;sM(Z|UhmiMNsI7=)qlUjyA7Nt~qZ zP__AwFu2OBLBjJM>Abfp`SzHHj1ktDgzP-g3Zz6>J4#hlqD;3)jmn56y17d|Ww=C% zIaDGNmB>mZUQyYC>T;8QqG)2B+W}dz$7evp!K+TRY33hd6fI*|fpwnbwI^K8XP7~5 z+{0IJ0Wpl(u~kw78YSiet|3_TaF{~-CUhqd%X&4+zwLIyWJA{Pkw=rXHijj$YBtlq z31oQE;LfeWGC(BF-9T>DDD&!;u!|GX=@Z#MN$DrtJoTKxK~bcf4LBBo=wYk&_m|A3 z$JdqJ4)x`?_kVqNmRKunk?Z)5lV^439I)0CJjEx0>yrQs9c(kkWvO$MiC@Gd4CC%P z_!`R>7@*8mfO_x=b{a{oj~XmwbKa#%HW({n)S_D>WMGpMi(PU}X$)n8S>z{3URG7izlGAhB_VtrO$MR2on?$zi;-W= zn7@SA6-7G4DtW`4PQN99F@Fp1>POh?f}iY9KhM!rH3#UU7-j7Y?w>kwU!)h~>aJ29 zwk&4a4Z0mr#u+)v1&+HJWHX?oe@=&7;*>!$pSvbxs18&Lbr1+a6{8$lo@jGo@h6-s0z{44BUA* zizIiRsVZXGV?(^f+GT20ar#7YNhnZ>hG>xyiX2Fn z_@m+KSfD--Dh)>Ul29lRh{r;(fP(xyo+t@K0)ZA^ur?Ns1wp5m*MR^JCsV$<=z;K+ z;t0rR1p4s#LQN5W`GT(~7>Nag!2rT{1cHGYopg9%Rld+a{%OVa3DY(2fOT;MsXJ-)lBRMce=#5T$s>K#$NOkaY(1+*ZWt<*Mc9!K?T81+`C-5bI( zLsMMS!(+2q@|Z*;9*8WNR|7x*xSCTuZm*JOZ=QHuRw@h&L>3gc>IZPoNa}8c5wPKD z9++{A;x&x#bhq7)L44ptcSo(zpRY!^{qTT$mJXe(E5zt;TF#(7vD5tN6K&-7e;`OOP zMO%SsFoq?E#u?}rMH0S*fz-I%$mM0Z9q?_yqbT3_g`cwEy29=BPtk5|1D$uE&T)qr zTXreHyjVr7A(!H63~FcwN5%sZI6${B(3D#)<$Eo#cfw{`Z{#E%Q!q&Eiwh{YL`AI; z_wkw*L0vm!Sx}*hr0<{>!0DBj^mdv*j5%rUqHWE34QgL=DG*x-HiXj5@qU2K)JroZ zq-Dgt0a9DAmgcXbYEcbOj`J)f7HdY|%B=*)KXad3(m)&LAER6~=w1|T;WJ2n;9zCz zjB8*<2P>6lXt7rHV9P;($!}gk$yKMVs|Sp)tU>`yy&C3N1NlS3N1c}sK@%3D(i*m3J5|& zI$pi104nC+zS0*bs;W_8E@9EvmPpjNz_mAj7OPMn(k%0+b+SDS==k{iuPfyl)lCWw zp%MX2#5oZl)?pY(@D?34i-*Y?8P9kImp+$f{w|s;%kIVN2M>L zxTr=JsZf%uutZ5lnebL0l~@#Pm8JtJ*;$h8?wq<)6kB0*?FC?~s&g6ebQ+ag#rOvO zVTAxPEsg_3C89kxPH-J(L3up1)VL2-=M1FHgrQSGGgWym zhOV=*JMVF^&gxMG`sNQsvzEov9z0z=<=45Os}YKsudl}H12i^nhIMd9eY=x-9;M&Dr+9gO%PQG^~|@zU&z$2$-=>GOpOklW8;>1eDE6BFDiQ=F5SXPtEq zm_LrCYM22T0|Or*0jgSNL?(Zf?{}-dafuNmG39~2`7lFEKLOSUSG6$Q!?&?`ec@DL zzl%g{HhyEfS03V0>r%|@C!v9Ab0OdYvaLcSipPyEC*&F*m0N&%f)-#k0?Xxuo}1?X zj4D;9<%!^!@nal`Dkh>5-p+H3KtD*4_x@U3`uXkWz3LNct*vqI_6SS3A1@wy&EMl7 zqNi{}ky2i{(r11PFEUPDH7l#`D0|!n*WK`#XK>d9HUq5@9YZMuH$YqNH0IK*?_3u# zEuYrP0KU~M%nW=Zd3>o}Zcp>l#{u*9WMCXpLbT@`9W z+yUW35k#l&%Z@9##(6LtL?)t{Fha1O5XU9aD+FDd*gpY*QCw2&))8WBcm(7!1nRk# zGdx3uJ(r-I14Tfv|NIB8D@~=c)MW{dzAQnxXjy_JPFcdd3(0z_yo8+>S0U&pfAnx8 z8vSxcsOI;hL?e_{IJ`OX3LO^@C36u?U8dMo%sq}mbj+wAmel{GS`~vzA`puB;Y0$a z2)t9kA1W$Iwp2yp5ojPnP*Yb%La{(J1O}@j90~`j{K1kypf#R^=L9&as6P>n`ir9B zNHiRndCMOuI%&B2qIwuDMIwk=T^cWfqe`UA=fB++42ONiPZE&;!XgGsqG5ljFXSuo zm6b&FP*rhBG8on)h_C1i2IC38ABCU^@dX1Fv0@!vCH4APal9rJOoT(7C;9_F{u|D^ zta-FkOKSwF_!Ex?_2dfXewwY11U46%M4^+k z-9wH{9C2PWuBd+S4Rcr`+I#>viQPh_>c^pJk${#N2#U_QwdtvO_<7g|QL`EPfV{R) zvl%C-t8rgt0;(wy#*#NNYE%flMriJ{-og7KO`BYX^u}WA-(!?xu}6xWMf-5~o533* z&Lz<0&^VA^8b!UKWk@S5+kZhR2jDO_owKpXwz-|8*$3D`jGWCHnFIsWCau0z=B=~e zCSa!sd?BxI5_`hg4h|RSk31h1G8jQ$*dR=VMpVuQiE zE_HI$W|}cluDelwxVGAxKa$wzTb01Z8+@vw>Q)mZ<^t@@YEaTbSgfPQGE9a#37hoWT!}?dw*sEG^ovP-4!no_g^{A30#Ox=a z8OP0%;yX%>j#VXp+W|&#FCJV1GYpvuAC;P)#Dg*qbSJI2z4-FWzyI|_yFnerlo%b$ zxSU*swA<+%BiV_qovJDG$ETOL603X7e~Kn{Yn1N!&A-HN>;dy@Sow!pYyyYl{bl&? zqrq~rc1C?Y79ya}^l4Oh;Jh+_EG(=P+4=rm7?`~u;23HTujR$Nc z<8@LxFwWnVfN61t#La@n+9`hhT&?KSAWCM!N>~K*BX)_q`~GYA?K7G@(#Sk(xD~{u zLW6j5+Xy1SGBU{8XiBB-W)glF!^;#0SsShcV%tk4ca*brf*-^`dx>8e)^Ld(!N>VJ z>O6!+qr)^>{?CcbdCI_p-gBT2abMv)+qQmqE| z0dd^G4x-qC$k>K0*oZfWGzi48%YozBB|rz1B!@Hu>JU@SPSfz&2R9>!jxU4fLW-$mhVa73slyKB2*fCQJxTCE248lt{&}_> zOh_}!2 z=v!S9NN&&wS~7%g)r)9xAi)rh%2F4-r)lsio4|Xq4A`GQ<%>iP=}?OxMGCLs_`|Sd zJYZ<3a379)REP*!d)RGOfA4k0zh{h+T5i$1niK7PWJlnCdL54%#gLb?SPa0!2KmYb z(^p0!UJz)9kfgxs&_(dD`hfiM1kJQUU8-*xH~R=WFzkhb1sF=cr5CtM&Y!285iiIY zoaOwT)m1+n6KN-E$!Em8zy}RBy7yVwS@wdjnM8D}OCMV(5YZv#yTk3SFY5IQERfF* zSYK3aQRo9CM~zN6Uh{xnTSNgwNRZe8AIMk^${CmDN7Tc1SCj=r+fSi31v{9R>iRTy z6Ae74sI}EmU`TUPFjs+}l@ehfcW{@R?_##9vYIjpbH8;O0vQ8}XMFS#V~?Rq3#z;a z7l{>6*t3f;a;EzJKCF%@-r#)Su*NJ=#1-yZSCN~WpjZz5?ieOL;W;tH z6KDaZdpTrg?1%WG2|C7M_Pxgg8+W`i0*)`g3%3`?i)P0ZYQ%{&t3&2GAfl!?05Cc; z5e?v32Z3^s=qXlWeid(fvmkJgqsW5x5u}0`MY4EH+GRL21*wf~kn97Gf^-YQuk5vw zKa8L;ME@Wp$o?!M&Unn@b6zd?6-A@*L?{tR6ovFUUpPp^qkumgjMM~54@F^*1lQ$Q zan|qCV*$|AiJ(!YABp(<<^DjdqBM-?=iwM!ApFrtBG?cP`i?~P0IEbH#i6)y`XD%j z%5q;Y7G6mB!d*>z_2poq3}m_vMF~nJ(32k=K%XyKu7?6X1YqA+6Ab#xqb0sL!l#4m zhj#?5r6Pv|{%e5{bS@a3?OjW!r%-8A zA;(47&$FOJaB~r%2m6l42E|2P3e@AwkPO^`1-%S`1@`PXkk1rqwnH~E1q%b9KjNh( zOpQ?6+e>d%^^7#)0Cs$9^0_IQgwlHp(;Z>5RkpWHHOslRBfUv}d@ zNPxf1!>hU@r=;tBdxanIm0kW0{NsX=iPou9y~CCxbufshcC z5mIvT1CThuxC4gQl*!=9B~3LKF|>56^AT!cdf{53c|Z!nP$Q?By2ZtDU@ek(9Yy@5 z)$2;>K^I6$Te4%oB~4sAkFb7>OT9?M9%*7gl69eEI)N@QhX=6Zn)EW&JcdT9TP8;k zZ_5&G%)|c{iO4}RJYg#t5ew{5982H2?fA+4=9e+bQFvZIL%n2{bW0t9?kX?mxpxon zSru=^1*DI^Qj`_{Iqbri8s}1~8`>$bZa9L^;qh)DMqw=l zpTIJb)G?mVxSdEiZNpNHWv(>A4uI_+@Sx>-K2|l`f$kCRhFr)RG%gt%A^63EO3Ues zVuz+J%qV#_qeby7k1S6tKjeu)kT$B2(}jyk+T@-yAoL7y8%!I1a(^kqeeG1%Q6r*$<2VVY`iF!o4O&Q$7o3LEP6`FR zjfWjU{%dr4V7!bU0YgLXAU^ZC0<-qBn;sn@clf#*G#pEv!vm=pFw*v;Q>bUXT);0j zmi3PG`|+Dr)@axfMHoa z)Fy!rJjOW!=0oC}VvHAbv2mO(NWvjJg7Oiy4ohUBd1F!o8Z1s4C)vOYf$cW_WHc7O zP~1o|C2YNH`ym+I5tSGx9UmNLv2s7I^?nLHor>GM|AO134BglBDD{HqbPP9>i#}E4 zgSrfz8JBxYIPg`=5qwBC$O^}H_25JKjF^1a6~bKH=}coQll@=4MNZoKIpTC=EGD>5 zyb5li=-yHmdgOF;LB&Pp|ApJ>=r-0#5xx+6q}6FBTxgL34$TOqFr+#txklyZigOHv z9|ak}@?%qr`7L!^@k1rLFgZK|-zkbE_(=xH08pW_Pp|X-uHu@2wFvMVnltal?kFt? zQ?Q|Mu8=w14{JKn>WKo)Xy?k6QThqR5J*T8dmSlZsXHx)^N;H7Bh91g7!+{hMzD@$ zWOfk)DPqrPmFk`X9WTa8l;|yJ=Fejk!AJ$(RtHF|)edl^1Li-$^O|f1Pb6!OtAaSX zkJ~b}8<)LYQKOC8T%K%ocyvnD=9tyqlK;}x8GO0rgXLC3D>G2X&TWxAjqrSs#EFN>wdMJekud7+IQ>1&lFX1wwIdeqv6LueksTwfyTc{B&-b;`-f;e24A54qa z$O#CB9nL*U(}fz1#u1Xa=Ta*gI)Ge4Q*`V<#-`!1f%DorF(V)mVQgiIg=(B>v{`mp z%dLM_gF(6d4HjuIhSMi#8%9X~W?lS_G7Lk@_V*!&h4vg2GAGSPgQIu2lrUt(KvRB_ zsk^yZ5y)d0X~;x1-$r$%0n0r%MXxY|5y24|%D0IZ!6{ycrY#oB4ZjzX z(}c}w3Ole4YlG$wU=*#VR5-lhmhb8`?-WUdjaYvW8;Mn`oW!+cG!X#(y6PfO13&wg$Pg=f@pI1nCh9h3sqY$Q z2S?z%AT$n7ntNpUMpYjqmMcr3kA^2meBs$6HGlve%hMBi;)kGt$Z7Tm9oDpA%OGS7 zjjlcfn<>$OGVCG%nLXs?V$*qn($Vp;tQ9m2ZM>Vtr3w@Y=AIvax=2$QG8pl~xk52T z1Z>1Fqi{X4tqC6CwiFTuiegEdbv5dnMX@6Z)Ghah=vYxygi)@Ka3p?B3;{*&(Amr< z`-E6J%oFzjO}q_AY4CiXV(CqUG<3j(5yO`jbZ$UNNOlCarHnmeSRr~~HbFtWB_b0% z)98V=oy06z`WJD*D$igKgD01=c(jU>6;~J4eQ{UN(D%D)Yw^U;eL^a&3#nBesP#ny zK_nrH#6qQ^P+2Si$~%w*LjYOD!h8zVV^EO?!$Fw%`{5Ox zfD?ruk*UB5RQOu_iBL3N|Ha?G<@hhIHWiyRa@lZHA2N^kzRe)R7XgW2=TdVIn6BH7 zaVwd-U;cTfw@K1;M2-&Lv)|ln#_x2?%b)&(uNP;LGdvd*7mt(a7D*zW?rKkWwx_$0 za(yE|Ii7X5XZA8rtXL7Hx>Dn_sm>Ib>13uS1>2D#O|E2-kpLb-9Py?$Hl=gNhvWZrx(z-5!xUmJV6UWl z+tS@B#`VCu#78X@e!(%5-XQ zZXlU%%cREVx0{LXj#tN(?rck95hs_kKyaMGbjOb0)x8x6yW0D@+7LV)8o9Z->15w) zV4-^}IH4}Oo`8!h^XVk}vO9MRFlyf2l3Ju>ghM2_Y`;R?fEGLElZ3QNrZYR21zh0E zkpP2j&M-RJ#-=HpW9vZDSb$-PUpk!XY6I|E8v)B=Hk!xY1`%qEADneH8@tp`BV zoN3Fnb*A!gn(7whvVwFBl!gJ<5GGqT0cH1V2Gj$<%5sTEX~2m{)jcv3JFRlhtFV;r z=xa-6+K2~;pQIgdtFjq(o`@bmR*(Iq*%b^MQE#xKI9VBz3-O}}Yp$XJtu7fdCgJ0Xh;yY@o5O_O9Nx zB-ECmt1;E^5=kzuAnYu0T{CFSCvy_4wq>IRhR_4J?Mkr{Rj_h6<9?^l$)W;a)UH6R zf?c_Dag+u$io5DKCJytp3}2SlA*-IPP}kRv8A6ybNJb#g&dy_!24B}4B#Z z+;@}-GXbmli74E&y?`j}%#U3>gZYPQYzpZ;`4u~ZfA6bjS~`vIz|O<@ngVJ^LR4tv zlARs0P+L!<-tEq_p0>r&mt&y|ds|82l}yV41bWB(XWG;4*qkRU^lTksskY=XP#8F!B(VM^I#?iK#g&Z+2a5;; zzfrv%OJ`dgCv6O1HMC*j09={tjNREL%?zdo>nW=)5E(WJNt;dfRLS&4O|0bRnnZqc zjKl|nam4x%vx{xp$yy|ad~G`xG&fwKq!{RGbD#OK;>1BLA0S!6m|YlF%o{VYF*xj9 za7+kCIo5_O=G{xl)k3LG!`2uR;Zm+hFb`JOvAH6m+t%- zSsT*Y(^&o4xu?0ANVoTP<$hyvu)tS`E`ZpTQQ%+s=G2)Ks78Z z=Yh2)8r*pDT*@jB6a9R6jzZW)hl7@}js@$y!Qs3K8a4qtu(UO$E7LHemRThUXMx^I zVK4TuItlN?S!5wZ$P@q(OK$BUHv^sR7!Tt@W5oa$uP=&^wc%}}I>2@AnFXwyD`&09 zBpW3Gt@F#sP_#&T=nXvqSn~v&weSpvFh28!Y5>`3*!@fM+1GtEkC~K3dVJiEC#2@) z|8iNcOb^J5d=Lxf6Ru#6@D`>j}i?Y}x_BnU6W+1kc;IneznEyI@g@ zGBL!$_4@Cu4BinSw81ZI18fE882t=)n3@w-SC_iv6GHS>W zay9G`$N@WLy~@?xc!gOahQbSLSUa?UMI`{tP0jwnCw@eZ&2fErR7(m_i(quEdJ1MbfzC9IF(RK9jPa29PelVAEbR>N6TSS@SM9qZ*rPyjH6 z3x~t0ux4)3d*3invOe3?<8-3Ktf08Gb8FwhnbNrPnc@tR-*sr;+@*cz*IA+%m!7Tc_# zYyl-;4Jwdj|BVWuISAGP}WU z<% zY8;E0E-Y<*fhgy48)QpIBJhyykCnAWros!q1_&}(Q}B^Y*G*^nO>$BjmtX;{q%*Ib z3oKq1=M!v7AQ67;?#*EFMj4NMBM!qGDq#I`@cg=+nQiaH`q8Z9O$ekDE62EcAFC{u z&DwmgM_!$sSu_eF-%<&@7JfUiKttdg7{C`M1ha2wS@vB{BDizIVE942iS{t|Y~#_KAiOzj+sR0WNauJ39_PN~|MSqzjzRb{OAA_+0=HRAVUW zmFdEIy{Yrf5IXEloo{(9eJ!y%fg6rbdLZZX0yI1JbQx zXVOg#e(}=|MMZ#tU4ORAv#{&WsIB-$+YjwR1PCGD{&vp1!n=ccMc2#Wh14tBimsNI z7ym+kMLf`z(^f!mMG@(F=xqi-d8N+4N*aLfTq|Jc$>B3y#x%|dQ@(v z&UQ!=0Qp-t8a4ZTy*&VIX%b)}q`@=L)HJXWeF11JQSEOjOW4Q>zuA2n_8Hq$#^EWo z3pc+tBmhV5%bLN~q&i_IvZW6|#O6Mr)PzQn-`IS43QG9`-rs5z2xU`^K4_K)u3X4h zd$k5I$)*~#@5pnH)&y*wQ>!b|Yny69NebOF=dEBJvZ5vhX0$6|NjFu3`3Gv@`{y@R z+fr-mTGMbMLqnD~Rpj9TF*-7ESfH_Gf+@*8ld_E#KzrE>xIr!zO8M+BC|r2T3ZZ|@ z&lj4&#vMjhsob1x{eG-^SFRgN=dv-!+jIs9*eDMDtW596sF#NW60aO3%pHj7KqP}p z+;SM%A65tnkju6sy?1`yNWtaTOt!q~RF{H)Nes%}+*~w+f3zbG`y&^IHA!yocys~A- zk`S9kW`?CnQB%GO9HhOh?}a{WeDa zWmkdpT>BxfvHr|D7;oBg4bP4T9yF@IatI%watufumfZ?Z8+LNm-0Y5Iyt*!{!Z@$r|;#bXNJ9Jj!c0;8b`ow(AJ_n zIZGWqopFrq6%SHB^==}z8evf_Oayf(o4q&dc2siq@~C9 zju3JC{5 zyu5z4VjZZPs0xwzEg>cY=g7u6PV<9pR+^KGxyVaLV8MrC z&~O)6!&*~8V~34$J2wZ6SfI+c>tb1uij3^@PNTqz$hjlNDcPM$VLfaLWux#;Ww9n3 z%J7{EVLfafys(62;bV^-M^jGoyVK}x@eY~eTqd?1i(ODUlaPDWqq&*jr$;w+yZ&w-ZQiytciUj;}TC`+s`6mA~e6`{Fkp zifi6>#6bt}v4Hw|G(K^@E0mg*8pu*e)XvyeRQ)_7)jO1P-Ii*cIFtrB`04 zd-b;4hxp9}$(m7Z^*w)ZYiP1@KA%OB4fuV-$pk(+2-1(}yGxjdQ}C~>xPtjI|2Nzn z!`*4zjlbnVAQ)IE(1W-~{PbIs{bh&+JuKeIr_iF&?NaBVDnN)YHn^)Du06wy)PccO zxk_D%a|WNX3sV6P`x!XS(2MLM9SLtM=2zKe))f>bUCz}DOC;_tKE*u?=QjxsC(dy- z2;M8n!;YeMrvgtIL|8|NkuYxG;grwo;tVB`4~>#0JZ^(8JBryMl_iDPOfyDiD88t8 zc)|B5>)6A{r|{vT2lQzb5k?VYlCG+ZAy5vNU1JT!u$0>P)44e~)D57oy)IRQ#)#Pg zxX!l~WP{1iRj))GJ)tkF6e7%(GXoE4Q*V_T+pz zC1&N+fCDd!2#2c@a%**(A1qxP8K*kVXuj)hC^MwMUys4a#YeqW@gu<3+#*5&KbO6C z2`#+Xg@jWQz(?G4%2Yp24LD@YA~e3l%0(H~(2xY@*$?o~a=a*Zyx8M7$pIx8 zJ?Rm>n(AEUKf_oL*VCQ5lipencxmwRb2SNm((6HVM#iW)WEx3kWuxczLC#Pemnq|> zPZ5^Q@~HP3oQ=1<@KXFJA(75-`<$Ec3^(IRJGBFoHgF_o5m6XX$JZY4rb?o9N-iI- z_+7n?8iRO<0)i*}bd@u|fl&SFgO z;b(U%n|G%|aa{{q<0k^_l~J%jIij`F*OMPuil{SFi#TBr3>mLd2u_J@NcXz)5}Toz z!S0j;A;mL?^vMKTy}v_A&j28pMrrYF_i_(0LCWan0YA=YNLVefL168*B7vysxQrDX}~#4dkw+o7yB^ zyzOy|zlq#)&w7m;sxrZ#3Nk-ss(WU5lwL`8@TVCG0Z5-kM8s&nj*wXw=`i08_h*Ep zrE}t0aar`0aeAGc$un^No0hGQN1d9YFT$}Cn`ig|K5~l1u+m_7a($MYGibNT{B?X= zy(IXWVr;34p39L&G*>2$bL|o}lz>ulY`5YaVI&tTH{T6Bdsjz(8brofLR_LXMgcVX zG)1K+0d_ZTHKSS4#+a!CaK{n&kVXzK*AJnCtm2uSm?CM22RG>LID~wJFtE3BnLogT z1*9v4;T@gpQ5z8!wZ-xIdCZZ-Er=_~7R~r1*Bmc)J6OJ#SSZ$v%arDzPv);2HhXJt zDXm!^zR7Mha(%?jfha^tVII5z?wtb?*33C5kqs1XHu$~+i*lk~2uUjzh$0J4GNs4&Tgx6z5L4+)$Aa zIIJ+AO9;k**<%QnB}}Dt{-EHCg!$K4t_sO)pJ7#_hjfI*z|~`nx}zIm{^RdH$9AOt`^MF{(YVn723G?!(-*oMXmkU80B8(mYO^r2 z5-rkPa>)hBF)WRyyBUEI*6Lq2Lj9T`HS)$Ojt0gp&a9`78%gkPJ#jj__WakB`_OSjD-<-|( z04`~BO<<6khR40j2U3hPE+7{ffLvfzVN=a_CA-V(+r?_dyolYawCdnrSV{E`pvKt< z3OE|`Ap$IFIoE#8cl5f?K==%p*vmpKjU81;kHQLueKuAWnYnC0Pn0jk!v2u&I&f*K z0eDkeQX26un0|i%k-WlT|B=#Yu(84yh`^6E0f0&$-thl*@RLo3l1X!4e@Pj_3HYLI zX@4-dKj}wEfYS7(P%Iish5Q|f@>p50wA>#LhVWmsts;~_6ainbCy~odSJjd^9|MGovYfhQx zL_g0w=k>3CIoT-gv+*5*G}!12zc&9LZJV%)4zxv1DPnqj1zXwC;? z!3nUaZT9(9saZ1;EtJv+^)-}I7Cu87-I(P{iRlW3X4)p*u*fFg{fL@MH!v0mOlPd)JA5 z&iW*G zqEST+f_BROXw{_VykHFDH79P2iink52MVo%g<@gaZEyGXxU3WJJipX1l{Hrl6Pi2fQ7MCYu~t-t=Of9*_Wh>i;ZSl-*i{_gg4b93QK z-?$*Pw1^B|WrCKcxp~h;hRNt~kY602-Dz&-YE!?*lGM`D`SJ&9>i5ym?akb?k-M9? zeK|z%&ShE~uFiJmd|_mOF^_uM`{{alvV#Z$J58M=5f)DIljW>@yzs_JNu8X?4xqz8 zS=-X(z5b*?%$=F*a1XOh`Jk47l`_nZ#2SRZl?-sOSOBQ3{&Gq8Fv5_MG1YQb(Mp7f zB^C||T|7(V4~1PmP> zJd}}=_BqNcD({Z-`I#|Y7}s_hiut1ckm1_a#l<@;HGBC?9E%JZU&vi($F70eRtl&? zyp-|bVnhRp=PE4u79j^!PJnM125JWt#fVAd<&L=-=|HZhJ1JvZg%rT5e&Q+zvrySg zKDU1+4+YR0b zD5ut6e-km~GH%$^v5tR!dkv;O{Mv^@Uy#06rx+$b3wB z$TY=6YX?|JPc?pu?6!$AppWDX>JaHfPk`bE5l1wYX(B=LOI%e!xk1=wa_o1=H77Oi zi`nOoVW`NH`Vz`n;h{1+M%ijM4D`gpiL=|xXuF4X>PcvgEvJdU*Ut0?zg6XWvzo9;CzbTamMe8T zall8=8v!@(&>Yq~NPg+68z#WB0uFxxjWBB$o=JD_GWn4~lvqDI2&{2Gow!U;9;u}aiHefoz`EPDLV9_H8mkadj4JL2!AmA80 zSZ&D>02AqE!jM5CA6)YoD-eR_qzO$dzu$o zY6xpU7l2yDlPc1p2q7YrjE)ga^mrAi(sXrGsvSRTew}Y*w=92&Lj1#8T4Xo0O%SB_`!+ z<^)BH+5Lz?1+xhoIX9(87&M(~I?=jv^G4`-R5RsDVnK#QJKn*t0yS`Z6OjSY`Lb6j zPoaGfXdB62IKAsr;5`ygI;fD=F@c_cg#Y zKb{55=r3~Z_HsT&Nl52O6mud%s-;MOk@V5;!DWU-DGG;G{<^?tXDBE;!rLBR&bXZr z_E;Xr7eBOq6~vPe%+iY_=_gz;`=%)XoS|sykhC=HG_AW{Y%mz3x_VFfoIUB2}-76>R-ET2T{|1-?GQ zN2`v!gWsn_6dq@foV0@TH?@>? z1TRx5X+tN)odRNMHgd$Tv|8`rZKuOyjUjDA2DqY*{hcIyy(}OAneE*E-tlP?(WMfL z4c?ih@dUM?2SOxRCy)-G;xqFBI$NkGm;-hn7JL=q7Z{F|;w|JLY3rT(a}Wd~+#qFz zpfW>a@^RGqCR$To;RRhu6drUoH^{W1Jzf+!?^)}AXNtZDsMl;01*w-qyTHryQaoLP z8V}hxbXP*6IY~Xk@8l`VdmJ&<8t=<`i!Inrn7t8eo_C=p6Hg!}=K{ zugILnd#x6i=PsZk0%|>{rAA*C)Q7Vj{5DPF4kUB$UCK|*`NM+BU!}VNLm-S;F83K- zn}NaY5GuYb-1cc}2_Bg!TV{z{)a4XnAo%txS_D zmM#H>!4$b32I5qGETMD3GoI(;1G*al ze-UjP57-UW5~4{$s%LQ9AX@4!#Mgy=9C}AZZgjcT#stOJCp|2ss~>64lddL3tKP@W zu#$9TN>sK*KgJhS^zBZ^-=aeJgG+o*N;r~2N5&$$hyB@_5@lbRpuX2<{3K3N&pcrw zB}UA+e4PI_OCH3BV@zdPUlyjV4QabL&CC;|izI(mo>4z>-<acTie7a|nf8rE0~?Z?21#BhqZZA5WGZiu(imBPSCP zh>1%QmEm+SRGCcFhN`PWL0>Xh5{&u%HNNt=KO6~Hl|&XVLL4U3PH~&=AjBk9)07T=zbF~4Yaa}~r*2T{e zG55V$#N78L5p$n-62P97qT{nmM8cbeJ))fW^0H-lEk2&K@nR$%`vk6D;ApHYsdhZa z>G$`4h!#3jLQrsn@U5!*K;lH1qtp=O&tK^6zoCuS+IS9Vvk zTy(4I0r4(EYcfSI(ZNcfP;BC+o@{S7dRl7FTe(Ry^JB`2(BV119LST_+@d;Vui7x4yE~L!kRuD}0(cTo$3eULiHWmNZeT9K(ps!uo10H9 zy*OnHRbEm9131$G3Z8FGPUgHu#?bAMisfR^z1&fTta2*jp4l>X>^dd>wHpIsI@z)J z5=v^xRW0CRk_=<^rfvY0OiY{<+%>?i?fSsXwl8E?^bWSPq%Sr1w|w6;`SK0Ls}){~ zd?Sfxh@G*6#<%qa7Lr^~faG#Bp`&Fx-Ei4ne7MJ2nRCsYoTK!MqVnx43#`)Va)}cc z-tHt0H5~M-%&A+Dd7IW}M`^Z0r4R$=P_E(I+Df;{oVa;zF+)#TwrlUSTvnirqyGY? z_43jp90kMzUTFjeWs}Tfd2O!;q%x@NVZ{f8o*m+OvQj)<94Gd)cJ154mtz>Vz&(A| zZ;is2V+U$QUy(0|$1kWAo~?bJEvm)8=4t=0uftAIc$S}f^!Yr?LZecP?}SF`Yk3`g z^)Gk%J}QpIo@c#%>0`3P1Av6^wfT8j#JfNv0mnja&4g=DA5*KiJmvPFo*plHij@S$ zMYhFbnjR#gjm3q8vjNX+6jOMLF@pvS2rqnmvgifpuF|a9`H4RLcw-t{BlN;{#f5S( zbGIk&Wpe0DgrV4-9y4V}dV-NoPQy}bkJ2$?cBF=jB87p=kJo|WB8@M!CFd4^Cs;96 zU%?fCU5s_wM!qllRI)y5RhU5{`nMF7#rZVLEnpt_5XC)5wkMaXC_TEl=xMHg@-mR% zZ!Z8{Ja+a*M-ScrBX;*^pieRPI>h zgCWxlSj*k-(06a7400qZ^T5JdTL!zeD>Hl#cTgrdV<>77MQjz6hP7&Y3)y|s0PNiW z6AX;&-Hk!-!8#hY7kj)U)3AMtWQr+<3?TMe85F-Nu82D#1HP$Tg=xlZaAQ*Dy&%fkw9VZQ z6Lsa$vb`ka>lf?*sL>ETd8z2Dib@0pB3S370;$@z92a#P@cp>`Fxx@h!Y|#GISR!=_`wq`GQc+>wooA|8PKTuy(q8eBK7wyxrZS zcms6H2I$=PZ}xef?E5!#{Qu*QA2krzLIqa%>9e1+1@^vnXkYJ2>^2JP>HR#bF!;qC zNMBKQC`A(bRmIOv<`@O#>PSuky93A(9g|0IqH7%}L701R*2-Lweb(E_S12F$9Rw>S z!@2Vl9CsiWS={iENq~0q14=2I%&?vw7QFmt*T@m3z9Jm~+-Z z($z8>#ae1tmo=Zcex>NMxTmtXyQ=R8I(BxRc+)ABNp57Cb7o0sRdG@FvX=*xgo`DC zn%0(If3NvzoGcC@TJb-?59GT8_6Y)z46|Y^Ut<1(;{s9*VWCo~Fi4Ul51f{>(HQ{K z(APO!C=4#itMGk=iMzt}M8FEgtUg*_%N+_8$a4OeGrAmD5HL*_tmK_<(c?6%d}|5l zZ5RzAq&7}M4;M1qtLMa2lYGZ$1D+(m;85KMqb-5#FEXUDm!qP^Ft<(+Tm%K@&V|LT z&hVo--Ii=aNb~|DnP5A%?Su+$lX$YaW8jez%jEXFV3v31UBj__ciujjCFPfm+!q%S z4Mt-xqOoa4eJ~fHw^9s55@IRYA)Hsq$i;jqa(2x3HtYGhl z*FJYYjLx+;zX2`xE5H7iyW$KLnMq^Z-qu@S4Hl=DA>Dg>XJH)#4I`3CF_EBX?uHmC zK#A>qf$2mDr@iuE`0lR&RdQDz%p!!kd$hE^xa$?Bkc}X>vm#8KM}QK{`4!}dyNBk? zXj)DXnIj{6f$QPKnNeW;g)E#8_I#17JL}?%$O$x;i@qTjyMR4H%9qT$Tg20yEcRH_ z*s?uRpl@I{if((nwns0>i4P{MJKL4vq7F;Hy|SQxVA{6V8+4HUu{09gStgHkh1YxJ z=ZOv$j5NI?SnJOGJkk|xJ$JoDFWIJv#ge7nrJ&2imT^}B=&2cC%nRd?5iF!#NkC6* z;0A#K1g3V^c1U5LY6#5&!Nu_;h)#BOFono!|0PKE&Wd^Lv)?Z6eu=&<-nzGK7fLjoL+0F7E;_WJ0NA5LCSZ zu}z9m5+-o*4Pdy6l7ZbSy6XWNRnaYWnxZ?L%L{kC+bZbYma-T2(?u!4*cR^kx^rxt zd?mP}{L4<9Li274@)nApQi<&v1`K`?hTG29azxFA-`Vw2MxQI&EOonRr0_!kIe?dfJyxt(wioLz(XolmolBQya63)4c}m?>4U>$z{y|+c^W(JTn*?jTJtE!Ou*}Na>Dc275kWeJT7M zXUZCdllXTKy7)ipx3nK|IA8yty`PQ1LHWIt8Anrw-+Pp%6RmEVLYOuD{f>P5e*RqN zWkxPy+92+ScP8X_3oQ=b=ev`B{Ym);rf3^Yhax*d$3g%1TQ) zomTtcbZTy%M5+_CI9UfyLRU-H*sX=x?z@AC3kJ;bl~ zc>A2U8~k-cx(iOt^ULdVXz=@N$SI+KN?Li=j^Of+?plESWNF#l44|hY<~{=szVNp- zH;?1>VT6O7;{pl$O0g%4X!^6s4SX4V*7vc%2C0u`SeZMxTyq-mgk&^U+PK2qb`5sd z=BNAZeyE{!hxBs7ZT(y0meycBc1~!+sTGzL5OReBE&Xn378A7oTf9v1m|s<@ijo z-J`rL@p6vOPO;k#@wSVXQ@Uf77AXz*{T?laGG?Wg^Q)x!nwi$&7+&t_HlwCLidg^y zrgbEC8zG#{iWVJU8K5=UL?93cRS2*_HfZ5 zEUz$Wzj%yhLSZ)%M6&0_T)W?m_s{s{K3}%>i3=92x9$dJPo#t-4$}s5R&2%_T{;!| zsu+Gz)E6jfH`+Rbv@SPdH3N|^16!wY*3wHux$I3T?S#vd!+tThXoHk(qd$5!M>LHctk)yt9nB+b?1H@EX=&W@d}FUZ%$t7Kgx{ zm?~M9D;L+5o z8Vnvf$9t-aZ5oq~Kj;$Fg1dN(6>J52s%}K>Km|D)--E!M*}#y};o!1ZQUXRB!JyedO*dfJ z4>Rh`8oZrz8ILlu!EX_Hq(SolxgM@{Sth;- znTm&+dm0gW5y~3d2kxuf8YaArNHVPJaCyTLLhI88SccOrX48X3>13H6ujCSS4}EDZ z>JwV9ks+g<$uRq};T%n|;io^7A2>j;n3o;q;n&|A`=uuRRg+`L`c(|vl9e{qa~H4$v|yMSvVdmFHeP1 z5yV4|l!l{?{!lXROT+_ZaQucVcr^I&WFk>E6fF%0BB4YZqBakICH*_KR{H&bLr-1% zbL+~_e*yn|VA|^Uxx(YutIW+VtNMRxcHXqExhAxO4#&4L7~TIBUN^7*tnahepsk+< zHQW{Mqs;99Qjb3w4Ar{JL*C{}+V=ZP#gpIExTAT?W9JxL+LwaQIr0&20 z!F6e6zKUZ9W!saR){f9cme|VDTieA%yHtvA9Sw#GZywmcnUw8o?T!>)c7!B%WjTv) zt!)g+-!q|1DboyaYq}7sPV}lAOcU_+sT-*pPcB3a>6k#M*@>Lz1z%?ydDCxRXGO<3`2%JXAJrrVeBI=R zaLVA6!+O{3$mquGimZ2B{qGAh2u=C0*Umc^#QOd)UXSXo<#iZg!|od#H#)uo=t0270lJzP zSAQ3fMnKBoIcJW$y1R#);VHL*W%_QydhEvs?v!YiQHmrzw0a`jZT~-1%*>ouB3Isn?9PNjT}6TU|&nZx}0x+=Wjf63?&?kZba5 zRt&*?CM~}+)k$dt3zAw4(`1S3eFv86%XjgIEyklVeXg#JLf;e%r?=Mv6YB%K=6 z0ks2a!jxJGx(`0+ybjYf}(`zmr_7P~?6_!|Y(4##1%uRLz zaCsIcS70t>Zk^@psNuH$4%*q+0OuT_cj3r4hGg(c;0aY4*$a+YF#vsj>zhbBH6=aU zNpHtW?pI@Uk?AM#J>Uj1D(vbRz8RJyEw(38p}8eRJF)2tEZ8s*yC$EZ>(-ER8ZJHT z(XBc(E9SP!0=Kl5dpbXgPt2gE-JiuS#QF6^i|q851}BYFSucU25b0o^{ubir5!5|1 z`N8Z+a4=hwzQ%-KcUj}8BWWG*V7l}-qTCkpE)}{4i)r)IQtXL<*Xac{;JjJSHV9|X zNPO6{396}UU6*d~3fNl;M=!hzxx~jtP=R__#$C?L zyH>IDEz@Ga8T*@9>azz^zC$?HFU)|hYp`6IMoG$T&l2TeTQ0xlI9#J&#-X4)nlvCJ~knyg?ixfwTgHd&G2Ei5V=d^hKs?*uM4T*lf4 z;=urTkhy&S)y-JQ7mCAgArOv)(vf5|Rec~Ci2C8;5D2FBABr9d#6zK^FO`b=Lp8oo zD3XYW1Aa3KkBCsH!XGG)m4^FTOAp7R!LkSrxPave#QK9(;H|>`NT56%MVWzQBpmR8 zGxNoKrS}5esYq40f^x4~zsSAzh3BzTVzGfz9!{y7;?mp6Wg_XcM(`c=VK;(+6Kfeu z4IU3$ck#4x_AF+SaA6!S;4Y3=w`}M#87T-uNPT$xuAYNK z>(KyCL{SebXw@8a82i}}4-Mb*O=y)kE(}?b&968QTW$UcZ42AySJ8%bhxR%-@YzU) ztreG-16**sylC0AX_097xYp|r$t$=;b|IcPN1ULiI#-u4L*b^@7FjNYQA%9EW`R)* zUGzJUC|z;zG&6_Bc^4YRKEb<-a(ATMPmZuQQ(hCO^&9f6b4+;2P#>9`P-j``K|jeu zc&E@+X@b-f>KXA%QGIf~NwzH1(|}UsM?EN&72Z}AmUT*-0P2)4>my+agb~b0=~Lbz z<_!m9D)X}muI=mHL|KpY<5b6v{cUB zC*kA;6L6xY$$QOp8z|PP9{hrZH*8xkUpeNwk)6A17+mlV=T_nx!3krVd9j4RpA@{LtV|udlq7Axxer0)Pfh)f> zKJ4~9hHat^=78$fC{x|4!LOI75#EE!QF4v5`yyMd-NHqrydaBJ2ob*u6iuET&vNYX z?~D7asxWvu$eVw7;Ik&2%KpjejH4~XZwz`o2F{>7m&y@BreixZHgdRC8S-$)l-5=Ds*+{Z8oR!(MkFJtlcHA8!L^CkLlw-$NyEq~Ehb9NoY5+xQMF zOg`(KFWuCxWZ2_JxkDW!O^JtOD^(eeLB0{eO6V!|0PdGM8}2qk>{vOPote_HLYaE_d6W;=ux7tgOT-Md0H zy3zG)6GZ%ksQmY-Od+wFIS>USR?he$pE|LDv$w<@@e80DJN53h6|?G|3dj^ zil9k-%rMLIaRv67mxr0kx8F>+u|BWdnIThlg6s{Zly>>~;>icshZ8*c`)-w$cUJ^r zwR~T~C8d`AESrkoyd-LZk__kbt04QnMAN1of!lh4-!aN|z^GE5m{vUGIop4BlRRsv z4wn{^)5Jx?y@DeTJo@3Pj;FwQ#F$)QrBbu_nAXa}Q~8JTh8Kv~`0&~8H|j+#KRBOy z&tDx6#5flb?dj}7kuUdJR=2&eJ< zDw)m>p1}J&xJJj770HF)ZExw`iWB`>yTzL_R`>fvZgjTzRpX+*O zC=!kO{gI&07yRVCW5;}vs4v)&^!ec+9E~Sp!IDTQToQ@KmLkn1et$3mX=2n@lZCV~ z9*71am8oDf5&2?eAYN*gNBlwmD8MVD$svC6?rIvA(2iMQP+O9{dy# z=go)n-Zd%<&84pIa81mk_bcZBCWN;c98}hiPs41G3jCaLkaEpzmYB$JDy071E*E>Xe?`23iAL7RVA_WVDQPn7vh=-8&1sYq7Q);iKOfp z_`P54$R%g|i{j+)uvFIB#a#dclU&YUlbl10;JhPQ%xAhHrz z!&%jaq7I~mSx&J=KUQTO!)ybcuvW2w>2e^N+k301Mw?8C7rhD*0t!-2bE5vGJr}H{PAngTXMr91xoFgA!Itj|(%&|s=^#ysF``WlG+dTWQVK^{6TPv; zpogM@hhQjO^f?%EbXYD#_$Zc~a8D_uq=)F6QewQB5UN9^?s%7IND@3Nt7lcFm4#^Tw_gukPZhP9(^yEgj6av8eovg;0yA zhn`YJ6^;x`kTAgtfPd6HG^olQF+KkGtLEKo6@+ z;o?TZUE%d_O#WF*aicJ_=&`4?a@(^IjBcUQ-}?vbUH}ydu>jZ}RwmmP4*Fgd0(_~Y zTmbq27YU)fok1+pY$~Jy9%aS|Yfb{pB}q3E{0??|pd&b{lV#5t?&UIK-1p4*Vs>pZ z-^{&o_GQG9bdNfvnb006hi#xYLK(hi<#g=YvvML9zA+OBKo&Q*9UpB^=)s;nd|UfF zM+UkFdo0JF1J$Tv8sMalfJndE0UPF?BEw}@>?>cWt&tuD|60paDEPqLX7|dZ0d9bVPL24ZiQaq3q6^VJ6yu4vHA91;sfz?LE3Z;EjejP9c z;D?%Vvn;YK@>;Yc$-Jb9YT7WKk~uNAR#}+XE@i>K39KJVCD0%%zTjfT?v$6}_6njo z&ECXwH=utOW?&!+Ch7pwRk{Js#@fj|MJWe0!3To%slk1+7ncanKiP3-FW>E>%-0P| z8UW7Kx^cdETxtd*jLVTd9wj%`B0`w6%wxu^UumDv4&juF!{$|_xe*BROfnP*nQq}| z>&Uo%C}*KDO>+7*2(bLw1A%}RW*3>K%n`DkCn#*0DmOei(|wzFo&`J@K1kSSB%2`A zotUu*tb4W|EHnHXFf!w8^TFFj5s>*b8+lZuICt2PY-u258{OEJq{;}yJZt!iLe>Ik zk%>KqUnK_r%IZbb{nGCv!YO67JS+2A_Wb)Uw{6yF8+JquKP+d_EIZjOlD%>nIol3( zs-A{k_*ueV69-fHVM=6k*+bU9MUR%Y34be zuX9{nN^OurP39;VYFM3tu)au9nwjP>&+&l0WHofq=)-Kl&4)1mf&u{6Vz@b{LSRT| zxqI-SLEsO!M)C8CTSZRzT@fg>z>H)TOgf7{hPMlv4xd|ehRF9zQ8z8h*x+{&wMM$> z5^g*+b{H1IB~n=b_E#PNF=;b|BCt$Hm2D)>66+D_D4R6y-UY`O>!AO>2_dJP~pD9J`QQSKjsi-W!R=W}C-D8|DeEK(9<1Q;cb4m_ zyNaqq1rTZQ=>61sffVIUA_I=PsKcPeTxCC1B8X3(?Fpk2pK1 zZ$c{bJtwv$B`Q_6khL21Kr7gw4w|hoUDp8dU~ZmbojSgEi+wo*U|{wNc6-NhO1xK_ z%MIj+-xxF>(rVT$JB7vTu_U_A`xD~^@p>~`Ge~BJq4c6|b;6yp_;PbE^E#yd>%<>O!q)Chtn9oUYT6Z7|suk_trkQm!3AZu9zv#z!+TYIJxH_Hj^MW&*1l~eOw;hE;n2%ZLS4R2ea?Fyb1wH zSP3z?f9Ue&J!S08rA%`yDxKHnORVi*J2#=tW>8)`7vWygXBV~irCj40$bSYs6pUSz za73zliylNK-|yEWi56ER8nsOZuHxalOF@ z{bFu5(#EWZxa3Gl{S?4?n6#c;V|JvTq*qTq;;Dp1t0xuL>rM_J%YqrQ^*^4-II7az zV@eQsNv#7n@8EXO&{hcNeICEhSSH4En;X9Ly>DxwK`@E{RLvyE1G1c01Qr+SJ%+-zkSicP(w)ckscii z2jeAek@#3N;SZdT0Uxlsw4@{vEvc{fR|U#_0R)-xha#asX{NR;kSO)VE5hZ0U=Rrt zB`{=zCOp&-3WS2thWkt6k(eK7fY77+8eL;Fc>UJ z1QF3D;H!%ysuDqeEQTUN;pz&!jRhm&U`Z$x4g36oKmrDfu~0M`kH@n^{s?Y^0e>VG zPr@ED`oo6y!!GTcZq2x2cx(1~YrYlzzmGao-u5541F@$_8NageIWC$#uP1vO_D1dL zX?gvnKm2EJ6EY4X!idNiKhNR0Ip?vsx;_PuwkeVCwB(=*;4#$+r*$O)$V(f=D;Ba8 zxO5ZTs>k*~7jQB7yYr-fUxkgaJ#1Obklh|cS;nIDe|+J~oYd=i-|xME6C@jJr^qQM zHimF>@%{qDBrCI-ocN#_)jX2$io!xhW?_LME*Iohd16Gc`tNTcD$c=dgsI{nFJEzsS(j*iqYEWc;Ua29K zIv|{vHSf)JsIKp^#+zrH{Q{n|)AR8^L&D~b{pR~_O~>JVpSjO{b>CMfzob2F|B(yk z);nq|y7#$T(HrBc^}Gr6wn*bO_yf}baug9QsZJbu_n-+ZLs*2+*8m-4E}L?t^O*}v z!R}lW$klwMW$d2ncIGSALNFghQ*9BV7XMlKnTOH8! zow;~ruaveT>)}#n`PmY6OH;ED&2NuYrB)5}C>p4AL;`sNY*sEjdp2O3f{RVYlEn`! zXl!=ohRayda8l{D?F)L~-z@@iAQvdWmBMFpSc^xMcnjMzW5olUY%UHM^Dnn>+eTS0 z;8n+-%)Fs1x9PX|B|RX?OA5K@`3CWBa*(h07uQ8^P}I%&#b@wy`6uA}O8Dv9F75?_DQa16Pgu`< zzsmf<+#bQTWH0TdBq(mipwiUZi`I@TIhDR3@No^q4up>0X)3Ut%M&`}+DOVjus*dQ zx=3sCPyQFDf^PePcb_wF)bDs=Kh}b{M6%O-J@xrJ&6}V~ap>6#s`v!zH2F@^jZ@_2j%>p5h%jDmLCL*FiqF6Lu;IL*NxPIjOm5lX%(6|FBsd$obUG`r_fVdn0&Du57v@YQC=2?#Ss4&8aep?L;SlmQg? z7V4r6h9JegjReK;VxS`zVilqZfQT1@7UZ!Z)uD?W+lv9_G58S;LDVu?w0yp?4>7bb zbo$(36Qhjw-kkXsEk~f-SXjzHl~F`)G7Gn@z8LPe(gQ(~$lYz<5$%<9I6bkQFR;tM zXIr%mbmE-RH?lKTp2KgsR}hG>kNSJk%><>|#X=NvsM7=!6QF5V!kr(8Lq8}9h7|Ze z$Gkvvd7>ad@6%-n%v7A_y;6W89#btOfu{FLfCXW&eJB^Uv?y)EcB36>HwXc%f(`R8 z_GSO2jYQnBuRnG`mCyzQk>-8-AZ+a>Sd@Zgq{`zNWy#O|f_XvpM|QD-0&#ykb?{Sx zqA+JnSS4Dct>^q5(c$q(4f7Q5I`gI2>41DbJI@e& zQ1~mimD2{b7w=FV5{Zg3{T|>)@;waqH`J1y*Qu^r^7#Uk&)*C~sk7BYHG|QJOGI}< zLatOGD-!kTD)c*jX6r+7YJX4Qh+cJ2*N~l}vUfg4Eok;0wE-^OZG&gRL66P2_)Y*X z%^|~W!-CoXA@jNycAi)~)yE_2wC<*527C{IQi1!VlU-PyG(2LJhyl(h_=;>o_bY?P zN!4|9gUoiS-oJ%Rp6n%PN*zP6w1)p|NcS#5ePh=|yO39Pa2ca$bpbkC+OE`@;xu$a z_lOOnG--i_CN-V1E!&+UNLt zQoOK-sBRP=h6@WCDylF~Ob4m_Z%$`5nvi54i<6yYm_o{@;I{2w&HS9 z*B?&Kp&iF?BbZUQ0C9t!X+$Oy?y*pmj^R}Zs&u5HWA8M}Gdm7he~qGAduZKJqZ^ok zO9oT376HtGR4wcZ)-<0 zE;q2$#4Bj?0~FGHlf7S?G~oP>r3V4P*oa;|`Uq~KJA6LH`ey`c)kjn{vsiY>6#YKVn|~7#dj(llv6{tiqdBjIsuGV+J6%uyeo0 zLb``h_PVY^b&0I}l8p76%$LzUIm9{OVlpW_WphDllzo$#RwOHL=YY;Ny8>6H?@}i^ zr_nK1S#ebu`omd-NZUF_HEW_YWax{Flh0L9TBKbY;DwY}FP^}gf=ZJ)0Xqo9No`Vg z5a$g8+z^dRsI?qJ1UKM_q~KrjG3Wh9V)}FLAV?^ock1Z_cy`zDqCsox5MxfOIk?bkaU%)%?>dT7`H!EQyy>w`f7@ zVKuYN4`V4uba>mNTNjbV97G7P%K*>xVW{t^$XF%3~a)s8o*b_`)qSwKYv zp41ND=g|dd@+V;ckmmC^EnN(gHfhVH9>x>+gNA|46|;3~5O)h4Dp-xh6jspPnDsTZ!rRHJ8sko5 zgf(;m>|h!s7sNxj_dih6;;4>gN#@UG>(`K}?QjDVVyyjZOib;pN zHQe47_iXWUc~|$(B0@tRUEq*FMf9K2++f(LPyl8Qay-U@LBoZu6P(iiOr%wY?gT!n z@n{8HnN)l+WwCJ4>$c+{!0!eEJ62%+TSOIVJdi+5Oo~ZTf`aQmVQLyS+i|U zEJHBMU&8;)El#@ZHLpY|zKfS@UXM7`BbGJZa_7uG@Nvq%3c1`Wr~#gHLT+Fl((xXq z7PuQVB0B=2qhtBP1>+n9;G~JwC~iln<*zE|Xzr((Tu_WJ+&=t_EpTHh9d{zdy7gBW zg@{-T2-KZeBb@SCFaPdE;3mn6ElfloC;lDUxowWIP*@3}L*-{TRu6V4J1FSYT`C>} zEPkqy&SQFg5wEWb3{OCqiqawRFkRsn8;GrpuarGo&DA;@0d$KQTbb^G+m?A%86MIq z#5~CF$$qfIXmAEurZsMISX&;!Y-SKze19ljkHp>*PW2CI;Pk$3OalE9^$8>9Haw4D zD~iArcp@`vRM(Y#U?tj?1{R0Dq;N7gnQCD#h$z-e8?$5;{uUwHOsB3>JOTqk-o-q+ z*zid-)Br+Y!-!8_xVg-?k{dN|B7!#eX_j~i9(}lxDJ8Qm2(#YX+Jr%ii8{;Qaa()0 zgvK-zhFgVSz%t*2`zmVz@6wHTSYo;EwxgrjY^-J=#P=$+d*F zXstlpR2V=xo1Vv^6q-ugYq^BMk#qa?O+5)vgiuc?RvQU)mquf$SV>tt73-)81=jsO ze@!gltMvOKF!;y>VAJ6XmRF?06$$u_`I3=D5D_Y2>Jf;P2SVYxSkNCVjV6PE%FxlW zx{~lvMMoPz6`BHYMXN`wN`Ej3v*855s=^@@=J$iHeg0I~ANHprkw7FGiTPswvPh_G zH3HAH+CXhAQ3sTUU?LPu1xlmuSD%VROQPYbUz{XRX6&NzpDITmM6i_dCFpd0%3WndoBmKc5U&$$;SCF-eosb0cH z;b^+W{VmD8c%qd4%oXR|bVxoy8(Y)cq3i4L<1#mES#A?eSrO!QZ8jzBxfnZRk#x3s z1I%>OYc2j50v%i9Ujkrc2{(1q#VxTWg3Btmv@6y(kfOHpRZtPvDK_}%0+9*K6I>m~ zU7nc@8V*m(wkWVE8SD3$sn$I=TNKQeSv0r4GWi%jqZg3%w%=*}Dr!zz{}IWP4bnWO zYUZi{HU!sDlMhy!`8Ow*Fuq)Vkg1jOa4#!uYTZXk;LC%CUc{y)I|2JAwC z^fHN^UHIc_&A0IgOe2kEG3UhG{S=~#!&V9?d*3^@GDCPae8~;ulr4eKfN}Igd=59JO3eeqsWo^|V||mnPF-7=n^aM# zk)T<_kr}4FSi$pqPh9$Bh%8YF8+qDCgT6y(T%}*UlyC58B3}2N&Vt?Nj2lBJ{wZx}SXIFWQK;nx2Sl8G-z6EzTM;n`48tMeswvt*#)@haK1bob|`3uf_mv{?3~9 zpYXc_pn)rcpB)AQ>*%6%4JX_ zW6Mn`<8C}@1h2U~B?jNh;i*~E0On%~%2-qKRQy19yd@Ee!>}5v z487VHOAIw6%v3O($i9e#kAy~R(v`l-l29<{_ay>8*gnSn{#dxaDG)Dth$m&f?lK@3 z1$^OP$Sj-7e%Rs*HNz+}5R1m5Kl24g{gFTa!WXP@@#_j=2Wy1buEpIw`2sD%oZB^OF(K-FD9&a{?|@M7npn+DHkQ z23X0Pcqnmt5)R^^OakQ!(o+!WIV3--={_y*qqd@Hv#U7%h@fRaGv=`o;MV#@bPY~% zivUHVAVe1J8eMw`2sy>wmC`FrqL-gFv}GO}&Y<>jSlxrW`jox}>XuRiSxs;ohd5?x z85}`V7haVg(-2w~j{ZpQ^10DX48UoApB9zk>z3S z(c^gAWj#h|m6=(JK*$WV=^78d3Z7@kfE;%Tivtf2a0gmkhF!8W9W4D4y+g#<-Jl>$ zJwGi{Hu)xGc@BGdxc+e&k>%HAcp)iNQRmdLCJW?g6nac`@t_=w>X4JCoq5m{why+- zZ@?_xK1btQPm!$X3SifI0phj3uS{qyAumARFnSl*f1PpbE*=iobMbp$&jw9Xy(8}NlZif7?Qq*P!(hd3p>sa?JV_{4NK4 z*g@+v{MrCF^7v|kV~AHom@^j=2-M{0Fs{!rTbg6woQE*_n)YFOwUO`C)>#O9S*+(428;%vvSCqjZt z_%#KOk)=7L;0!ni*tC^}7k0nlJPlNDb5mqP@MxQ!rzj#t1-21CaI6>z=^8JdNdpv)eur5hQf==vHo8>WI19AKZpbrJ`6(3E_? z;L`6uAzzKDW1U4Wv}NSg0gmOd!`Q!|}0{u3&_`U_!9cQvDQZ zf)C;(wL+XrrUst~dKGi#RKFw3^+70_9>}?v_<%L##1qE=eRmbb_i)#_9}~nF4|(rX za&{UZ!Cz-%B0_@Q;4>V8u{f7MQnzu1`oKl@Ncf8w4>Om*TF%~A znt~o1uaa(WFF+@dObC^Zp^xAwLNcjmolR~ffwe)gAFt!t4Fk>}5W>oK@*$J9lLK~g zv$@GZ8Rg|J$6la(CC8KV6h7t-m|C0HkRw68Q1LJsK}umm!LA@<~L+$@U!Qlim!0N&kNfno;w|#)-*bz z`99?;pk5iZGo0uz1GeWK&pgv)!aJzMGS5X~Mo40;*=!}{o6T&7Pj}}0UUAkEy#@#D zeO-SxJ4+n+-#%l7er7^jxI=1x;3E}Z<~UUy!)1;0&*en(ybUR#Qcp?;yB+4LK@<&pMvQj^=t5ZNjuZX3-9!WU5qx-=m*Y5L%5sRdz^@O?EZhg>s zNBdFCf}=AN+O2PW`_xUX6Bv(H=bdrwDvm6_@cN=QoN;hZhLj&Y_w)b{8ZKXx#Aivh zIC1A}Zu4?Nbxu+dS{g1N7SOQ3e%@AAy8UkEG#yOa-P$K>iYeG=hz5e;su|?$O)+&# zB78!i*5odAFANDSsag`Iru|HRFDlrTsU|rtO3;v0(@}wfO0lApV7H~PxI0ph{k}jt zsEU_5B6xT_?e+^~X6iyugvjivHjiIF=c{M#T0#3x-V{(bRc)qEz~fT+R=(%1?J!8a z(LhMHBiS*Q_yO*YfJ?H*xR1eokxVbYKERohbx2!c+(!nfL8{D(&z??BD#j&HiZxD{ z`=rYrv&z_UUpGA6rx380yY*v!B2caXG6WeXMFqmTC3V;O9Q|^!9kae+FQyC#{26Z! zT7QaxEXjZm+I)&4R|(!JM>ZhXLF_e#XKs7hBbQ<#(1Dm+C^762YI>oLVX9Ky11?X5 zfn1jP?_-%*A}!R|;7aA4U5OJaUQ*fgNV=fOdiM`*Yk|x+#*yk1QO7lk7%0TKcZdlE zh^>y3IK~SCQ((PkC%!9uk&|7N61Iw$6TAqouo~r07xQ$p2?}ai7>G{sa;IEzK|~qx z%tL;mI948D(f2u02f0!l9Bbe=o|e{zWTB9uig7Udo-j#?ImYCIQ!noFliYp=M`M1 zhbZ1zV!72NxCmLvrG)K}&_M|uQ3qyz`Fd&Poth|-HujQpu9tswyJlt^+Ik)``RaZV#d6*FsF@x+< z#v3k8Qn+Ae?o3EKEzkSM!y-&=B>&yWxg#*gjT8Wg>=x@EH57=63E{z6G~h{z3%Cqe z;K^(^3+{B2x6gfnJLL7M7^$i3g$TuK4WY}h%Zt%Q1XJQ}i$pVR{V4{bsa(mT1MJXt zVDUmbVhRB9Sc&C6izAAU0`~MpT*B7((A#x)Wo0_-mK`QP5&Jwq4(9oXYv}tBKMHp7 z<~@|V;M2r}0c2sGw#WDE10=hlyB1dO6JJ7c)n2e%PbS8-ct&tb)8y$EJc7abg2}0- z9Ms&)D|1kU<4{k9g?UkTt%}2qt#N%qWl**P>TDI&iIZto6u|tI1WUV&U6N-gbEp*E z^{OjC)x>@C16hb4n1(lY)^^Y=ay5pQoaIi!h-V$#_DSaN(tNAaz_Fp27^GS6gS5>R z(w#GC8%c5)K+KIleGw8A8Oa(FsNTg@TJ{u(yaY`rrz5>4D`|(J5#vE&!5=e85;!SA z#lOh$K91Y-E{!NIN-C#;7oWt7Cuq>KF?==7C3wf9(vX}_hdlir>)RN~GLb5#=RJ7k zc7&YRt9oyF9Rd7k4u@(g(JH?u;L-JnC*XG1Al0eA-4>5Uf(ak_&_G@Fy4gH!*2F@I zcx7WG6^tc;9@WqoC@F1-HH9nU<BJzZ)lW?l9 zj0D4_5&VlLL%zDoV2M8*OO?dK!QfYpVtGt|`?sCC!s-fvUG0WUx6jo*wQwKiP+LdY z=@rENhM5js`FZc=5_P*CmnlxO+vhnIuW1@07O8HyLU0t?ePG!6?KQxdm|S^5_;Ohl z7eR$fh{FweCTG*C;hF$uBn(&0t*flynXJ$Pl3-q8;fR2=NMxnFuyTZK){u*ZpQk=2 z|DsfLK`=-Kh?2u&!MBcl6++?+7po5p4{70SigZ!u)pddB#isqmW2{$)9)tL*_zXF# zl|ud~Ks#KnC&X+MwSm{rJvg*L*EvaaiQm0~x3|57Je8?f#TI+~IHU1pJ7B~eM%bA_ z#@fTOGVBYY`W~}1&M+Batvb2CLrfh7op_1dM4B|1=CYI~S*3L^LZRXSNQQK)C5CKn zz1%D@V5hLKhy_ZvPTjw-q>iulvW=XwyU%x_BG{Sw-QEUwSq;Ac)&(%~u|MFuoM&d| zI6I{~7Dcx6WW8cHdif<8wt0Mz>)d*c8Ri0`_|vfB+m2CCQ1n48$*)w0;G>k<5rH z0w#=$vx@9Qh;dM&_Ne5rj6{%Ksx(>pJ>4TN(4aeTSl^|T2`Dn$veIOMo#hBSvpRVn zJPJ<_&|AZ>(>;yYVT8+*1wI9fFa&KCI;!wM^Xi~Xd=Be2Hjjel{sY5+djV1Eg5MjKPg zk!_sAcDsf&;C*kuSU9KvodPc|$JQgVwg^b{VMhjq3R5A*!s@~S>?VbF&++FGj;f@Q z%Prns=A|wF;u6K?_wi}ckVZbA;zhC!vk(a%Iw~}EiY&T_xDezN=i)^d6UgD^ z!%LaECnfbkmLr-~nK{DSOo?{84lk~XVa1><0RZ#{QOhTYMpYU=Cxu90vSx@~*-z~( zahi3Wad<9rjQO}O!Y5}Xg*-q66G_d-0!)5Y?geb;1dBKU`!}d&W@c>p*@W)2{$Gx1 zka`Jahj2_ctY5}bS$b$YPTvwJ>5lnfz=1wnLRkl)=K%%bKuemuiik~E>OlfB)xFjq zp@>#+_)T92uQLJ^FX&D3)VdGm+0#(Oap8`@>UVCIDi-OOew`5za|_D2<@;F({yXHr zR$ard8(qLPJLiM|kD8woDB=?3f46zkzwQPUnbm|mgO0fM6m?e{C<}+NX*|1pQx04` zWK_%&8jTFH1&`P@B6q8Az^`YT4xd3Bxnz;=*7P}Q?Nnd}p-vHt$2I3XruStQrCa|! zO7DsoYtNR^_)Rfgfc2*JAMkkpeo%V@lT`~1JVF%`@FJTQ`Pf6N^lKAZRn+7va1ZJl z^kFZ4KC}k#e4xyL8kp?eDLfmX@uB=$gmQWj@6$JV#JS4;xo&VE5akh*d>r?ymyY8; zNf{oW;5W#4WoCAA{kc-mBwbEM9b8~4#I&&$TbPFDpxClp)=h2r9u6aphH_4JXf(mz zoWZZFI2KX5&h2oG2SZvei1KG#bFQMR_+p(#7_=^~#!Zi*udh&BFT{a`e4cW|v(`Vt z7j#~ea|f0nY~@0)DSm!64NFh5~-; z-=pMVN1Juy3phtsh@rhyQ>N+IK^O8o$dWbub*T79V2A|HZmWaigqoqulAlq-HNU|a zO}6c8CF~AVBqJG7C+5lqYN)yh;5F5hn?zpPs$paKMJ{Tb`WH%d=R@=u1*wOWz~@s+ z+gTgJjVw)quLkpvq(II$oYp63Q>)lwPm4mjh2!hh$rBvp_aljl&?i^}!LzWYT z$yrXxL3UN1)QgpiXqp-?AkPB|WZ+9d`revl&ak1+%+d^)K&ks4PYV;@oHE-+iVH59q4b!G5PU{iQ> z7>T!#6YXALPd9P?Op{VCK`~ByWH~N@^n?yK)5uW0e*i1bJ09)1Fj{p#WFmYHnk*-hoFCp^P>MRZ= z6hxfEvkMr?pF^AXXY_DGAQB1JRE8o)qmdxw$QMe3?Z?8|j&Q67;><)a3cJCuuLF`z z)3sz85q|&zYsjNR;j58AIMiNt?ZZ%M0CA(juu@FMqW&Q48$-Tcy!1ySeLff~215^F z1X&GhM@YdFxP(LDKoVi7E~M*Ag26x_3F}CI0zdp^sZe(yRX!37*TZ5Yl92f6)i&SX z=Ichh>(yC!3}Gdy9|i|4j5!)2QA>$A8jq{gc)^5VLUAy;g%u zKP`3-Xj~inAZ7wEy;x0&tgu4F#Vi2~T7ijM;|V^jYw#+xy*6O*Mw#N&!paP02^WYqK+%p+)+CsBw4bpR8qFfr5VX1mn1t@ zGLDI*^EFP``#Xo_m)f`ax|6Ws$Z2RU$Ah)YQWMVDGVI?mO)6RwA+@%oK4|iZs?e=*|Pls390{AYj zB#1c7Bv^~axj&@ltYwom#q~;WMHrAHQP$!Ey+{)&uE!%Q89h)QsUuNGo<8NDMNV0Jl@g?9qZN2hpff@hsxMr* z6^|MoyoDcHwfACi=$OTy%+c^0^uS7OODv|qN6R$euBw?YBhl<#BrLr3Xz7BXw)up; zI3A7Si^Nyzd3(#@SX4W3d@nqZG70(HIm2{6Bk#De${u<-G1zZHtDzA*l%xNk>4tLXT0B-u9(| z`sV8Zg}1(D{7*?n+LTSd4zGF#PBFJF-Vj?)8~UhS>7?P|tc9xT z>dNCvi|f6{sBCkMoIgpUG@9_|kLe1F57SXlH*8 zqa3nQqSGg1pod!+w4cj&Wh6@SOeHBO)$%xPytdK*?GR=JWZ!A+5KkY62#ZeFTaZfB ziESK7?k_nC;e*iO*IVLH-iajViTT0N$2YE&*W?Mb=p_gz-@WrrIB7xqYg6NaJ_-?h zdeQ;{ZBuEE;zoyr?`|u{8J-SDpW{bN%nF}8MH>#_w!q8Hs?f?{%#@;BE7(lEuS2`q z?rWn6ikmY9$q`9AX1h9hkh4>|kYWyY5Kn3&D|Sxq6|c03}2v64M)3fe}uG8i1k zlqr$RAx;a+l!<>lga~x=2!dWr47q+syqEkw6EPC-j`y_*+`qiv<5FK$Ou-(0BtW@~ zPJ4fY0_{Z-*ULNH2v;N+go|9&P+~2GyZ%)5?gGjATDx;xE35AIlZf`Zot(x zM*z^WDDtbgsAyHDA}G7?V-+Qqc|D&hsT6|}l4TTo`Pd11zjEzer>i1xPcqL5&*{JJ zbOpM+A3qAO8|l~M2fSV`4iv?PPU}@$%-9mrB6Y6_h4%gKHv6$xT9TEz-FX|4_T?sr zQMZVsjzzWVeNvHP1#tHoK_3W)AFw&H$!o|S2SfO^h`U#{Q3h}cHlW`fL5HV zSAU(g-B=RxQ>C)E=jXh?#{G-Fi>!&upNRje)z);{AxBsVO?iUfjqwUw?OL)pFrmjw zJQCR}(|02j9hfs00Olyse7n|VklAJ{8RR+qT9?YJl2)GyMI%_Zw|ZmP)eGk|owr!9 zfC)hbIJyZG_&2$HN__p01nlz!A|dgyl1y-Z6iUo0(o4G}s^nEEVcl#DVLgWzM)QFo zp1U4X=%hwID^?&Te)hN)%c4ZjW9{m{x}aQq@lPvz1DFjo;QatCtLpZ%pw*c0)}zN~ zg8})@pc%#6TM1UXm5{+wTorcRI*yUY$s}J5yUyt%MxK_vGUFR36~l znrtqWNTf5V*7nM5Wj4Dzy}hO(mC2t?SLK_M`DAr2UtL+BuS-=|XAfczsH?5bA|&L= zqLoeNQu#`Po-(;y>QkfvVy5ENc)O5-E16B;B_mOTKSPymnO>xc?y+?Ca0^*#fy=GR z#N$mpUD<4PRi-*qlfbPdQ_W6L_pNNy31>r*!|z1AU;2wb7A*X7p*~O_8Tg4^?&?hL zq8n&E@cHoffrJ|Q?5BVDYdwaENM@y5r7R-1dO08I8yNoV-M@$L1lSj)8wG9@M#|~7 zMgYVDF5{9gX|=<`c&))T+CAMxg7kS2AG@|xPPiO?5#TfgR{}+SOMy`m1Wouk58hS; zJPqMZzr7BDsVtK_=Itc_PMMt~zx^AU0TM6YIS3rigXKpo3$+y>wz=nGdD*1d?%vXL z&{9VFw}JDaul5s2y}dBVDafuwc4~hd@QrX*y11c#*ZWNfN+oz<5HKH2%r0$&7Ao~E z(0WG)?ByWgk#xswdS4m>;raRY^mRy@4JCb0pwfV@50~Es-?LtTP}Xa-W>~eL)G}2z zdMee`!HlQ%J>9DEW!~g%-^bu?EPhY6;JL-gf$bZ+d1Ej4T6iaH z1e;BtW>Jf8sak+ZWq|4R z<-}P25r$mQM!gsN21ZM>V`RWblhS73b8zb~1^jTsUnZ5G((-5fT>ClZEAZK*X>Qt$+5~ zR~NPVm6U3|l;)fnRKCy56C9F1Pu})+!4gpkInSPJn!jl_lLTn3EozEontJ__b-13l zPDH~kG5{_bKUx}YK=~kJWmK3qe7oLP9A(JwUOGBPDm7cg16%vIL)7k0qI?@TDj+ok z|F?c1Q{Xbso;NJc<=HzBB4UJmw}rR7an#ng5p)_`{G)sw!(GO_D{S`@qJ4>Mj55-_ zV1kMm`w(0uR|iQfZzm(g@>Vs<94M3Mw|*`oUV23dDd;WVxRrrdez>=r& zN)5c$Z6l*wz2Sy#r>2(#Y9(ezxzt8Bb)Q6bTD#$@pj?Pa$$aMUTJ3;?n_KX(kudIu9pd;{Y&K+=O?i_FY37| z^0AZubp7$c!j)-2%+@%&@rB6(;{1#>DvO{APfyk^7Zhay92)TF53whx9J4aI4QH5Xa`Yfl%RVX$ULp8#OT@+p%vb#fB)&$1VTZMZx+VY2F=0k59AaHMc$ZejLr;V|0MV&Sa5zSn#*sB9R_v_5d#Cg!Fd z&Ai~-M@9?fZg@i%=|l0sQtv&R1_ObH@gdKFOPP2wSU7e0$oVaL%UR6Sg;Uu77nu9n zA7}lp8D9h$d2vzsIv?F7=cHncEq&*P#xGhk82-Y@h~DFOR;f+>yi7pn@EOpF8GR=@ z-on(vv-Astuj;q}dK^IaG++Ug zUmCnPx8(mQwZ=MFL&smgU&>vlDduM-eMpvL{9nrRt+;V^zo`!|O;0kOHXlGbh4MdJ z++8?C#wI9QsbRgBh&))nGd>U01!%{DKSk5DwAfb|fGHqphPtFQDEh3CApuT90SdF@ zMFxLSiGe7>t>Ilex6yA;2%i7WPd_TxuZ1zY{O}IdPt8n?TgBxsd(#W31r%?;wHg`x z4`H5F5=u2#IKn7_2??_>wQx;6+iNS2gZvW+!-k`P;m=Venl77a!U>w~6=Jzx}U&^pug9`Y+N1 zNX#uOm5Z+2Bccw@|nT?rOo$vEs{++5)7FEs#wQj^3~p=%CpWQD&oh{Y6FIq|HyXhpwHx zJ6O2DXZZBX$k*BjY8x$m((c0H$puA(0Twzlf%{mYm*oy=qNcftNfZ?mrR7b+x!Gm5 zx<^mS&uS)<8*5;A2NKJ~1@0^@@U7oxo%?A=)<}WSrydTX0Wwl^EI@?KKS^v z@1toN{_OXDqN?Y!v47!IlrXF?jEUBKUWStOL1UpVI9 zF$RFUu!#UmOI90#dV|~h21MS)xedj3jk1!Un&NNh_Tn_wNb)R ziS}QEDDx0z9+C3(vL$%k&EWB_eZc4t@(c*dV{2)sUw>vpL0?0$Kv);v=o>UJfUm#t zdq;;nFQ9NHl=Ka3?HxVYCqQ`;SxJ4yGT-)(e&D~`P&XU|I-imlt*;Xx zFjCD?f*ut}qJb-xO7u!B)8#qlnKm^kfi`|AL%;F4wa3t>e6Pot1`>oNE}KPs0;QX= z6{W8(`pD-hvvuGBuOEsA6r$0^fnKZXIqSs`rXP|B^9iEiTPMfp5L4;s z05Tc^eDO`QcXWv9qf}Uym3;gWk_^?2mXV{Ue7N=vqsyczOVvJraLL-Zp>m-vmrDFH%b)|Gy0DhYehHu4w@%C>N{`*LI0j#Hke~8w?B-us$ z#}%q9@cl_;hO#-qM)S7$sH`K_QjK;w$a%x}ZD=Y}McOROTJ~B3mlv>vY!`mft%Jkl z^DcrWkCpr3_=FOi7Y?nbRPpt1rD-eZ_u=7ziJA3`?{96WX+@@3!=~>9BK@r;nFmFz zsRrNo=1*ZBOfE6r^z@hM*XS_gj?(mdl#seoUI;U`*h-7$h6d7n696ACFSdS088Hy3IX3ic?^#~AFgZ7{qkpH51YTUg&2+9*@C|flgwX`Hh(zxqaBmm` zX)?DBOg@KjEZ@vvr%amLFP*Jl@m7Jc%saqCV9XldA0%(R=a#QC` znc|=8N^V@o+H-c^tz$>p&PVLnvwl5ici**`>|C2&KP)qTuI-e?bm#2Hpn1ZZA63rW zj{H-42Z0~8}3>ygR1sjVkzzs$KKXMO>>%a%)-0#-~esbM*y;p}SurGODd120EF z5+(#e?w)Q_ZE=(z?^knJxWu8~2|jz^`Y!k<{Rjd>PaCZWE|!thc9_?+Y^c?s2M`;J z^Bh0+IH4Ev-!s6OfqZy?PjYfXZw+v*)J2-yBxqV%p%(uCC!U-yb zOU@8JWRQXSPMBZx>KVSp&6_*5oDhI*nFTfX)yG`!vy|#PEYWV+han*kv3Ae-5H|?V z?ZL>O2x5(1l`GRqwb#e>!^I$O!sQ2milX@yJoR`t2e}EBoho}HI6PS7?xd{iA0-(A zH(Y_MJVFRjxU0|9orPE=VoMeSzxfgPSzpx)_vOuo41jl?;cMtqw#6OqhiS#tp0(J) zt#WaAXfA^?uXa*b-7uG%`Z6hR0IZp8p zY2EvJe2=-5T+-xl4FbM{-~)ft^4+N1OGM2613IcTaLyZ~*1hRac+t;!FYnnC-ueIX zoYRL-GCY#IIaN+jz$Ql|0d*AkRMg=3vS{)x zYn|WIRH)gk&kTkgG*@d)Z}7JCUU!<$hr%yVfANL#{<-L+7+ycsBYHt|82v%HE;UyW zCMFgEvA`dT!&Mbg6nr3r;TY&ARM>^PN8rCALel&D^n7bE_?!u+Xu6g0a0SXHSS$Km zVR$P|;Rsp*OUpb>&#rucXR%oXHrP|$)oB&o21u;@EqRN%nN@>c3ns5k+50pN{721R zd8E0!BI$Kx`8^b27Ee+p;#4dX1voxU-!3qU=M@5Db_I@?UHA3VcV` zNO0o~QxMIJp)Oe+EnKPM=-QYUAcl?y@D)1R{s`7{=kH=ViZJ&_Zz?={*=kc5vN zUf>#DYGn@|er+;$vt$hHXaIJT$=d3S{z*m%XxEy0PMO7cq>`ACs9-bXtCUE5z|{sX z)OX$KtkII)uMST6Q10dn*6Q_gbNG(Bty1gATz}jK^@iJ9Pn*xg>*G~;?1VcaP1S9^ zP5tbkVgFA)66QZrI+OWY3vt{L%;Xc%+?YEa4A0KJm?T)q9Ne3{YrF{56EAS+3ZB`{ ztbC~D8}vd1g*`74_=+0sZc~5lJTHfB_kf1RfW|rn0P<$jq+c{^rsa z11*aB$g0%bxD}3;-C7uJzO=b=Q)jrsyUj<{9I+^=Q_%Q8R3jLTf-kVhit}B3w})~4 zn-chDc{vRTv7r28i`Le5@4K|4vdy=zF-5r6Ud?+}qHbQxW#zgZcYFVca@{?VN0a1Q z~b+@Cp*4>GqWyhA+PPz(o`w1udTMwSroNu|7vDw(#SgvPRIc zLbGrg0_Yf|L=@oeekY83h60gG09i%6u%VZ9!B<7*?j$J{4V~e1G!#Zx!aWNKs;&qW z*LR8SMh7RsFq|ZY);|4WIHqmk;UoZsr5QJ@P0{unF^t2Z5atQk5Sxv=h_`xTul<;N zGsigWaD=>7!qj?rl$r0=3_HQ4@&xvJ@TIQ_h6COZp#__Zp_jdVtiQPMk(9M2!T-Qs z^KU#~nNG*MKu@wv=}7>v6OAqDOrj~7iZ|z~@~LDxm#)jDn$y_~0p(TcDloTO zGR^7w%6ukI8uwhT0p#r39K~uf`TWhMWVRK&rQG3sJkwr#DBYFM4kn+0w_Te_fv(iw zDd;5u5E>1DF@@=GFoqI5Ab z?z?u#TZqkdy#(@Rxx@w?)!mtr;)IXDuC<{&BB#=2D=Wdetskd2{O8};0));rp&xCT z7!fqlueSkVazkC^>es4!?fuA=8(lbjhY$Y)QACU{+(9UOs;^vod}HeoGRxOx$g>ny zrLNk6%Hzp<=MR0kYm4P9_iNpX{JA07*GBQTG(b`!jU4OWeynfc-uMDi3Ui^{r&40R z;Sna%m$Q{wb;ZG*TMNC6wC_to_PR&oJ`0AhzV4j2R_6^<1uW0Leplu_EE^xLWpekM zx^vr`tKQIDobJ9<_xE|lT2D#gwdPFq=yhkRvM-fViw*De-QuJoM59n1B%7+{^kRjW ztpA~vl~=|v6Zwx=SJ7O{-qf+zZ3p;85M8009!N#LV0^-ahdytxmQNLhEqkxkRnW6p&#;XN-ytk2gjVc zVjY!$BNmxQO)WlG(Qn4MtXXB4xHJ|9$1=9=lQ`NCZcml5#+Ns9OI-$wCXwcnPhLf}_#5XJo+e8nANd$0@ z=nF}BDE(mTB=C*EM#~gNs1?5+gn~lI+r(*u)2)^Um^qYuV}jp-iFWiqZ4SDeqv&8-GQymC}Ae@|h&-P4j&(|T;aRj0=+Li76M zz<$M+eppPUK52`^i5x=Cz8nLMGtm><-<7PIQQhzLyI1!PC%2%{Age~809XmBYWBv8 zgFKS&&RS&X_HGqD?(WKc5{nzq{mLh%_}Jxiq7N?A3rZ^6(Y2#1o2ea+ge-LJn?NXy zY7{p~rtOy`cp?^(BYR2hbf$u6eD!Y`YpF6Sd~(ZvbCjD$3FRBO5o4V1k3@_@#u3Z!oX)FTJKspnqx3lTfH7BLq z8OmNLUEj88TB&f(7hHck`MjE>N5m0z`c5{Vw0rW&l8w(#0C! z#fOf>*@nYv(M&L~)m@$A^m#n!jE^JrUgsv^i575fl6s3Y4MX9Gn$nFb1ti&B94sxt z;iH@xDE1A_?)^I4R)1N~*o)cZVg6LlI{4{!lm8{*sQj;AD#L1F5*+>M38pwWmR-cm)C+bMCl1ejr} z{AcKPp-*b^bC$EOo_kLq%on_G(U4kDlaY2HZh9VMKY17vrD?wad3r7C(_M^&eCVjGXpriHr zu3pp4z8ffRAvKi`cnY+L3_54juctH%&R-w(E``UOA&^hM_9w=iJs>~-y2|kC?c$esfyfk*3|J_yAL9k+a9Dgn;eP^g< z0=Pl|m?o4YSIp6e%0}^d4F>2S|AqNW7BK;n+=ED@E89UrPbTu&WId`hwnozYfE<&o z$<&eLt}z`axHRv+-F;V<{#4fMv|J0Q4^8WeWF=xj6=AS#~ zRP{-D+Zl>Jf)zv$OGk)0-$j=?GY5{)%o>PLw|8Y9>>nY_<{yf7gfx~KinFk4;Gs$u z^83EKNtXfVHj1k(-P_30tzjECgQ$C~K}N?t9ka3=J>s^#3>Wd@8LP6&_B^_dLp5Z0qtqU%+*)z!Q0oIh1~`t?x7 zL⁡wjJa5J)2D^vzd!xRX-(J)RV=hL^|;?Q+mf}DEb2Gb;oAlmFQ8LHxMi1v>K$s zRuB$mAw`l`OKEa8k*pkRb%`n*iv%a8*M1!j1-&0(AP$80^THS2Z*o3Z)JA_?gnZ1B zq~7KXVj}!N(d0y@u@TaWV`q8je%|Rz6-UCrk};k6oYlu_?NT^Kge3k|mPE%mfYwk2 zsc`YTWMk~2f=%Siv}jf8))%hSRYc~BxSYujT59nLY3^4h!og<{r&~PqIH=m=6=77Z zARGD6w_8GCaxCiIS|jg<9n0GCF6Rfr>@u&~ID6!_>q&MjI`lLbLL|z@whSSbaB?q1 z-m^RS5S6!aU~S-d&C1U0DeXV5nH+PF9=sDQ)iECt0yzUWU4sw(P7*|2UvAj0+1sj3 z%B{+BJQ;GhFiM`}MFbX^rVqyg%K7r0IICNnsf+;~%@x|I+_om~)_w_iYT7e>a^j{0 z3padFLt}Z}Y==Ir$<<@Kov|uLloDI5zZ=9rep9Xrgd87{VAG9&c%Oq)#=<^$CZ?} z{ifp_3|#%Jrn574j^i|(p8!SqP@?7kJWte;#^$$pe)~!B$b*#>3dhv^hUZQ@j}b7R zZH-pM;x##Pf&vd6Xw1f=>E6o5OfC{3S<9m-HtAoNbUCX9b*Rcq9$;s)O=i|a>OGFL ztd*k=Kg5``*@y#bf|Em!;iHYX4ygdK*mC`x6SzYYf9*uzD{7KuXR4Nm%Zy1vT_PmM zE46OBGMu^@@U{c)b;IpXMWGQB^+OGoMI&oNenmsJQs<@rud7(AqNR8_rkZBrLMRRo zFgaD)1Sh!k7%b1(S%a%Jw~&0ZnzbC-wk_TTJO87_i-nudAU;WGk$Yw z+Ev)ohx4esG=##FSjk_DEAOj;SNo_NTf80`w&@V5u<)Emu=bNv@0FEq^(^w~hlx~0 zKgq@EDT4n0l)*ehEoP~i9NEVH8^xjES=JfN z6@mH)&dyh?eBR-&YEsU?g>YL0WFOq<#N?zYUW`1{>gqxyytsI8X$?*Ih;QMx0>eP< zKZU|THD4}JHe=ob{cC93?`o8{m^z`}xT}U;=rd7*1tIk{q-I!e zI0oYs!p~g;G27%mGS+)SOXTH{_shJYq3Cy#xX+~H05%3ZscQegHson^G=wm?p9@t+ zmjh0)JP6lFr*zM@#P`*Cp>}~?x|`8P$#F(&>qAnm184SJ@|Z-(8^$cIzK>+JpDA0Sy=PaC35>a-w;xV?ep<$DvF_FKBl)}x|KD|#OM7ix9m6IT z4{f_LkW{Grn9zNcnDG7;T{=b1ih;nGQ{Pn9WS#5h=EDd)i(Szt^?7G0vNdTDG(P9K zZ^T&u=2yEu`BuL5uUYj+jf{heNcniECex@*6qsxs zM>cVBOmmRr2H0v9GRIb3vX?JPoI9<3q09SMR0Wc+_Y`gEKoNdCl*_sejk!uV-hAzF zJvo1xYU25P22=F$^d|B|lV2#CtILr&I>&i^dN6stCsUiN={f19_ND-9yj-8F%nu|h zv-vu(8Od8+pMmww*HpD<$x@vW*h@_|S>0BhtgozINwhU2DszdNBnr0nT(TPU#>y0_ zu$OD#n5)5Osc&deI-_)RK5?Zb{f)2xgWzDFCFLB2dv1CslGz*B!iLS)bZGlIXdQ4s zYsV#-<3Haq=2TzRfV?kPIyWV8wNHoYw0;{7kfqU^W)lqfkjPr3mf-7dinF3Un1n}{ zNVzx(ODp#lw>J{@qB{}YZd{?%UUuDwjO&PQ?UzQt?GaR=mgGC!pO;R!YmctSjaS}s zgbPO;+#*=aJ__$Xgnzg=`Iv5Z`&9I#_dEams#BK@V*u6)F_G*ZilaZ|a!>puC8Khf z$a#g|yXp*Iw!JrHB;Z&F*Ee-@IBxoNv9QKNxT9*_-FT7Nd(RM zZt zwII^Y&~>Y#eM7;}JhK@V?TUyD55U6{@TjJqlESjp#=7K22qsd%)94o& z$lC7%St-p`<#26Pq)=%u9qyKTQ|&rYwiPEFCNJq9kLpStL?c9HMK3!O}Z*- ziCm)F)K|?_wGl^hG;UVM>EH!T&27TNj34(2eTTL)l6dW9)TN(ztkreOB$8|S3flTf z*4@*plk>^sr=eKL7%%gz;$3cVp5iI*Tg>U&sR&taS!aFp*kE-&dNO0I(PmK-1LfUe z#H~dNnUiFiA`7^3cdQOl#RC(zD{<{6LtZIO?s?IZE2hGilN-~_)K*FFpYXQ!>-v=Z zCN(05bcrTesp`!FX1UW(OXvM@G>j*UoV6rAS~_D(zV0T)%vZ%zYMOA=o+tdAu-d$@ zcsu{)Rj2=qwxQGN#TQ{1a|FXu=DvDkMA}GTYzB}Y)cScS)$A1|ie1~)Kk4q}+Ndb; zChzB&<3~=FJvOJ+Y5<}ouh{uV6;Tiq@k@dEDGSKkofHD~%wjou8kjecl!~ebaErg9 z78d2L>5|UY1fLIh(cMstC5?8Apmbjo4RU7W;W8ND49qOWR}xVaf_m|U9`>^{jfft6 z7>Wx4ZU!8K<&sYRD7iA_mF+77D1)qfm)`UN(>L!HeO_%-J?*yF^Z_nyX%)=Ch>jF8 z^gy?>q61qEqFgMl+w1)*AJDxe9K%C;oOm{n3jO?s8Ha>fnniOwF(?uxGoZGFryQtug<{ARN-iZ)rABFkP;+-=NmLY>wauAt8*E!Vj;HEvXyJegD`?2npy zr97a!5Xxk4U)N{u4hL~9Gy;5Fz`L&wsR}=&LR;jgxE^bT*xp>g5Mn89yqkNlV|anz zzv|R{81cP1N^DfS;R#WANEmH4je$Z*7WiSqJrDwg*!E6ojwl$hg@1xqA4qt! z)bu&~}vmWuSz_W2&MDM|G4EsfK`T5sSFt~&Dp5-_4vyzl)K zzZ$|vDVp~F66f9To2b;H_D@Clkkvz+v9T&|+^>r_-nA9_<-QZgb6Fj1N%cB3r%u~Q zj@abgrx~=6=kSrynT+>sURPVR86Xa=S?IlHqOh${HFb&JL{gpHMJ(b2G!=ucacE?i zQd(wlIS>aXp)p1=aXOcJ0Eg#_X6hoT#w8ewTup`3;NzlMd&oqYnMKdPdb-H+UZzBZFgHJs?)0=#&BB$sk;pMY=8f)JjmMR80<&DOejs(t0`xtiMAn(D5BhSqqp zs|eLQdOCTOs1;PnnO#BV=4Zd@kC>7rg=D#0>s>X zR+US*pJX%Hw)mmicuOvU;`v)+DW_xTy7990@UkQCgfoS>`|5~#B%=v5t*+b>ADVnV zFVGT=tn`Ze?yCg;!?1*R*A(?_5x5)Zk!(b*T2s~Dw~t(Ry3<02hw;*`^b92b-{oTa znPDqMcN#TTeR)kFvI3Os95V2dx{^!#x9GTAPYg$cxM7qxmJwU&ySxe)vM{+8~ZWIm-UXA2~k;>uvsvWM(Hq0RnYVJO;|Y|wpoS4wULCu(;l zG%t50kgw#-+~lvSYH7q5LXisZI?ZnEj8ByGOYm#PJ(9P=_wZ!fx6DnOVxCJ;T=NBh zD=UW?$6JzGDnr!f?yzN%Lxl-HxH_myy`HPy$%*-L`!t^WZLKtVKhO2%q7))yXzB)n`gwtCJMc;xOU^jef|WC&;PeO=G=S54oya7nOw(kj%3(NgZDZnmkYdm@LDh{iys*i;UkNxw z5VQuWNGJ?VKFI0SP~fwJcmHN}r{l~{5N@zd&o@P)7y=A3iYumEi1)pZXf^nNlpsYt z*9(mf9K$+tkNn1>-bZA|9%onWPz@x1q(44n=5ER5hkZRy6ZV8f$dx~iGZcG&lf^Pv zLmbIQ(#6l3W9}Qe-<4`%t;ant&yNYYcB5!LURtgMm%skHk3b4Q@8krdnOC>tt#LI zz9PP1NGl>Clh=sJ?bS7$-uHfw2bv4V)XCeND6EoMgwrTrzX35)8 z49+`b^>u0Gxo&1^mCL>8y-0N}); zQQ3aH(ZFu+?H}$)@SGS_t zsUM7T81x>~pN$8^=4)n>kz1V4LA|mw9gfe@1bG3k@tE(BmAy3H-R!=zcNw7X?Djm3 z3OSK}h=JJ^h;vfIaGI>~Lq%S^; zQkJxeCYeu>R|3!=n13UxTg5>ZOE#s=08#_i17#|^34K8JO4I^oyPMIzT`;eMcDj9E zVXqWM?Nb;(78WPW1@IvyLh><~Vv?&{IxldjmLG+Ym|fuj<0qm)C@A_0QOL8AzyNz) zDTYd$3(i!_#1TTv%68B!E{6QDWzg*PoVe~3$d|bNA*o)ybNp&TU3!aOmv?D?@9pG} z7mq)sy&;K50hp}_HpA0oGp1`Y(9;8Gt|?yMYH5|;N_;k2@04i*!k1? zkQNR1l1ZLP6Ac3z;4$xKd1_}7y+Po!)yl1q*5BnSWN3R{^?jHTKK@Fy z!nc#-78GzFM+49W^LM&0qO@{5Qh~<%2}!m5{ftFAInMIv;w2A4;pcufZTmcueHic& zcwgL{Mcgfwn+^HNId5^fS>w7-d5`4<8rF(D@QstA`Jou-e;9itBAV1cOR~9VxTf%F zZ9R=nT=v$I4^7!EwOhve=t~l$QNExH;(uYn=te&#L~vCuDGG>k^ZB5g5*G(Su+MV`d&Bsz8A*b z8(ZnatZQCAvtYJY3!FYMEl2$}w%5b0sqJB?It1f4E~A&hT}gcK=^+j`&Du%kXd2|E za&o}4_Mb!mHe>r{3K3oHeMH|ix4+yOkZ{yyUC=7Bw_VJ_N%MV^f%Ag*3l!WPsPTT} z5qX>}q4h~4UMAgJ4su7VmANm@*nSjN2MpP^Gq3)N?%}s318#L9wRNDASEu@_TB=fK zT&Fsltn2~jJlB`a*Q7JKt+{+W*;$*;rm`r$2^mXOkLHr;YJ$o-^PSmZL#8I4tHPZm znW*lJ*Eb+KsAw*g$xtel>CYuod%-qORVCb{dm))g0*Ic?$AQvB^`6L9#oc5wl}uKT zHstbPt7n?)@}yxR*%D4FsRX+Cd^L`r)mps%1}5%qwmE2+PC9hPdWd( zHRc4}cT%m9;ox5#|GM)exb25FyQ};1OKxlHtv|82!)+8;-O>iIx@o-O@eeYn4WG$+ z4VSZK?8^nd2w(T*65kic?hTKWA=3W1fOgG3Lgz+AyZ_t(?aFv?MFV-8TEcFIc~@vH zYj~W7*Y=+l3vOYurwsn~ePG!BqrfdTy?N$rL|lx6xHvkveRyd5uFt-kIaE`FL+o2- zW6jWy!l&-dKX9vCFaKoQ4mYQX{9waGCURo}ZQdK^aBl3idtaQsuigBx$Ur;6Su`M3z)VL7g8Tx~Z1GJ{vn8b2 z;o;#g!N?YR*I{G{ZJJv^voukd1o!m`jS(E|q7SHOS?^Id5_toEBJ^8g#0)N$#^ToU z1VmsSJFMs6S?qopdG!#0zK`S%0%j2Gq+dnfAfUWu5XhbbkQW&qT)x&uPym+n30Qy|(QRKFQ-hIQ!-#zEJ3ogjFg-DIhi~t_1d!9>0~i%F z`GD$5NkMcxD6qu=AZmqBD~Le>zwX#RI#@Ulp5XOKoFwUBK=2S-9u;~IBf2O-C*>VS|8*8VqK6jx2)A`Gnx=@q2vLv+?2r zsGDz`H~y>Ggcru27YGi5-M2Tq0abHiW?^ESShgWvcOHz?(rB?~eqq&YTr`6PjZx7C z=}TW&dhOk%J99IOZ+$Q0h4q_{8Qw88M2DSYe9$v!h}P%-Yv1wEFEL(50G`Qy5hL`o zLx16yb{H~m?dvq-3t*huB}N9fjtp(v>3#PvTySb~^RG?EG9>4guYTaJ?#a)%m8})C~MV!I#kx0*S_lub3qu* z!-GS+wr}&kd+P(IHaowe!^?>BH9t9&2b}d+Qcg>u$+Y$(Xzho9MQe21l0!I#K-wkR zd%qmJ=5%C{x&x1oOCAVGl>%TGRZZK;Q)uGUr05%TO9f{KOJ_pB6mf^tx9U=d0e69qM^n zl5^n_2ZTnXO6dTqj&lIc1?_`*snp0!`FY79Z4xOMlWxf+_`Z3EAf3OXM?9C7wiH8X zu1sTiNf>5^b<&Asj1Ka!8qfJG&J*N&l>U5bPgWOq%1*SbZflU+)CIEO%1UA~H?|Hr zSMw!Ou6CLcO=n~$m18um)@R)f5eP*RUbnAoUTg_P{Md2uTqIL|91l6@RoA>omc740 zdpDzTM2Ayy!fy2y6B_2LQk$ZId-+HWJZOsISVRi`)xG|AaNoB?#uzzyXt&#S*Tx*p zI-`Q+K1^Mg>{6C!4LbF_N=2j>D@fAx;-h0u>bS<>x!G{@raepTqu8Ewi(0<7U5fwv zbtb)nn#L!a3UITl;Y(@Ix}_nlN_)T0*dE#KN~<%kOD|*9oQ^pa=zZ^+Hpc|pR=j|H zjY|vRUto8wN(4XeRCsN)W`DD^P~|E0@uns2?cBxToI0lH9Zy_yhMU7$BaD&U*A~Jk z=}`}jBjktbBJO7IDP>xUGATru{wS|3u5Q^E@>hLBy-hjwPc0+kPyMehptZRf%Y?hR zyvOX0Y0Zs->2zvsxsg8HFtCx4O3FBtt(4X$oJnZZ=yr8VyeKu?c9%IDh$lDtvLCYs zoG|4s{Za!%KIAC^oGBACGgc@@0)yVOSR}=<1n9euPu6oiG2=- zpMv)-?!E7Qi_&#oRqC3vxy!6jeU21vGPs<~s>;kZ)vGbNrf`1y+5EeJ(!=z zX-y$#D$*Ja>&II(V28b?^fjlw`aQ1HfPl%mD+k{9Zt;GYXMSV|gevU!Ypw1ltsweG zy7YtAga*Yu?>IzOgs4wj#Tivjp34b&>iLm>z00Dd^-W>I`Nt`8nulg0hJ?!OQlSL#-;AFSg3Gp(n~VX0zG zoqixvQA+-@*0F;QD2NL_+M+q1kYbde3($PsRSo4)2d_6s4Bg^w!jrZhSCU_2^m-ZP zGyHDeq2AbUGr7@W-94OJ+AS}vbVlWd9lnj=Wrn76{+RI z{h$~Q5##=2d`xW;`2hlVg|`c>D|YbcCZ*}Z$3^eO)7x{aypJqHc``@ zAs{f7&H@)n^xQRHwmRvlUBjjM@ zy=^v+Wi^pFkg87QsyDm6xJhSH)!8G}NtbMw`D`5LlXTp2+7Fc&(Wd;+!n9Js%`Ffr zGf%n{StD#@&j#}|cPw}5Yq1Tp>X$I?834umo^5U*nnz(qWZFjLtJ1xoVe8HDP`n=B ze6q;s1w}Kh9Mh!xP(By#hZ7FeH=Ef5^&&q9nO1~T*VDpaJev|vfz{{W}`wp%8l}_z8evsTMe6xTH zEdRF5BcpCdG;AO_*mQZ~QLF;E3!&?jqVjs8$!X@(I&7exS~;JKCZ)~>fYk7c+|~Q4 zxGEYqMEqh2LGm#*9*e#nJTk=&uz4kw+!Bf{&AtW``p9w6EaGLQs`^3^1a)Fm2)5I2 zSO_*CO>mf6ND~{b>?0q9LriuSi}k|}EPQJF4L^r>-nT*8Q>hM0_wL}(;#ino$@hQo zsA}IV*vFODAs?R8Si5dac#5|B%`u+2F9ycED5ku3R|)C%-uH;iEvDpf;V{R6jsW6@Y1qMi3YYB$9addf*RAHP0no#hb?3iTIV|-9CBiiAdG}a z^d-I+pZtZHsU;c3urT471X{|J_AG5^6Z@Ue^z1$QLq?+G_?1h^gKGr8Cd>+Yk+UxE zuhY8r$X2~G?fou4_Idw1&2ElUt6GQmqZj{KJ}tFZ?`UndqV?X^;5DbP&1Wr)kBo>r zIab{q3$i7A-oRe>6|oWh;-Nnbg{HxD^kY#{-VD!fDvCYR8^%I<0&@35BmBB8GT%`l zo@Tt08f$7R%m5ZjXu+hb8-orWqorARBp5b4s*+plY-l||=d!+NNj;HkaKd+=VMr_? z2=qHKg51n_Iu239#{@2z01R+i%zWS|Rf-cdJ|0E^K%} z4SH9VnCF@ssqctixAxROR4w(%3_epWmF@9LLm+qib=AETfS}xryLXaS_E1XO|BA)= zxy9Y$Xi_S%Qq|sQVCU{9Aw9OkinRoTJ4bvL#tDM6!q%(}JmEy{Kt@CaB`;y`O-|rX zO#Ie{9pvoC3OJz1CFaio7{J;rpz${F0c5Er+*FboG!Vky69m(E= z#6~US2CX5nHWPHRw*5S65m`vHXj0ZsOi1?_J(iRTOtPXmV864C)%HZBBT8 z#^h(+y{+iMJL`_n4vqjUOcgw>ngFA?1B`+%Z1;b0-w>KBFhw2ldcq&D~S+=m6(0q-oeCuitX0yc@d3rN%8Bo_W8nhfbViO5cdq z)`4C7)VfrS=nMy7(pCEu0qxQw7+Gm^LeId~E`i7PISv`I5UVM6%FFz@G3RW<9(^=2 z77f>y4Iuj?KZNI?H%@_SuPS^E{Dc`GzsOfq0t#pf;bXF-F*?gLW6ZV51;PQ4oit-A zk&^E6ts3e*+C3JrmLmqkPs8*o21uS4_vHQND`Bd%{I7^E9Fu+^7xSIeq!Am!bCM79 zevY=xqDOKm8wqJG|TfGU$A@7;0=v zH-S!(sZHe5&A24zYHKPn`@=G((=|;nsen@?fWg2qfLOfh9FEK>JP#T(Bti!xmrUuE zRio8};l&428Q^IXmGOEUq_eHLrUXUOU%5w8b#QK}sWw@K7ehQ#3j_}(;^}Rv9k9){ zamW{-xr7L2)1+U|q~h_)`0l#OI^F|(2L24m23YFKOg^2h%`_xw!8d*-#P+!bUUm?r z>W=u(TE@jvpLL7zJl<@CFFq_u`EZ^Cz9=vNTE`De;c{4VGJdCYwE-X>6p>A8(@v@T z4t8<)MAr`Muua#F=m6d|(xhFqe)bPmX6;}F?GZbCs7Eg8Frb571Kn6S3Fd&a=H)dQ zjx$4Nu=<$#X}4w|Gr;?cpN}~m+k=ulwGM_<%PG9t`7L$LCb_m(YS+4PN^Lk|+kdUi z^E&UJ@^G{FZsRqlvswH0$M*R9s-vY8O=^tHKCkd+$DIBVw5Nfr)UpbFi+hR4JY)aQ16{Bu)g2#;)s7Cu5>-Id2YS!Pl3lr; z!P;b(3a`8y*u6s|t=czv+5dLTIpDpbhR&=Mp$AgWcuTGMxG#W6gJbGV(*tGlG;oas^X zV(qbfL{3~wgj=Hj_bn#*3o2F{>$J6`a;GZrz!kET4=%@j7!lJ<)On|yuQ|Ifnr?LU z3}w?54hC7*&?qYXzyX6KdEvk)!^a%~%M+i{F7g_Gh$y@PY zKXX1H0l8aD^MOkoo{9wD?&ff;TeTGEI;N9Za$*Rjq+k{UWQLYZ(dOY`Jk00|o7DQV zLVY+GH^W6Ar>FfOT|Zs`KY3_Slic27<_wW|Ss6H{x)cDms=-LG7s5;-1 z?l=%@Y}AZ%w?}0haxGNky87^;a4N>Cdm`Q+(7oeD-L>7$Ty)*zYR4Ty0l1vDS$Qg= zpowsjMaknI*sk1|*49*LXyZx>%oVsLD|^7)?j@eh5yoo@WuNslF?uE(dC1qnOW8yL z;bDeUfpE$bR73AG4Yl3m2=jx<)1W8j5t#u*75E)&)#Lxw!mpS`5 z8v3c9M-57n2virEORJiDmn8OgYUq0SMh0}XopVANiFjF8ptlTqf9lnk(^phXsA6AB zM#L~o>^Kd5R}H-zv7{pxXv=lCRU+KV9;rnppHjq_+4rMH*~~`So5zcp&|NfS%&$^x z#e$91kqEdjB|V@t4GEVR^`!+YaK$x#djLcuxp6=O)ERzY#Ady;xXXz=#ZiVYT+_ww zfW%K?D3EIJS{H{8w{ie)PTkPU=~=T+qW5^0AD4+1<;E+cd&VEls+$i+LQTApku{*8 zTHLJ}TPaKQ`R<^15|vG%2rF-T`A_MGgxesZe>oVOx`S#=#X5tD>G6l4_9Np-vYMyZ z%I(@{>NVVJA4GAbI`Tyg+$N`j3_y>30a5j#!^R~Z&+(Fmq8JY)UXTtRKeTmK>eZ`G zH9A(y%l3x%xOYOEs+X&)5+o4n$tP-BQi)7@dp?y(48`l*-fYv(m!X=TQP{YZc|&ln@kbu#285;l6CFi*X2lF5zi!&g;aWTqNXa5s_y2h zJCRK0VXYI{x@-zYzc$-YpKMBI$Q+SLHRN-Rl{JY}Z6;HwO4iioaYHuv3?G_#5I(y} zIo+Z|rfXGrUKgFPW5{P6{ScUKB)@^Qi%lH1y|Qf+r!_If0j{1@pH-Nb!m3d;LlmeN zE9&kLdAVcS3D-E%Zt(za7l3m3(#M|}D~=C3*Uskh#+6(##l^8?$|%mvZEb^BGg4Qr zWQJ-(V)qVSt1%7CG2L^!^^TW8qi1_^YjmO-Sq!t%ssykrcC}Td!{LNnttKam(|E_z zeC`E02P#t21Xn7eSQvU-79X>66Zd~O-bt$HiNr7`avz9Ocl9<`ZjqiuMSZ)H5Scn-=jU3-kVxxR|n)R0*wwF~56(V6UD6xL~`pP7BOnh(X83|UcRZapYJJ#qUj0Ti3T7edD z2{`T-P?;;W*PPlWv0ttuKB=F%gC$wAQfH%fnr812Me2*<>9=*C(bg8KI46R5D5s%} ziV#JNSe{O@J&A6OQm7H{FbW;c<(Ra^Y%FF-ct#YnjGYDJmF~$#I@r5UZG1{Q?I>}jdE@Wv@GzSKh5A-d$P=HBeTkpwm z1-2mH{4&qIm3z1f%>6BGK=KuFVI=wNsD;~?p&9myo%+-PrA6yRG=3OvQ)ID=uiSks zspvN;H6C+oJNtq3g11%qfOs0Q1c3~yH(}P8nz+Z7p&m}UT|lWW&A>+$cj^5#PC}!! zhCn3-XC#Ee8^i`xdq;(~2|PtsXhrYp!qH%Qc>**qt=uwgruMDwPA5F|a9l8}U!ogffy&G2q?|3Birk_DcKr4qzWpd2K+WYKw&Cp0oaZd(ToVL?_dx z8D6y#jB9lGHKqnVjK{Z_&+vD3+JK3%oez5?TLKQ4CySpliH>R(8qQfp|U0_sayLDzi?QmH?w+4%L zmbV6|L+i>Ja6uI0b$Uh{#um!pwhh8P>5!Eu>bW0?@Vy zgqo;F^c`K`{$qiDB^SK?pxu31heIB=4>&@l7PLNhADaz%?h$0%N5Jj2RobL}dN)LU zq;l}Rk7tGDekH>ECUDvdKyyyEksXhB5;aM^t@g?T6^|64~ilx+Y zA1R-lji&50?vuP9fF^5JW02OboVGP&svmHi9xqLzwA9qJec~Nl-&o}SHbCSi?|7xb z-mIOwr-egp2L}LHAA&*(JEoht@Xn5a_dn7L1#j1H0b!PRPX*kIftOm=i;^rtRo;iX z(X)>qb(`3N`fV zS_LkBtbpO*U`Ezj*FYMNXt3jI)6RK=_a2pOMgj8&6dK(@wH12X;RX&Qzr15Xt$x21 zA{B;zBQmP5znPGVKxcQoPpD;2hb@gDUJ+A}*Hhfc0JO)Oc8WRaPh^wO)(^fp=9~h= z|F7~y)2N=lBH6?BwJ>{)kfVHN9vTMRannPqt4_Nn5_ft3kSBY(BL?tbrw)wU0r&)RUl zc{T8Zhq&A$R>6J8wnla7qQ*IGQ$MC{Ze=7Cx;vwlu0h{o+uyhzk?b#@5DYDP!UnLy zbI_a)@^#1uzf4c&~inva&YSP=H zf=|PSHlSVPf-5rkK&Q>>^wDrxKX0;mgaQFfDdm6C5%BTZbQB{XD=KVVK z=DpwgFK!?P8CU{v%6jscC_v3e4);53gFmKuziEr^T@2+?HA%2g2^K{6->{vWcB!gd zrmj*d{6r2BpfZ!G&J65pPHc)-r)v_q%4}s7QbsKq?y7P*@cw}6L$avqNaoU+e0MD{ zfQiZ5naWI@c*9J#DV+uQI+M)i2pwz~NvH0_bE!Sq>&evZOg5ewA^wn6KrmrDL0xV!uXojTp?Xu)0j$BW#U!f{&mLN8d|g8m=EB?HGo*si&)YY9s*{A z2`peyeOoxAV})#Z_<5Ok&ogPq+4S&F6vJ$aFN`MwX`4~uHWNw`Yyzl%Sg=*PcrX+r zB!$cUQIN zuDo9XJ}-+}``bVSkkWNNN3XdXskCgh6HIO;Ix1t8>Koig;rQaXS#a$YV$57LB$hu8 zc7+<>^$z?7s=ErDBYDS&cadM4inh0$JjVSqur{ndqaN@UBQ;xUHgS26*3gSl)fdwQ zWk@+Dc7`of8{C_TfP|bxYj{2!udwq}M>v-|uo>h_yM8)W;g=nBYs%MlaZU9Ud9M6C zuxtMFT>EhC{7HC=&Y_-qN9I--gz-|v+sYMly?m{nYo)SH+x4I%5FX^r+Rf`qPd8Gs zO8f|S$JSog8g3rrhV0Z_@5r3h9c`Ta+T>r}6wYj_Si8LI$y$w_>+e1{paP{gRdap) zRBAC4E562N48U9}zu<}n`C9!Zomxo1QS~?47^t&0$I%)6zNFi>N6d&dx(QpZ44tOJ zJ{WeqPxDAIy$jr`LGi^z_W9f?8|Z$VJV@sZ*Q6Qo9Gd?ZC|+%8T1+7fvt2e98QQ_D zP3TmGVE~mt+!{g^3Ys(7piT244K{&1?)a*F;HA3sp+5JB#Hx9*nXFQ%wEF+hc@89$ zh3-j$KCabtYi}`JVQ8x}tiVn#0}OI^4!)XbvXU~9e6~oC0+;E~8@rtfK!^=n@tbf8 zhfDNgP@K={HG^(y?OgN) zeM1C!5eZ8+;WO14Z9+v>H(K=i$Mm8hzKAEvl6zaAJhmSyr4ZL{SpuieamZvgd_|jK zMbP^lS`oj>D^!h2HENQag0WN*&r;^=_d*d^P*TtN48yc^<7=~E(ib>w-ScRVX@C5L z60P39q52N|zo`pN?Hu>-d#zR1oUMDK5I~T3wEY@myFEk_8dPhdky57=V+IRN6GS6d z0NZ>#T!OS8@ZO_}5g&}C9@ahZ+*fQGE8ixGb@OxY>y+s@2kxJCNy8A`r*Dp$i<$Te z){L)J))L zUhr%0HOz>_XcIL+%cnu_Thu>VtYF&uKuV(K9g!q1H48JP5I0mVri9swx4#mUeO?1+|MEEn zZ;LcOO6YaqnobI?L6G+QOAE5SL3i?6Shbq*mP@B8&yEV|bW zqQjD2eprim>^Lt9WxU_v!J6Xx|1W3n0UXzso{6#h-rM1J4rl<4)X1@s0|62Q!5jb* z%sC*EAdv_HOpj#mxtJMAqpgufCF!lDmF~>5MUG3s8rkb|S)~b0ydqi7arZPOf!fE)6Sp?t z)JqsWm8h;T?ubIlmXW$5MaOc_T!t?u`*tjY`0{CzCNWOG{2sWRA3)G1j^B$W$9cK{ixQ_QaseBGE1{o3|7)UD0f`Z_YG8NWUqxhfL6&DG3z*^& zc5)4&_J-`9ex6yMP?rr+{c;_P6H;ghCp41IfW4^ilJ88ERRi*hn*ljt#qZNK0DS>B z+oi$!y?_m$yYP=NB?T)055&MY2|Ay%*8vf=5}YtEHvR#-)tlpJ$X$34nZ8HyR|5B2 zhza`zE#*3bU$>1S3zrg>eh~PUQRGuRubZWCS{+M;qorZkGfX7Isj4&>4Plt)E;#dN z;GQNGt%P%&+8EsA#A>4vI|^*Q9~q*NbQJ_DqOgG&qj*p<5e=6%C1LO|6$(c)5CtlU z!QNr4GmDfBiRK zuC7J)E=6WNcZrXk7g9ychx-SO2ZLs%&UwDD>3Qh>DVkj7DRW=`BC_?ez-r#*YTCGK zuJPR`tdX*a$vImyMP+p75JC&NYBY zS#9DZV^OZ!pqwmCW5s}z%GF$I`T#NrBV=no6Hk-747ql2uRtgAJ>EbIjP?TZXZ41- zY#PA6z!$&AF>0b;4oYMbb*W~5+~HrEGHM_W4Xgc{T7?4&PGZ|YTLVNQqE+J#`>z={#|@CT*Ti*)oPE$80wV{`{Rx!QS*ir#XvPrg)VfRIPg>A z^s$v3l#5#MxtsmnPv&6#5x6+OZ1GgD7r&WG#2M;E;;&w!4@vld;j{fbtLl|sqD0)P z{-!+FNhm^pBJZcO78;7tEPi728(WT<2#RZ&@~a# z@&ul3)9?N?#<6M~w#CTx<*Z)POFM?gF)o${eT%?(4hNoG{3=4U>oJ?0h|)~H-!x74 zw@^-VLF|=FyO9K%#fhEXo~kHd6xf5NdL#P42r*y&_# zu1O1*L`1x%LbmLn7`C3rB?)Kbb_Gcz0168XrBIHe4u!WtUz69tH!oOZKn!q-i?CN% zy%f+LK})U%VCl_t6Ftz8b^inltNJVv1RSYF$+I3Vm%}XxuJdV%({hhr?=YbCQ}Ul` z(J$6gZUz>o#kv)?ynvdMZWQ|cHQ^e3elRG=BgGi*d3T_*xl6$`}J-++wcNOhd2Pa7e5 zlEGCuE1^_IQA75dg9cy2n(eoZGFKmGRcS7%Y0D?(7TmWOh2*^-d|h(C5bf@Svyn_3 zw$I`aG7iTQk=DL=wsasGu7W}4OxVtj!T4xhsns_j6~)kF>+;2LDdA(|`^rdw`*c*`2mie4dMEMz~s=U0lk^K3k_b ze2^_+Lj}dO?iAe#*X47I_Y3soC@O5iru;yjsok02xc+y4yg%QUUwww-3~0mRTyEfZ zezj+11Z>c&7tBnCrE5P`rg8^LgFu!Q_5!Dt5i_Uf+8#!B{|CKOjxh zV)Um9{`7+D!Sww*GrV5~CK8KlWpQJDb$WKaAi6)h2K8MBF_(RLIH-UK54ia><~aw} z!3UFKHXlA;0da#@xBO7Y-h8o9bBn8=-ZSqiz)a5;79Zz(I(oO$Q2oj=}Bmd-i-5Y!;w{&!+Re9oYQ1gJCqei)L1z>A8LnAQW~% z5Uh+dt50=A&roMi=iZK7e_mGOv*-DZc?`I`>~>Q7!8T##^yb-yIT(wB^yLQ=Va@b* z^cA*Sj^_4lKR z8^Gz`X4?A%Z~zFs4<_H$iPc2I*q8~reuJFChsLH)pa%5KXWtW|`(RS65KMIL2qv09 z^YH5Uu4DpScf;pCESGn4+~3(#81CfB0bCGwDN4P;rrA6T5-%;e9_-Bd$0S3)cMkPo zsoa}~-p%S`*r<8|B=~a&8Eb(P)tmpE_5u38*FY=_y|F(x$EPxU{HK5KKN}FsWNn{8 z2VkRcFyB3Z{};Q5Mg|5)y8Ana2f7D)T+jb}-6*YiAE(GOdG`R*Tgk87jT+y&8#5+i z;enx%UgR4b?j7p=k*ljQ13{cYf9c$OyFK1kps>I0c^&-^qIaU%$banyezeB;iu(rPf8i2DS zpA6Q0+5PH|)fh*<{S}1QgNElXz3zAaIO84tcFW(dF@Djb)46>4eKThq_PRZPU2RnS zNWiTz5abxtGN@xv&!B-pBZDRe%?w%?v@&R8(9WQPL7qV;gDwW$40;&!GU#K_&tQPT zAcG+Wdl?KH-wwDVM&)<4#H=Z_CtvI*CQ8-Y9-yG36eJlVN@FiF7}a9dL~1>`8qEiPCxH(>Z*k2C|#>! zDkjv~mi>Z+i)&h?8ITV|xVCUi?#`f#lVsw1Dapi*oYKVlJ5pLb%fB`y&vH||d{fE~ zEBT_%$d^qCPlNvN>4T~kY-HF$+iuR`g2aaPh+fx_D%H362c9+DF|0r!2-7Dv{_}6p zj>$Wof<_Rrh(QGZ;YEx|Af?Tcu3T;JlzX@;Ve!ra+o+yMRZk2I*juugw)PmF-r^(H zC?-gx88KHfHEqZ^EpsE$3o-S!61s0&?qZoP@%BPcdakrGn2;@$RvPPO znu2;E8HQ#2Q`!%#F3=I_YDjs38>ONc`iL!w_NsNsB7_k2NS;R-&YqWNX_>Pkt$D>5 z$0Nfh!*EiDPh_2;5Im>~Z-gml86K=$p^A3O%9X@W_QwE^VQ>aza2`v47NnMWDS59v zKa+TgQM0o0j*m$7FQviv)gFm#T#Se^?Kzb4NTI>Wvc zQ$oE1UrWy6;)t<&ons;?!&j@yG~sMfM)C9|Nj@W?9wwoYsq<36X^GbZ)Xqwr2xFWQ zFCdl{H13zW$K-}?wd12oPcexh@z10Hy>NsC=L8J!ojmHfe30ep$d*Sp*+GAxNg6g& zE)~^DDH{?B?9#odRZVQ4BeXgvE@fSi{>Q&` zzmyNXti=&C5>Ax?X!^FDaIYpp!FKKUzLIM1Z?9twr=|XGFIK&HA)OEo@S#gw-X!5V zAt_ByeTd~dqJ-(hrT=<6I)?PM{~o_5WuBap8rh-^ceBBm_yu;lrS}^8-jR}|jcQVw z5S5rRhS)9)W&Jx|i5L1Kwl(N&4m@~qX$E!wFG|`u83oPwJS`x2zw(N0DM#EeIXIhe zAj!Ozd9kfQ{omSTEjda&9EV{YlnmM&LcKJyQtzCEWfHGvQjY;Kh=Ruv8mJ@l;S5V6 zlcAD<&|lRh>7EAPIce-e3HM68&MTm_2rD)8)cykmVuI_!GLK97d1+7&fqX%zt9dWZ zRGGT#JxsP=?O`WG3(67j;0WEV!PMXRd@M6V^ zJ)E0+@nw`i#?h^=k@j{<_*Ck5<0uohtUNoO7~je5oBf|AWyT&*)?u{p=&^gWA)mrCbE#4{(nTIu2p zzBH3Cndf?ZL!$K3M+o4f0!Iz=?U$2=Pbdp}mrpoyAZJ4su`L3rvmeJe9(CCXpzUQEtwCf0ejz3Ug*cyOmq(b5>&WAAQ-f~dzun5{={sE<2py1xY z%CKhzJamXonr0wq(K;9imBg5Ah!KWivB3%j`6-^TeU?AQB*9=L8H_}DYMCfLV4FU0 zSFL~*LgS$<1|%wIM+0FPQ}m;lZ~)FMg8|bY350`Tzdr=8p0Y{X67;Fo8MyH%aF!t9 zz?l&{?&*i5M!>8zd+JQvhw8dQXhATYwC0)!u-fwpm91*_RAYPsA-gTC%y_7GFyko$ z>(rlCiCexlb00mrb`=hUO9K$f=S#0T-0V;IqXbZuuM(HDWm&71KrweY!eOrPc7mOF zq&;W@{lR#l$G}{Y$=ZI;eRMMtvQ5;60fZDHetdl4Kw>ob&Yuv*A`BjO2!vtVvxN0$ z`caS%DR6SzkzfF+L)mNvjA6htAjMVTSR)(?Mvbt6T5*u!ABUt|U9Zm_r`>^Q%wO&c zw5t>F?421ukmfK|9C%jugiUYKs9w2hxGpYvt7yrfCf#&oe*}1IAXp#}wu6u=My~4g zu)5{B4#A692XP9^CkRHEO(QN5GJ-zL3-OGgg*N;AScvd`3V|8ZFaHdm{DF5MGXRBQ z1ejC&D=pI>AdZ56j4OTtBN8t@gh4Zke-`sdz#-9k;I)?jY!&o0@g7L=UCXDbrj%5R?CMfBsvg`qB2y8MG(YFM4Op37(weHc8wl! zK)@-JtZX;@H|rwNFZ2mcV_@S29S#O83w`AvpavO4B!#^!TUMMm9*bEh6>ekTRwfY) z#6kcrsEi|kqVN#%g)mJa54PfENYw)$hIShUJ!tz4JA~iu|0did@fRx;?S{;FB;q&x zOba7^CNmj)!LN;L9X{F7pciV_qSsv)L;3r7nH>?+Z=PHf&j&=Cs#T62ea!A_s!VXR zhLTQKNPgn#wft4D?TDIGcOZtY?uOJMTaDNuwckb$xz@t*@R#q>y^Uv2;~qDV`(sZ< zse8%2AojfdxZt0w&`f#?2 z(Pr(mSoAdc&AhV60!%@b%}M#L-~t=tU=mK4BOUgneuMp(Z~P}WjYuui3)Ta`D(M)p z>+zBMHKZ#cYtj_t+q^4Pfh)}#!~3Pi>pE2dQ7S4p9HgA(dz65^G;|IU`vQzD_Owfl z^Q+%EN#Q-eBR;nMYM_ryN7xWUL$KX&q-)gj0=bX@b>=xweoHP^D`jLPtCg6LAEIiW zR21us(LIg3IM4VyUT;5`jg(Lf=Mkj5-f0M$@I7gGXThT6(f>%SV=)r;rnE99g)^E( z+$Hb+F(xo`Qxq;6ydJ2I-@wOvhIgh|5M?|sw)=1q)-qse0fL5UPp$C2U)rL2v`0o14BK^RGC=SJ8PurzN9b2sK`35^XA_mO zMQPIqm&U@c7la5_h@Zm}5?K1hfx0T_85?lQ@PQUDQqj~7z2Kv@YnkPB!KeU*P#`S5 zt!%*1=_2%zN&XrO`0+}fv#V)EHb9bnu`wN((^1>(E`cN?uukjJo9JWkw z@-gK?jW|4xsDfXdmr_DNoXy(d=iFEV{v?>wuUNhzb#^cJWvE8w+5^C3LRZVP-HpjQ zVvAvJ-!K-vC@x*_0S6L?w@x3koGw?nq#%t=?jNCfEgsALJxp}zlof)+_qJ0B+`3>6 z)Z?E|)wL1Ntc1zixw&ntcO#a6c@0Jk*nv8HJ?n>|yvO&&`iZdVH(k3HvqX!NNks(er7J`<6$Q?v^^JZXk z84AWSfVGGygJ3M>px73#Wnxk=frs#NsK5yx6@D(ok`Q% zu8X+p_OiZlh((lgh8-Lcxb9szU|`;zeG2v=5UVOhtgw{fR?tsVG7vHm0`Swb{s;gK zB>1$Y2~{fmL6M zf5=LPy5=t`Jnd9V>7T9Y^yeA{-l|K%_8p5w-J#T{OP$BiIa4$^Rq!kY>?Jg0yB%}* zq$)KvuHB2=$LZr)+0}8CE2ps-)jyT|aJ@jnRkT`lmM5START>#{C5&EbDJ1rbx;}c zRQTS~bNbB`Wh-dfio(`N>U|Tv5_yap`i>1%W9TxVGY|24+8+gPP&c<&3oVSO&7?oD z3`Wzk$QDa4B3TmupK)8M>#;DzX*OtoS?hRFr1XM6R9Km3CYpvr1+yq=%NrKyC_nVO zz~_b&6?~Xs850CdcL_os`vZ{BDC%`T#W$x6#u~tkh4R57_Ss#eY4pF}qgfyg06!Q7&jm&GHQE9`7B@ ztkT1yT{Jnu4S0`~LnwBBqnJ+X{8ost5h2qBBlvJ-^{FACameT~ESNHW($@4fo8c+xElyulK0;}+XBP(fpm)^x82+0+J7i^ms5|dgnbrktQ zW`qzdn{iJY*Sh4^b^x8|eS)45y~kk z5cgKeA8dqu@(?a~Ni3mcv@{fl`e-Dgj+Wc$NH|&D9s>O#o`I{&bT&0r6NaJ5P<1q( zjJJf-Wr=WERh6C0q{4}Cd1ha%G!;*zOG_)mRlT`rER&6uSC>>&C6k@Gl4PR_m&8#` zNl7#vk0z4-Y&LQ_94qH6R*UON7I(3YK_PT!F-+D1``QgTM1Fr(Hw}?T}9}EKtLkh>fE|~X^=3+ zP}92{OJamE(Wi7F54ql*3ubp;cXyGXw1Jq6*c<6=VTQYYMFbFH!`NaCcxohTZ**Vru0_HGw8i^#w%(~n$oOEtZH4x z`MSZo<88HY1%JcBEU{%>h=_$?VoJ-~YKW@V60N>X9mZ3&EZ_G@~!F#nv>@_COW)$^h= z2>(Uhk@#^5+a=t^2O#T|bnE9b+5m>##cozeCuHI3UNuSt2<^RkKAvzsoGytS-Wg_R zNFv5}#@RV25vO(*uX92o&hIQ?r*KJPZoeDjn-X#F-5AeH1Pl?70L*%qCE^8HkK)&* zyi4^n9u|ra$|7_$d45h}&dLzUMsgm=AP5t|xrTn@%y}e{e zB4zxn6wxOkOj#p+t$fuCu{|=FSX`bS=SRNOLv~m@`(u&}0QpSS{N=Kv@)2KQUCNJ{mik2(Z zt|7{~E}amrpi>Z{%XwACqs&UE0kj@NKY|`E*F8k578<^9kbOSjl|4C3DB8 z2U!1D$b7`gz|`^SHCdASe43HI%8J_ZS?s;;#B+()?6}uLm>Q9GYcn>wCwjkoC0@_z z1$iFhwA@v~O?0X?iqJ2;1DA@uLp9XYD^AOh?kFRZx~F`^$;+}#%WS8drkms{>gv`-foV(g3}x20Kw9QZ%cx4Z&S9zP5?kP0 zlbQs(cV=Wf^`_FtP>-a!y~Cl4HX{!Ve0lBzbYp7Qyg<0cU0mm&S1e`MlIFAMC2lW@ zoxM~wgI}s0-d&};)d=Ldu*QR{jTT^R^AXu6xX|n!?WlSnSDO)aI}`~qu6?PbREhOeQG9NYN?PM=MdJmt z=bj%VbkRj>b8e6VTjPhLbx3YK1I-qkD;vBU5c5Hz2ZI4r^Z*IcEL|J7y+v+1RF45n5ELV zb)iP&Wwr7X2too2td|h}!9kMAUq3lN;FrPr3|SQ(AMk`u_A{rfh8sfMu2+?eXo@b} zz8c|Eqq^AVH#v;A?k&a`Q+KiK!RsK&V;Aq_nk0W?Fqu@(__5w;F#u1N*c>u)K=KFM z51bD9PtFY4Hh2*RPXXNxfKx~=20Iw`tRo|aEP#Rg+wyl_Fe?Vz)OQ>R zA(X}|!7V9vU9zl6vE5RvKB_blqmOHi^R9D)FH6}Zv;e{ZpCBk1QoIIl^-AGSrHlts z_Dd=IDWA7YiC>q--t!1oNN|>|a@E*i$L%cc`0;o~HJ8AZ1Aa;qiG=D+Br^ERA4RTP@kf>7q4=t@ zeOSLCh!gJoJR^6m_%mq{;cL3K7 zxj0vVc?6jld5-h2-0?HGx6E}>Ms>$maCE;CJ+8mkT-4(Ve2yO1z{h{}=I1}7$2HLU z@por4nJmQSck6KtwC;FpcgG+6q&K}=(F>lU#i#NDJSW`G(J9PY2UQv1qka*B?Lx?f zuV!&EE{?@fvUtdX#Jf0Oh7Q;qw0GBOi*k;xqv?eC405i(a1J%0bB9-#m+8)CzUan2 z=l%~v3*P9*Ke{{}oH(=yX??I*U^oh1#Ni-)5`y$FMLoTq!>6Uyd(S&_<4dS)0jfr@ z-3PDgbZ#w*x8Fz2-r_=OwWKO`*GWU`scaAI0#no z#y&ZF1m+T!;H+G0xD8Na?daNKvA@y~@CxRak?}Fp6t&xsjw#1sh6f&|;SYWs-Cl(f z9E^HOrXv^|7`=q%3A2gzoaAAy>7{A-Cx^`ccF8i%ERhOu0QN8NZ5cg`_HQvS_tq0$3Ajw$XChDZ;#TuLZExF zqwliajt?Y*?nz;~=-}=H?W7u-RF&s&ekcLPka}ZK0)bBdd!20=zc{5eZltUCL?^8{ z@EF@2dN$NXinIEz_0%<+e!K?7J9h5_-!Zx?u+XY^6rS;U`Sy{~w z=7k}%{CyzSzeAC@|EIrs($kszROS7xdH1_N^poC_-6srHiTk%ziTg3I z!vF+laZ0S`4pY5uC4ctWb0`MqCY~3et$Q67z5` z7n5TtFgfdI4D^;eb^*A@&%vmFKLe)mz4D>dwFWx`A1WKu_+Cte&PXmTxJt&+b2ArBlhhYst` zw#qrPlWgEq$#km1ygpa78UYIt8K`iR43dIct;d1~jigH?99=xR0p>0t$oDVEUN zNwC^K)REivN}Bt?s1`8A?`MEcBs0J?W$}>v-TyfMfs8x^-p@G9At}~6+>tw5geLTh zS_FFnc8i*t0IO?ogRrfh`2Ji|J^8(Xzzk|;JQ%aIto@;`P+_@PxK0b;@_2I=kn%%o zgog>L5cN>q=z;Ez+>3eg(sRT5geaCK8p5Kpr_E(`tgH!uW-MNyf$wtn z6#l=Bt(`jbVuGDUMR&4eAe4g1*!u6r!|xkY%xu(2W+SH#YPoRY1d zIjBB!N_G!-4i5GVxZkU}0e1}VpOXE%PD#`H*1`RTZ%QnH6|!DGhx;P=5sAWW-ql#0As@UqtNQ9Eh;1|%==<7IipAFuq~qO0+`lh=)Z0kcKFx^l(% zvKde2b5~^%Bc**b4DBviMaWg%x(h_-akx{4BiC zf)w1ruY;D?{T_z2rLf~F!mdOq!aG)bsI}2SDat-Fz{S3#=EG$g@xEbsr(weLB_1pM zzHLKAGbq=&?1SrvIhYk&;#;?^9e)dgT=dyI;iF}ngKR{FAJQ@q<3c&TtZ~%6h%VIC zkw~t3N&RVxLkA5~HqzxZh5G8c5KOpFknk|14{1vE2x4w1A7*ybpRt1tR+11JGDo|P zFo+8wRdXPM1-aV}G-EqqN)aZDwoQ)r9-#lPz_72L%`nCh9uOMr>#)j(Tj*cMS%>RS zPZ-3sOVEMfqzT_k&2#d>%}0cI4}-b?ASU^C)#Gu_`_^%ilGGSeZMCzP&OYgD59M#Z z2EouNEi#xY&>E}?P^i1if?F(z;F5xWds3TuWUKxDU}5KSsNQZOYS?eTyQ?FLWjyxB zKMkkg2Lp*u)*?6-u-_XE^sUSuYzvuivGq*PQZ__mXCn9e@B~X7wJhz%;*I-%VHQey zL=C9kFkzP$4h$MKE$`j{)Am#1X_F=vwJ}`EVE^^3t`k!(Ij=x~O_ z!CRC)JEtv?4*HHkX3X;51Mm`|CNJ@R?6n*Wrl#G~W)GzLi<{ zI>pyTlm!uOJduP~9mD6Enl?OEQg&jEl98LR_=#%YJY&{F&}qTw226T!MpFV+cpbIO zhq#Puo1bu$3?x*0Tz}>MQ?xOAgwh_zDWg{2jNpM~;A#N-qAV)L75Ij1Q`KkDnHU7@ z_8?Ka>A#2R5Cf(p%nrJ*&tEahEK(Gw-Two{*0nF;ITJ88xEJ@Kgt8zdKUE)L)pba3 z!R{vgA>pmyHcVVM>M#4|=Xfho;uojN2TRFtbs%mq;4+<>W>rZ1RLt#hWNs1QJ%rs> z9J0Ht4i4eCS$=n-47=a`&d+#DKEC^(|6Z65e@EPxsO--?A@{#Qlb-=V{@$f?u)>D2 zhPY)#9PXfrC)u1z%m9{fp^4Yga()q5EV3Ocz&sbYwMD!C##CA&7|4cy#wQUyQDsae z5;;@i(OeFW8;sl#X3wS<`z$+B9u$RC1ttr`*+h}>D14x7XoJ(|j5v%%tu6rB-Q~EA z0}E%X4+X=3yB(C-;1{!ilzLU*f)nKB4o+sK$_&67%{1{5C2rrg3I^6T-(<3v zecN)O*?NvuvasbsY&apn)Zxf4s$$E-Mwutlb6+At({O-?B zVtW+G3+T55#vH?AQiLJ}nqUv#!xEG zMq0u$J->@^<%kh@EY_j7!ABofJLH(3qTE|nfga>OsRb4UGxuEaTCZF?+sz9&&6pn$ z-ZbyR&g>7|iey4jc$={IhT_q5D0ZZ@GM=f(C{JZ1luTEbM&hxOiug*l)DAU5F}bpd;>{KX}y`_cXYF#}ALj2Polta_kVgA-4QPWKLFRIMU4<{=>)j zfDWVg+S)vLn;V#N*t2}|5|HfU#3x48$6uTO#Q=BmUibG=Hk69oZ=me&dMr2bL$L4d z-umR}v=MSK@_X=Kcz`f;lzLHcVk+Evb6cGb&!rKD8G!h7w;Mb~*hx|S(WhI62 z2|YK<7Yq0;D7ghfIp`F6fjq<6n+>fD{6MAvN~_RWh3c6V1@oF3RqcIN-WO`|G@9{{w5)i~DSJlz5Pt-N~i63`%L&Y#hMtUmH};m=BpY2Kx~nOFq9PD&4U|GJF2tcO$%?>CNy}U@kxq&)>54HA6~Rh6%g#y4 z&b0pXlA|wzdL@GQ()R#EJFAa;-NY@Uw!PMT1d*8+vAPj-2TXTCmyG~j5992 z8e0q$qE5)#6@_A53JmS?7Ol0dVIj@K%4!+5iRY3si4eVh9j(I) zBC}T}CY*H=9nmPs&$GU=(-P`{rPh7s9kKP2ue9Ss-^%JtNVEWgt17glNr z!6K@d3Pr?2(}F`i?FHu(YCs{qmppE`TExIbRF^mekGCTJn)`i>a(!tDKDQ_<^MzN5 zA0LQ0Plp<+6K%=xw|*H{@to_s>oMxangJ<$_n0xTVu|@3Sq^lAMu$@lO&9&DqjE9m zu&AZ><~mA;0Z|ipq(?HuI)d#-l#XHCWEU6Q}4Ip1_mz#+W=a z!dRr97awpvcsZU!-Seh9iPEYs_!o)T;mCP&72k%)aK9%=Af*PN;6H=59mnH{*O;Bb z;YVyVR*Mo;zt|?_x6@uPJP2xu`k3i;pQGgdz?#l@!~J=@-gW=`$T{Pp8ykeTkiuSM z8f`*Q4tTGVePo#Alk)!M^L&9u0;bsk)#+!GUJ%i&uo*E49XE^)n>WN&eU}JYfm3>g zHvqZ6;pM3jgj-PfuY;9x*ysL5UK9?o*m}Xe_H$SE1c{yq4h=K7w8>4_z6x)O@RUg8 zUamWhtN;oJz(-(J%@2QdTcu{cv{Ll6Zj1H6E5SEAEA2D#^8Ih;ewsa(eEtm%bo z&^Oc?F_aZ{e>8f|s7?fE2b$MTTFOPL)9x=Jz5!nLmZ;!@`vwced5+B;h;m!CgiSxS z)u7d+1vSU6#6CwYLmYx|>0G@)@EFJiGBMIxV$s_tpa!`Ldw{s>^fGlB zES&R-Cc{-GX0P9l^Mg1b5vQ1SO&MP7RSV2=aoqWwF$2JpXbt`Gu)YCZI>30F8mMEY zzB9?y;*j9VD(l0CGG2{l=_9X30fM=I`32~&7ED~$Fg~^Tc8S1F<;tkHhV2IJ6z!z$ zf-f=;%a^kl|83Prr1tu$8%egl&Yktyi_6QKyOZGRgwf>k9p~NTZ4(jP(pbjV5U;Vz zs(j(K`(Pt4PtWcuW-tI9&c#`z<`Am75Y$9>>Nw={7meye;q^B+pu@v79lQ@zc5{>W zaS_aLlTUHGPd2hg`y+lI9D0hD9uZB4bIV>sBDX^pQ&1EV?JLMqN`Eh_JHonNqR-DE zj)ij4ZtoEMv|K1bp_lgWPf&T%+u2-!eF4f*QMz}KP&98CpbP8EB#ebTB}jo}JxqS+ z+o;Hl!*MKj0VRaWEccs#0(^IgOH40k74T>wn?W_S9q>@^ps z7h%Pnz;}Pb2+zXJ*b2zBS|d*ABz73U{vF_9 zaQz@|CCDOD^9zPCzl7~CcWJ{g++V`THrOhR4RiBgEE#cs9}xou!@@*SwdoQ{D2*q% zuhpjI#eSEK>)iCgE5KtUpgvO==m%WmQeWx`s)bl0h*yhb*h(4P9pV~OD{vmxrOm(= zILyG}cEx(mvw|8wd>q`zJ+c7G1!@w<91wmJFV6x_2sE4pp8-ldb}tuMUp#0?LvCZM zueI1Wf*KIeUX!S+1=IqMK6S|#6dHK3*^H|61xbM;Lx??LR0X^>Ps5{e(P8UJcw2|O z1R>cq)aD!!`lqvM6ZVvAinmoV7(-)KzbRB|>`3>s`j? ze1zt0c(F}245|?GQ`1av(Cb-s?Y;0AS!hP0XI!m=JR`4gdleY8a@&kmk-~V8WD=3e zRda?hGryz-#W5E1>Bc;vyqqZ~2@$(zOY0(lKpu70G&OCgk#F#AivEjBi6xl$pMJ8q zPM0?uA_I59#NzoR2jGwXw>0{AddMqs9znA)Qe0}UV2~cm;SE>r-H52vH6XeU%IXmM z(73`&GpI$H#937KA6oQEUqw7XZnc*Cf3 zZ()eq3VFoI0eg}gVUmfHi!AK45G-LRWg1qHAtRy09pE#-4pc`J^Qsxxw!aMDNtn-GPlEOzgWzNDI1cbDBL~gI3y`~8^3utF@ z()7ew2u$_B9y@Q-5;xMd5xz!p0Bw7_n%G~Jr=Ny zZ;ZRi;cLc%C+_C|*_6?k;ecP`QWKnbT=sjN?f&K0CZYZ>ph`61`ZHXA$GM1rMf0ISWgX}F*ljVvv@Aps=!A<$L|o!cquUZn)?T8SNT)+N zY{vMxF_G>>91da=ey`@W^@X2*>>;jo>9~6vT^Yg+_7g0SX545?zCH<|aZWgo;3`qC z8^5KL7+hx{Dp-nlB+o%M3Dy_!c!$BJj>OX(UtjU{ zHJ@%s_d?h$1;K0O_z((jzo2vBeMod%N^3jBGX2DwUk82R($M`>ELviRl91Sr#KHj1 zrQs&Ktvpg63YCN+2^g*qClldNq%x6BmZT%qalD5s8|`Q+k%6jZx+E4IidR%b29seG zik<~+gjSL=*|Jci8&bpYD4GbRlc_ZPf|jRJ(bCcs#XhgKM?(pi$B)4GPj@1ACShk1 z@o+jFi-l6ho5PWkuya9`X6})s5^F6o?Y40Dr(| z+4evHCMuxWi0>V=$_AnFXhkDrxC7DyUv(f|))R>Unz5C>vbGjah7U(iQD7Fb|9nY| z#Qce16qkSKx_EqT1GQEl3lEk2X70-lcST_T1kdADG5DqB0Qr{m*M2K(<=~`}QHQLY zei*NZ&q+yd)i?V+)qJ!;H;MY~&}b(dTrvWF;<0Fw#gr#P7D`5ipc$XAlJ%|Sx~Sgm z1pT1~)Wc!$brf6H50gRB79Dq_SPt3%tqEy3#CWUw;gFMAkTlhkheJ-j+_ZB2x_uX{ zFh*S>J3_vCM$R&E6m5}4j+U~Hy~T>*!&@4FzfyxQ5WOD<_wRlmM9{DYMGJm7 z0+g_-4sK5hg6YNypkmq(Xxjp^odii9_hFv+hZr0rFbnqZJOe6o4>3N&q!n+C(K%0z zz```R1M9>MPa)9D~HVi-X#5EDCX zhVS|E+Tt|MguDC{^j3jA%*)VeFhzZx%UAz!!X$Bq)ZKTT8l+}uv(?L;PS8@(i$#cDgct$s7?`*%I zT>W`>2!D{f<85s1s_^vgIG#bfb9~-&i&Upt-!E`?X0)arN^Xcsilf>jJ1G{6ok>|K z!|+wK0Nu8Z2w%56MCJDL6nClx5j((c`&7#Tn0dmYuEXauiq{q;;{%t1kSc$$`b0Zm z#r_s^C~6FMH!tjDdBJPIt|Rqu$X%_!X3P{SP=rOUdx`SNk=nvDcK?3XEIg{GvPy}& z)K7BckMl~Y#DSFZ0;1#PkdU)Pt?|qtv!4*3Y*(4mmLwtJ;D{bIU>5H>e#a&f6o4x# z7BTF856#J0)2Lz1{VP1DN)$KeK@$rd6bnEa&sLY`keg_L&(pTAK8nDCTOv{sx)zVc zL*b50IEs_LG@dHK$s3ACzWAUt=2+3v@}JE8X5Ck(d>MC2bST6MUNYba#{l&2{l z!~}wmO;C|eFvnV$&;B?&9uPz5n>N!(AjEy~e+hg9-#Tl$^M^kGfmfwqn?y|>wlXvD&1+k4O_$be#rePJogv) zeA%!dASoA5yiFR$91jqJev#vlYtj-cN)!2g&S^d^J2A$&6qjaWj1;G*qDoqFiSMU4 z%N6W`pt?eil|=$qx#Sz8g@yQ4f*njlD{1rKTB5`onM&CO^jzmD9VFC9dR89#|il;pkt8lT7*r*9ARB(DJi)rh=`UF)`uJ&C;Yw_Lh#m38;`l!X1K$| zt>zD~TILHJKY#g~ciG+dl0OT{6sbi9nS`79w z)|8Ae1nnSU!a8kt5&eNatvm5A;jwWacl|}NwUBs2=HeOb7g)SONlq$3IHe&sdpffS5BN-*{ma6?`v{Bzu^y% z*ePD=#58#2Md6?1If%pTjcgr}hP%c%*o*;*oqC`KD^G42V| zJmu3xIXHY_L&V(VLhEPzl@O`@A7QAPE*X|MVN!32Q%ypWNmB$!#&j&h1_c--Fi_30 zE2_^R$vE6(!W#|_&g;DSX+bP~BZJ7tK5OC(QXDM!&iYv$Y+#wy@!$B64_hjD-sEVVMbqA;fXjx9cZ-y5QZ*>Ma6x4VK0u0Kg}+s#;h} z8EFlie`DP;2yyWQc$OV^e+1nrA0q`|W(>hTK?4HZI8W+WTq}f~NW1!ko|h3@Zv-*g zl%6Hb86jiC-|zkv1|#ME8p4Pt zyUn{O=|@x&!dcW4)S?>0rnLk|W7woO@vVstlL3`}YYBEAJf;E>1%D6oj&SfOAI+G= z04V})#Q*NULaRF4;1(U*0Cx+JMScrrrah^_38BE$9wzb?x!xk?O6EZ1P5cl*W)*k; ziAgU>=BV#CP61q^bZq>sRtO~xx1!KO9jX;G^;I%rT_PBl*L#q1D9tp&vlr%-u53j*F1_YMDMNY^=!?#G+a~L@u_ZPhGCR)+1 z2Rzn>s1*z*uyg?kC%isr90>XN89q(HFye5y1O{?L@nod5G}amaVskjUFcm&B991px zk|c~+MdNn3Ri)LXw()o}e7rK5iiD$)=8a@18cRjf;rP~2e>@%CkC$k7s^WwShHGNp zq43XwKiX305dP?%SVyRPjT)PeXCQF_cL}H+J}cMfaqT&XWeFAC5X2zB$aw*&u6k>&6 z&C677GIT)u2H$R)YvH&Dhzz8fkg0)7Ty}7dJF$bpMYWuDeUSBbu=Y}JhPy$L41$Mt zX6brPCf$8FOMbqF6I+Cmy6FvD>#}J+g4z>#Utnt%IST;-blxH7SoXC*=mj)JiVoU} zMj-e5{Y3>FeREYOqL!%Q6g|B}{O0}n(PyB#Q(Vhw-)(enk)^`@J1EciPQCf9pc%xV zufiAM9EMj^>HFOu#uzsFAEQMbkiGgJe*;dB3;reCWd)a&a&034zTzTG5>j$>8)l5c zatJ6EpfBH_rW-}|cI5~#PiXqL+VK&XG7t*@2w`>&h8FMxQxn>7=#!ua$!VVQN=Vf5 zXOlwsbVLMYxlkD<9p0%rN}-XCy3u-die%TNFyI7N-m4>L_Hnm6S(q3`$`-Z3?RDZP zBh>-b$-e_lYLgZ&?AFjlRTr-;5BaM#W8k5%wg#C+X@z!B*s$ivqFLe8)Q7|(;{uA_ z%7-I6wkzL?S(-Y66z5qayjwX+&xlG9H*=~Z0h(}xxkF6v6013u4t<7`qMmJM1s!$6pe{+-Q5xw>Qm z;e~a|E$)_3oC<_Ug?KOSr0r*OWdt7DSkbv7mx=p7EgKoV9R`zBj}3b=7zhGmhq8?< zq7_y?5dfQfO&YU|;kzC3lD#K12Jt50+z9LtIF^v$axl2MvMSa-0RvZ2Pog|=Ya>9W z6gqTUSTd!&(>lk45iOIrV=|Q#95ljSUz~Zb3opWn$JlmM1=+>!A}XPtR)w@K6`72v zU1v38V%X)1DYl8u|3%ITr<8Por}M{ zjVV*FBSMim8nn)D>?&CrS|en)^oWBeQ;6Jmi6hf8&TnNw<-t#&3ZW30~Q@ z5sDharepLa=(ElNjLG3r>h}u+k_fK|4m|~vm53rlh0uI*h(=8k;0gkc>n-{MmPeeW zXa+A>DKiM66iS!u+}N+eJv`E_BD-T-rr^n7JegYjbC|F{OO(B)(Z=o09D$u+pkYAy zh;CO1i~uN_C=)EcLeL?0`ml(0@R%CqYa{@C6C>1okl4jOo86a{8YN@vq;NVR zS98-I%UC(b$8G~SOJ^bzn1IFY?AC0!%B=5&%hqAm=Ju3~7HZJkC?WDV>n7=ZSj-{M7EjPZk06BAM0#$L?{-vfUMb4qE36$2@*Tds--0*#_%-8(k1$rH+^^#W&i~vmVj0!e5~C4G z`$4}2ku7Wo(SigwIFV`4awr%So1uKuYuK%{Yy9#a6dxsdZ9I|ULwt>RXqmdpnBl9 zaEXOrgqW3q;pZ4m#`h0mfeCAD$QzM%$bz)8ruR9DaN2{~IyNT^IvcvM$Ee>Cp;u?k zvM_E!i6LgVY*OCj%`z6ooicy47g5iBUf#Xwvrr{Mq^qo3V27_`xOh1)Orx+?)AT+^ z3%Kjx#t1f)SMNa;9aD&iYa}4zmUds|7I{ ztd})pAH!E=`$CIr^Y5;NV__3g!2bSjcr1UuJj26{7t7b+o%|!rO>-`Vw*W!SLq7Ep zv@Xa_9ugSW=>9d5HGl;2PyS0lxm77fFEZdsz{U@DqS$4bD5O-56xvW%Um7*ue7 zURs$fDGw)8nUZuxEEP+}GU?J(MLJ!bvQr0Q(ReJ`m`tZDD=XrO@|2xO!y|f0Dts^& z>nv4)s;YP-RvLnR-((V=&%^PONHpBh7K_8gbNW!UIkgy7-te?2yfk*QD@w+1p+y+Kdt$2?)=)RKCZQ+@8E z&Myr6ozo4>&m!PJ!rO-T3FInkJX<_^*G7cjui-Ct{EhVSqb2Yu7>^eIs0nd)g=qCIbA&u5eSGZa{FKM^@Ek1k=1+i|(YF;o+Wn z1$rC+cE_6P6@^SEyg*BFweiA<@_2Qoyep9qsqNm2$(Ra(r{hV$G;%T#gR}ZXJdumX zD`V9Z%}!q)O4P*<5SdVuV)5+2x$f%NLn1q!rxWpt()ON;3Qr55eq|z=s;o`KTT-c1 zM@MIiNS4)#vTNP6rwL6hOXLcPWPKtV%Z!#MOJT+hZ9H35-kqf+y*ip5=_(O=lb0vl z11`H9p@$=430^*4%<$f@(ggc!4SZK3b>SEjjP7h|Q~3l3K$T4QNt&+;rRZtvUq7`v4isJBlV@R*c}W4<<&cJ*^WNZzB;$Wb!YjJ*ozGr z6_`j%*2P%UmD8`&9KVv9aE3vzyv6-1NT}2mNVu64^W)v1=PbUn`qa&% z0lezs-LjX^Cgk%|A4pKkM>%kJfudHzs$CLZnQpb&yj$HvMfZF3uW!necx9t$C&R5Qj|El-llq%ELr2+|ll=hlu~GY)xb z+|z$H1$`aPMuE2(Cp0yPu1@H3@mO zO;C@Sz6w?+zo`iiVCUefi4$9$go6!@t}o<78MKXH=_G?Xw&!8tG{Ta8jF>Y31BUn` zN+s%`fsN3VnykEOE7_D+yd6MO?4uP42#1v0u)cn&G!zb7wt>9YVxl|Z%us6itjb*_ zs0xYsy$dMwP&167!6+(EEG35XM1lJ7Ua!af11z-eZfp7>9DMKK(j&A%kM{q7U}t+E z$c&XslrT#~*{RF8e}TdKE?8)l|I?K5W%rl&T{C{nlXSmmyk*EE@b5gZ~|l3U$4UqwRigx{DYwsHUwD}a>u*5Ruj2r@Tv zt`suApfBRH5O*#@vtw1xQIh1^gs>fkV;y}LKvd}~uXhfBix}35F!4k=X3;$exv%}D zpdvzG0?v_sF3$~wMEFtrc4?sfL-gXcXVwo2Y&_Cbk|^2giPfZHRi)v0qP{eGrP4Xr z)}4mNAAB9Ak|FpVg!?o6izcGUgwq;T*TV6-p8CXe5=)U zh7<8rBm*QT_O0Bg;rqwh+=Oo%fib)L2Vq!IXfaW-Hp~l=b0dgwtA;yd%S@2cvIX5# ze1I`>B%i{gGR4CvS5*b*ElANNDOSaFurLn^Q5S4+T@=T>LBN0l%GmZoKJ!+1Ak#D2-LwCYyeIsBXGiK z`)OX521ye*JK0j!r8J9VX)9ZiZ#Oa>;&`OP zxxvLhcZ=vttC8GSraF^0ag=yV+pX&EM!k2?gtm?&?A@tRpoZw3d}#8l(OPQ&hGD_; z`CK1=u=omJd2kWA%gJ97g0>#RfV(`nI*j7i@F9TTX(VkOKDGK1i#yVP{U*jG?O z+kS2$vszEG@6ZDG^cC%3wCxx+U1-OrwYb+i086d1=q<5!J%zGP(;}%RAI#RUgayM3 zR~X`tp zSAPY9WN2%HI>U%1fL$sTeu0FMu zPdH7UtDxeVM#zX63Hgm1Mua{Lqecmg5y$YGATAn(hruAkny^@{7=R56IRFVv3}#T( zh$Fv=hG(MI?bHe9UE)qPIO6LQVv2rs)GvP3fiiTG{aysr=E-4_QQWD{AxyM7a7)sxj(s6{Sc0Xd1&re zX78%w>gbMUdk-DpaEP$S1F;9vUFlS^#`_RH!-(%~Qb(CW%wu0rV#>FDf-!k^qFsg6 zP3XrQL`x^lF>Qc30K@)bts3By3adCHP(_18LHS?wDf)b54_omE#T+Pus zwTFEjQ?DX(5`c6C+Ea+PXD3D;+65NlY<1YCoLDnkS}H? z6Syiyu+VOCh-=~Tb`%20DC0yGvtMv992g7+Cm1nSC3?#j)eEs#Um_xP5nMv64dl{n+g(ODINgUy~0nbaUtB5vwP0)o|D*ga~Vj}6OwD?2ktlK~E z{EFB@2!|x#7kt*^CqXOX@HA?7VBN*J5cz{R?4D2{6pVOoBPpOXyuOCuznE~4M$CiJ zC~S+vE_uR+b@2?$0YtFnxPIBfH3ma${n`N~(ikG8G|G`EOe?v}^fApa1A&IaXP**O z&Q?93fp9hyMzeukhd8LWJ7j2kxzyf1M1+dTGHdW`-RIkpRut3D#rAVWPYZxwuuUx_ zvkAl7gY#QfVFpVG%dnG~JVy~aDOrpJwW|q^_EHQ*4{2Q(2>M{(i@N1W9^1DlcIr7i zjNp<6qj(ySHM3R%(Gmh0#lF3QpM3x*oV<)!k$niMq zMDjQ@wvU(j{qOs#P+)^C=S=3Du$#sAecxN}yYIgD?uw28H$GEA8P%Jsua3bC2<)k^ z^=f}TL-<=mnp(8?pNKU1GS*P(9iyvu;=QZt?cjM#RZbVoPncngkvj7haO6@>o!)q* z@T~g8cFOOI5E_s~XYI~ry(LBy^l6OeE~7>|*bN9fba%}M!Uf}Hn=aA)8%Cszx85%C z$Nfpe4tudp>MQpVPyum8ekfrYBnM~UhK8OY#a`C{+oukh>&)+ZA-Y3-xwvu+-4qNR zI(RToF4O&t7;U>ofl0Tk+TM)d*&5R6@t&rmFrr=zy(ZP!oA-F~2xxyfa#G0mjEmv8Pgk0AOgd?SnF+KG566}e8(@k)L zDK%DT7a~2~Us&R>19?Q0%^rxPg79d1nsWY=%r@$UL7NEnHE)iv`1TQ@k>y zI#n16h!br%cv($bNU*zZt_`hB|M9RoRM_~2od@pubKRmgH=POE*=0BBE?lh>&*WvQ zVMbW{1{*HmEO*;6xM}0}-I7cL%lZRIj56XWsR$JH|N9CDK&$s0tv)~+;Pq74I&GoJExyZ!YiOdBCaFF{R6RRqt4DZqg!Lm4H;9ZDO`-4paM<}4bg_idj5}1BrxeoV*0|` zj>qcbjrCEuh?>%&gk9kltC`s2?AS>hyo&%N90?M=aq-vO+9mXfPlaeg8YA5GzJ_wV z)?1~Uk>&kg`Nfxu7h7+5-x~`hcE?-Lbl^|?2cF%!J{BVe9Y6r=IgZ zb=dpV5${vO-lvXwpBnN0?lCX$-FV_o)gOnyM3m@(nc~;J^+&p{P?;i7h zKJiNQSEBzU`UBB7qqn0I%i9VY*MI(v)c)n~rfOObMt?v0wdmi8{&e(<(I1QcaP;3s zznyrL_^DVV`X_b4#Q&N2H;I3l_-5iCCjM^XEBvkaulU~gj(IP>KmPm2yg!WOtEy_l zKlRQ#@BHBUs;b^!aFOmv{j8-zRaJfehowAHzip`?T^;|slz1mlRn`BwpDU%_{F0yQ z`_51Msm``XeyYCS%069H)w#}6l&!t~-aGH)t(t+`|J2VoF!wb-RqMJiL?b`&8+u0< z1{N(v7rIfYkUm^-ihQ@-TANQARoNhRa9l)^96c zgw*Sn3X__)6mTAxvXllnX(_>Z!cv0s-=;ob6{e9`sp|UwWGM=F?zb)EX{r6Be#ug8q<+~_t)#wTseN>Mqowwe+F+?Yq*^Sso0Oa2 zT~+z2zJF;ick*(SUJ!+{IQvZum`FB_&{jN9b0Pw%J&&?F6u~ZYOxTP9NHCw8Il`TAf=N+Xk zSPG=AI$^0Ksb?%zN2UPyNCZ9`o)m0~VBetuq`-8gQtNT}V|D^8ybbw~B~>SW|kBL6w^+mUZY{z2sD zB7Z&dlabFwK3-Rq_@l({C;I;b#OOB@|03~AiGP&%dg6ag{7mAn)cuXR|1t5G>;6*R z57)h0cdu@?ZnW-7@_O=m-PO{6#rn^k_TG8_kNJHqBpr$7z`8E{;MOLtR_!1u@7%c< z4|7N^fL34+39&d8!=jM``M&u zJck5z1KG^M)(lDyTX@Lj7xCw@H2r$%c_D)y%F>jd*FtGbG=?zNC2wY7VJ0IlBe`+E zN#8-m_-G=8JG^MuJn_V{3$OWK=QCs3$+_t_KjMG2-~nT=_n>Dbycx8ob?%>L_fM1ir_ufMBfmD*QtbTb zvnW5R_R;ByE&gaEQztCJ?aX?=7f5E)&3-R{T4U)oj`HgLaix3elIN>J2AvIEHfIZN zJR7 zo+Bxk+v(TjJ0hRSr2Lvj=d*XW`E#Fsb0IU9+f;&9PB93m2%=XNXAO+x za;Kj?=zp77To@=NvvYlZw#>cTQfZyf_4o+PnwmzFxyv6A>n7JJav7*9M!tE{+xeN+ z_fC8KJny~V`rZrPZ~WFzhLFJ^fvbAIt149YXN5<-L2TZ_^`J@?EoKA;xiS1cWD1WY z@%X5m1EF4#o+&&M?|jFGP!cs+d85fJnn$Z#;SuUC*m}!5>3HFh6y#>)2Jz7@@?-li zmf<7uxktSiDz;gv+2Ss{@K6Wq(O8THS6127tJ^_*m5kjgJd#R=X|O+6=Xu#IHMYow zu2)kpDINe_D7^R4z$XsrN`mw#Bn|JvBP2U0u6a^{d(^LVdoYq6MVQ10j0+I-LgV@A zOzzu<1OHeu%6*%Zi$K&%g+~%qVTHoI+(XG9zY>KZa*l zFXYL&=p)^dZpq)qL)~$n3&Wz0Me_BHsZFUyfP?01;n6lVbvP8rlQ!^pW@C0Z9LT6U zvwWV2O7w+NjX`opC@`fjI?$()GwJ}`gNqqtSO)Aqr`u%dMa(L45N&+7Q}+%EM&zOr zk=&yu4WdI0d<>hz9J6b0)-y?J`6)i^3I*?yvs*bg%56(#Y#NABlTFE1Jl0@|I8E*@ zWvLEUFXA6`Uho#%V8mu!5-l)Wtys*tF)fo{aqe^{L7tHXBx_j0(Z+=NniKISE zDj82;+K=$>zyaNo>-sjd=pq&?SVL%alck9`>SWo2O8`poPklAzMj{Db@V?NCH7a$s zU^buUIf?;(GyleGw#-G7rmTqlG+rq*zN?-Pb$^(Q|Zxhl$}{3VX6ARqItUEd9Q0}Zz8?XOU{fl z2lD;v{Nm80n!ziJR34FAy48?GRfsU{AgI1ZwHT9jiB2U*zNRs}8jfXi*-=!sWp3&w z88bwk0E`yo14Ez=LRYsUnxq&=!~jsHiXq(}*n?l!QP6=Gs%{`uon4%mNl$`6dOjGc zzDVg$Jn!@!%htQ`3 z-^!2#kXJSI;k=D>Hy?snzsh$BsHiVn&?bc}EU-GY+y=w4N&pgi=mu#=rRw=HhERR~ zIn`@6)rA+tF|H|i-qo%>)v||tm=}(s-g*zcYLUW^QThFCQGI))KHeXYO!-Jn;|C*f zxXgtEq4@Z8_D(uyp~GBfvGAN89Yw-icqB#`TLdxh@35&B9*G4Wj|K4z_-Hrg4tW3+ zM)gK(yNXY5O8D+b8c#<{{%;Hf!y&%V;lJ2{WdYva7`O)+kyNcTi(`Lc*NCK=D zL*5cZUc!x;)`sxqp4=KzK-m_wu`{VHro}j5LjZ$1{@ycz zPi(7$5J*BJ_rQVrI&Wh%gkTfRE_1eHp%Ly1k8gl+go<-Lnq^lK#u(D#6oHTlhK-sH zoN_Rd0ZHE4cQ%JTIdU_s=&XZs=L5I#|1OXTb6@tb>ENX63|ZZ59<7dYz=H&((Ydva z<0SZvKA+p}PlqFSP&pSx7d<*w+8abj%pkk4-4qls*?F{=cRe+RdwZF#F8H;1#5Z~2 z`Bu5Ocq9^nkz*P=liQkreHwar9m^0y0d4Voe>N1Fo75831Z)V!ah@(C9u8YTKvH~s z3Qh`LtlmvwNEDd`3LM=LZ_kb}Td6qS*AmSOIC{W~l}P;4l3kg{(LxXIl`*lKzJ+%K zD}KxiPmkTw?yU(vW8SwO?VxN|0o7O?1B{M5<;A#`;OpI#%}Wd9mM{e%*`mG>s`0}c zvHw5(sDypB@jEdScwC8x!WF=N0oz`>s15ri6re29iocw8V>viAecJ$KyC?SZD3n8Q zXYs;d$R@%ZYtWhNvXI6EFS}&r@Ti{0+Hf>Km(_7k9s_NR$E)#s#vWY)*$MXNTWrui zZXwg;@~}iiICm7dh37lz06W6I4bP4`PDl~-%$~5kli9|-trAyvcu{=Rp<^w2_g-F; zN_KV+4ttogST9a$q-OhIkEfV_4spBa@(Ht3f3#CY2IRigCFP2XLG35UNwMkEWaC*g z8jU!^2Ls_2y=kbfA)=zw5y~6N)%5cEm8cZ@9!WTf;C!jHs6T>jBUUFuF5%GWY6zr( zOXu4?p=#YSW>8mmXUY*aB$V&vH1N?D{135jga8nWMJE`O&+geBw$5o*l6klLm5#6b zL$AoMerZchMdX?Ak?F4Wn@A&umpMAZ@Xv-k_Ic1N82C7b4>}MSZW%Lv4+MlwD#-8s zeVu&WI%p4tSg0D@s*7*@>YoHQ3;nm%hs>(S(C=We?vJnHG}D^8NYg0racl8mg(Ww^6{QvK z&}YDlIHxo2MzDnUcemN72ggEzX-&yVnte-z#6r~`4TWMe=}~qz1r>5Yj$z9IMF56U zp!g`A%7b2P8=4axDt8JAoE4<5)PYT#2WmAM93$Mx2;Mr;F4Y9pQM*L!)g&=w-FxVW zm(`(M=hv$j(GYX(EMb#FQsm=?+~~QTJc)PZ>A5_eDN(Of>F}d{{f$U?p1UPLSGj}n z>gk+AOMA}6ZT5|*?9htH*$~wGdi^vZ_uhrw6>!L^DRxiDmW8DuTEgUqv_*C zQ#fQ=dym3wa19e1Hf+#BG%rVaw>KQL?I~CtxaUYN+6g*yXGNI?BPe%55tua-f3dA_ z-+)cTT~8WQ7SgL|ZA)`(M?I&|jNCy;!j%HOy?UYo3IXh5Am(HQSnJm7e3 z>-xrq`eYp%czef-+?HfwU7~urDi~<5ioS#10xajMs-In# zif;tA1#Um`pBgiL-_W`Q8NDIfJcII;rd%^)U zIkmBE9Em_tI4i=Vc(_-%o!S}>6)zt9wcv(MEljf~*=* zhxZF>b`=|bJ(zV4uWk@Z>-)9h;U!nJC-@GeD z%D0SlunoPR0QYkJp3#;fE74JI-fVRKNMDV3+6~NEZ*#ncON4d@)Id?U{DcKEv^zpEM4yo%e z*0d>YlG=iKGPG&CpkB^KG=t_^>G=6Q+CGMxmDv#ntL>(q?c8w0l4F9&R#AYhTD)7e z$hV>jk8PJOeOn`#J4%heG~k=nVGOTX*AL#H`q$&n3OI-Gt_qFTbd+T2SPB$>h)L+W z(N3oe$ME8(E2MV^Xqgs}-nMPSd>lTPIX3?o8Fo}ha7!T4@4`+Ehr^s3D&YNED3Fz5 z{MEp_?SUi3Usel&y5e62u3P$Asi8|ipB4$?N=Hf?!F7$KRwrhI2J^%=YM#~Zhl|5Z zOw$28dq7QaXd~wn8WPUpxw(#Mpcg4Pn|~G6U&!PN&Zj+C9o)2lmAO(o zh8t-@^Ud3f48=}{BE_dEwlh!UAQ7$-NJqK!aKfjh^JLp074&U|IGV2?cK_nc+K=wj;heno#rj6 zQzh-k@>@y!c~KRe)sL+Ydw0gG8ONW1bGGoBy7m?fg)-pBLtgRA%*ZB-_ViRO>#q=u z*Ta*5m1#D~8aE{tyw zUe^>`{smWcirc6g+EeXKqwAbREk!E2bYNGmvbv{#kCR`oXXKBl^I-MFr!VuzCbT5^Tw^-Fm#oyNLR6os>P@f-iU zTs#KHMhg$#q{P*&>qFkuB)jHEROYb96^fJ416?(`3On?Um+E9W`bhe8C^9yMSRzwciRhPjj)M5SV95*dRrV<7 zRNn>p5+7kaxj>)gH8c^9EV5+_`Oj0}{<=_-xZ!dJVWF_`D_(fGq!0T;)wgia>`b1i zYLLhUb~w%xj7?1i&hYk`a6PfR9}C4duJTWXA}*$V;i0(ch2z!XX*?~lQ%vhIQ60YKr;I`6!tXJdGPa7;V(7x_k|6YHG=^w z!9~Z)gP(-(a^-;%=U%?S z9cH8`5hd%la#l^Cb<_}li=*kLCL%8-V*8rg_9W{PKeSMrXu_ax8%jDG>XME18|&9? zs!uj=P1ZL>8aN=wV_*H!887^$p{mBJ>NokZKR*oZzT0rQfQ{Xchrdr8?cU`teDX8< zmOuLk!J4MWVwCo_b#yOZ{59_b!L)lVn09aHfC7sTbATX_Y<4as_d3Le)`T%XxfIb) zxk%zE-GW(Yr{fJBa=pW^tM8qE-uJvT)#={YK2 z5JoMeZxJP2UXWH0KoPPD;hd6pO`@MxeqqKhRepJv;KafjV)d>d?#U|`J``E=-v?U> zNKQ;)d9+gC2FM*jqfd4iY=IQDSM;f0p^9N2&dj8w+~8+^EDOE%OIwKYyi96EG(S)m zc$u4?) z$yQSQ9nZ0FSJv*JU~zgbbqnth(A*R&T|8J!@mA$gF4GN>JF7ByC@kJ^+l{Q@(?#RC(K2`OfIm>`^6GMr&mO3Tp7NOnKZC zRW`(WBNqDjw2d*dRy{1Wp7sH!lPRwqj+ErJ z2%XYTos%*@4Db~OFs%mUbq=y@LM znCfStDaiS1m?-Xix$_L!4ZO9-MVxm4Xfp`(wD-{@P+0!*znd7ao#*lB*u8BZjE;Sf z0PEeo#jhXc=6`B+bnM=W=-9FN=K`Dz>M!QEAO6Xc-*@v%_w3ngU1<2g=C}OWU;f|L z=UD=Ci}Hw&OSNh__*-AUCg*q&1oZ-O;$27c%me-l*H0sD9~@PlIcAcd3@!+Tf%x8136>r5d&8dBRx!WbOkV5dwhpu> z@HgWJj!B_#i6$fjy0l{f@s-WpPNn&ZW2wJe=@dYhz)hzEl_hFV2Q*hYHQH)dmGF^O zr%TE({CPYq1Ke?zhMUVW*4hb_RiT5x0tVu~e$}e);HfGa&#%;Gqw zODVZIP^bkCpx?I!Eq+#wT6Xxag1}~Ok+XsPe1L!DwmDR-H4>1~_RO`ufo~j?E9zJ^ zMi9$2B!7PSC*=}GDN36(W!LP0&?a;5L%u^F#z&sq4ed+A$MP3CL|}l#%7|C>R+v== zXorPTU%NX1bp?JMPnx`Lz&vv7LPyD2KtmXn3yLO>tSB3Pb;&JGMSIEkMIA6^32mP zBhH}$H~)cJlXmFlaK~(&8$R~ba^N5Dd-}h2*WdEwT|XNC>TQIjejv_{oyboVh_eo! zE*yY&w@1(j9!=vKKvI+82=3As;oO*9eFI&0+lT^wU`pNb%n zq?nEwG0mIR)Bsw43)#X0={(*<^V9dh@`FccYE$gm0S)tDxOj0I7skbp)6S;6@v4V* zQlN1^ytLa*@pvI9-fiLS^J1y>z0ql^827v7x$`nU4mL=Hc|Uo|cx2lnJPZ+Qf~;>A z+C#yel&p)akF+G}LUI0kwoyh_U4`C+G1cz7$PdF}FWzsCwPegzn@C}*^QNis-5&^t z_&R=b%XGckxbJ)>?UqX2g9iH8haU4jg51EamZD8wBSmYcjm5GPH7=&UJ_Jv56#2c>Ly;of?c(z1%Fy_gmro z)tK{vm{Gx}ir=QAEp;Bt$VayBP;K%5;bm7I%#^(Pj?{V00Wx7r;Zq&w-B2h5(-F~u z9-cuX7WML5WsX-CxqA+2xP-AsLf$Cab`OrLx&5IS7zJ%aCly?>E}%|`f~ukhKZ)3wozTRz7(?hm;YKs4fTtmZWc{NZY!OzQSeQl9Ly9f8^N-%m5$9L#EnBT^| z$f4oi7Xv z@}h1YK)~YBZzF}eIG~!Un9fWZas<2h)MFiMNNj`a5ZZpW5mbYmR~S0aFTO$I*VPc8I$@t zRB90UxmEl;we4z>{O*vvE|wfP7WNfyzJ3E=Q;;kJG0q3Insa2lW>_K;hTTEhBH{cdUEO%1TebFyj4Vd^IUlm<%sY9TWfD{e$>D8Yc$5P##9a*iTw@3c zD2O}GIuRCJ`Kcee;-!wTF2A_m=fUq8on_ilV^ju zS`-3aDn9#Lcy=oGP}x&?e8j#hUCXO2{PdU(UUjS*rOpRZ18G&MFK%{7=naEIBXuoj zOsC1>5f3;xm2&KmCg7x#Si#7atu`;l$TSYlOCEUGOP~g1J|a!E3Swijivh?1%iA`x zS5U^w!uuJY=BpO?nevhu2|dj-MjrGE_};NLgvB2beeITvbVw51LI{0&mJ_55{A-9u z!;#|O6!7w>pmRS$FhJG=Ve=|CuBCB}sFJJQoR3p-u<$m-L;l_=lH*0X@R3M_^O1=v zEZpd&eO~NNdTy0C_iO|;*9R?HK9kSrcS3SeaI&TN)gv!^_30p-f4LA9^S@h&e-!^d z$XB$E&ke}8*mK7Z)J19VKzPtF+}C6v`Z0>Rl5A)p+|j28Q4JVXER-zVntCc6F8)W_ z*?L2($#Oo+XRu6#?wVs;BV%pg+q{CjJaDuPiv*Wv#EWA$G-pn4RZjAVeoQFFQS)(z5UIaUH<2AeVSXS?zBg*sA3~&nEW>iR>>Q@1 z7vA(cc~a&g4iD<_$@SJYk}U$um=TsC z=oO9>`58cG62OZDy#AE7soPVWMhNQMn2=C0>mdTW14pFr;6)y#fr^!biG(}6;4D(X zTfDwx1j$xVLnt3%my^`ahM@SdkPd~4=_O~oyrm2a$>gFja9v&OS3@HLPp9VNSv}Gd z=DSS;KY)I?vnbHI!aWx(;H-ps*Y$O~otZ9#La6yc{vmB4^|JWSfG1uji?v4)o)69| z>oZ|bTe3N^-W`#$j=In~%g;IOD-nzIDW#ij3c+2dswqBA=`DF>Yu2gATrU>3DNC$P zS^8^Soh3iK8=*-Y&5o$KZehaakMh&&$kW3K(pX=xRwOAOH4}#RA(Cwx^2>I@?AJ0n zy+d$eiL=r-)S$3lIIOMTMD!ha?!oxI0VOVs`fG9MTED(2*<4##ND_`S){jJ*KXNGTro7cVofhK#+tXp<9yhaNH#PlHrJV% zJhHafE*aqW*T$3eqfNC*_Q3VN1s9F5`l&xuth|vX&2n@w)ZsknOB(ZrDMD@mg7m1%tm>75(|(FaGU@=J$hp zKh3%Gbp6GTZhw0DslmI6vx&_YYod4;U+BnAAZ#&(@JvVXjW7LaurFGAzFB;q=Ph-m z=M>p8^UIxM{{<@d@BU3Nz60??cESWMuu%{g+Wj*)Qmg$`2KAoxIIdccCYRfe(f9vBlEqR$Kid%y;g=W*^(0jCh zQdz&fCAdRu)3X{A5=y@s$&#pQnwmADEPk$GG9bqsTTu559=Rz=oivsUNFtn{Y#Zq? zaTW<6#1`0@ItycI$!BhsEAS^JWie_1ELEsMSD_SCI>o8F?7+CjsC@?2h&qxwL%c?R z#~n(Y(cpBtHg@xQCN)2w8lENI3Bo@YK4W#&G*n=)53SR46XxPkYhV~D8#pwSdOm#@et#~7s2GILgYiDh7`%6`=ketGl7}hVMKbkv}p0#`1sA`{MTa1PPOI2mpDG@YFVxXydcHqtc>8O`3c1(^0k0IAE>CaZ8_UEcyRf> z6D_g5v_j=Kt+Cu=qOks<{zIMp2YdVbmcRTa6cchstv*BBAcqujz8(VoEK6+^Va@YTSFFI9zmy+RIc04z-@&+Iv)Ip{L zO-j#{pj0BU+4)p<^mP;?fY}844sLZqbs;I7g;JwS5Yr_|gk-wA{Mw&=oZTj)MNXxV z>uhR1GYcy|wKxaJ@FzbmT1}fiL)M7_x8VRl*>RSO= zXQ~n`b9b^cC~Qyzd;=BKUI+9bs0^B88hRp=sTril2ES2ktF=?ijXw`kC=2kB0*7)* zGsAT%Gm~?h=GatfHoc^dfSroakdomSCXs?!b`<_4%XRsyfACu^c{gRQ!v=4+iNYtc zmdleuL5xvQ?a)32sBM25$tSW^CCo@=W-*0d0>(52(C0Jx z9JjIb43Y|Xs`f7pW6El>L?2K1$V;ZV+?mB32U1?MYf4%FI(=7+-ql>wz(Z#V_i1tuiK$>E{3dC>VKmuw|D@TGH zvjvNb9OG;z>fH)H0c=^$7>zS|j8o*ejrv$BcRRa~>r7pR(##lm$CrO}&#Mhxu6|7> zqtqz64<70Q=S;yv$}SowS_`IBm%5u?{?`L9HoYp;r!|f>hQUH|*Rozf9_J<<)|O6D zS{R@tdy*?Sji8nE+yX;L-H{dX0_T(ocT`!v_w-EzofchDC!`0jO`ifNximA+#Kk;Ew8&&NVjdIETRmy@Td!kHniI$v$KFY95*{t z#nV4N6innR=D=WN8>`U;XeE-~tk#NVp^PwEtU6Dzc2}@w1s~m!ZrtzYT8K)$s?oe> zEPwLH>N}U;Tf*I8dGO0$_{?j~iNT?MNG)0ieO-gy%ir7Z^_GepP|T*!fA+NyfwCK_ zqK_i4c?}%bJ@3HBpD#Q-**INj+J5;Hvx9}Ci0lj^HP7VEoZqq-g zzf$?>CZBE&{ez9gcXp%knqT!z>+3dlnVeuCE{-Nb;Gie~mnmMI**7Cpp-I`#&Qz4u zEbHu7QgF~hf;P*}E(3;wtV^h2-N`gKMXXtti7oD_%<}hszM&3M#R5t1)4AA`l-M5-!IsB^G|ae9w(=@oLx*MW=WhZw zR*+73Fg6XDDBBf*@9woUtX6|ULt#8d{HEv2qlO@{W+yPIcIR?ucey6OmUoO(Q}kDgv%zfg%5KE|x?{P;-W;fcn{Lc{ippO_vjB!p&@6==p1om~sdl2u}Vn%cY!)LO|7{RUcoqNe1FM;4>%U#jHb7$ zKCg4hg&73Lr3g`})(LF-rf@jJRX3MOJ8H-7qMYXxvnX|eMlj%Z=YYF96qYz3{z2!g zBxiG(Hn$_6K0lJWmYts&PaTDF8mUaRa^#XVZ9dhF(p+2VwEZTh=YcLxRAvFMJ#7VW z?Q9oz=I7+YQJ6izZxtqyk=|n*yQQy};@*UY^XaQ2=MJdFGt(29)M;HmxZ=_#JE1LC zaeK!2JD%$AQ&VmuE4AHE-LuWyh#8*o2hH|pb(dID+VL(+_j^_l%cJ60 z);3}aS72`WeK3QdbdyjQ$lDpTk6x+Pt5SoM8amf>7dv|~*Ouzwq&1J1h=tUxIkD4L z3iyL6xOaM!J_2=uiMap}ZW~Qhzq>hiFmg;W* zD=%ANdr9ws4DGOGKnhhsnD_S7BujS#fyhQmqCCqYv{- zZBDgN6{uUwzx?8-Hg{Kc(2&^bsC-Kon94G+mcRb%Kiaf)RR-FE|86>jIwPK1{^pCH zYAz;+z7woTo=aOV;b|Dym%sd}f4V!*RUi85SlP5UX8kG63QP`L`K!RGiQX zh)A!PzVlFCg%Ve~gh7{CZd!syDKDUQ%5BoNq~ZK{`nH2rN@#X`4)2s)LWrs@?lH7c zZ%-ORS@OJb$@KD4X41c?*oR9Q3MoW6VE12eZ=Pcw#e-P6E&6>jS_YhofBl7D4%X(u zGAra8mSpTfc0`uIl@^}=ENP&vNcl1Vb*Kb&`&vOS^bHy=cZJ-P^#npzlmqo4&_1&TCQ1~%(5ow6(FSO%Rqf71OIDVqvi zO2&LH2i6j!dGU4}wy7<#iNq>Ry@9{OGC-%6;6qplHtP@a_QItSgt*5SsGwHiP!tab@2rU27z9UaN3ih{d5*Q@j zKh)LLIoR7hc&K~%3;R1Z6#oi@t}znQIdkjJ{=MI?UmwwpyU&=LUA?`%%kS;)*tq;> ze^}r0Q{VhnFdPa0=c?LY4ljT1Le1`9NNo&!Eqw6PA0d#OyJ~-a-3PDQxeRatoyR-i zu(1KMQ+F^m+1cW^-r41KZ7hGkS^j?0eINce=g^INrRS=*dH>3O4f!h62|HZFwdpEf5h&v^q`0WanYh=eeE8fV;`NQvh&K*+B5DFr& z-1#5sHs;Tn0Xn4Fl3Y=bb)x`PfLge#e*MlT-PBtaS!@Qj@^G zu2T>dvk-P(owIDYsm%CJJ8V!q{aB5<>bnM)e|7V3HW$A;*zQG&pRV2O)#gvY3IaFF zouunp8R-m546cKnw^q%c|8=HRqBFHd6-FwcF7(xyed*N7q?dM0tG=C)2wW@pF*}XW zZVKZlJ0O-|r%h+3_-!E;a+}n!`Tz6lWIq%w)@zohHeXpkt-QnoAk?7Z1uj3~)Nqc) zO>e2_QN#2sT09Hs10%A9l3OW0n<&z+e*{&d2g)UBYaLf-l0n#azKGBiATy z)lP8MU1@h@YJQ1xyvAAX%ZN-R42Po_%a!_l3}a12kgXWsF{soM zu1K*?DQ7#5$tA`ITyb2t9K23UW5ePaBI|)+u0Ex9RkU*Gzz5%)dMo(z|A|GsB0BQ0 z(#*-s>>98=C&LO!J6AGZU{^-E^w?BgFmclAnPFCE&>>`3Sjbp|c@ZRfV1mEYQCSL< zzpeUoGEHZm@a_7OilvYemf#7oMmlkOspLG*b^n@1e_5l^GO0kc%UI6NPlC`Z!#uk* zmWB4n=h@0jj+&hPG4oxVnWzBaa^Pp4ey*v!5LRew@n-K;uO-?))ZNuNaHy}l`1O&` z2RDp8iAZO16@sjfw-p}lYg{Vq+CKL28-s=IIy1wu)v}frgg=4McR2NQ2fB#)8Cbwx z$5CTBy)?ML__b3PyePH|ZYQ`|&Uv#UXF69D?cbO$WfSY)Rfw@-xkB-;!6a7`bcX}@ zlQSX-Ja+z4n^CoLM>*=exg;8BJalKSIn6Q7Na}pX8_(Wb{_d;4vkvPoXrvC4Z1&UR z?DG)k8L`BTAT7>uiInKV@B>dMKF>DIy^%|;Iec-K#FdtHT+&T|ZAn|d%`3YDid-_$ zG>Hk01AOD`{QQhB1ChwduFJYA%9RdRU`Zb7kli5d8%p(dv{3!(6H8ZzLsB{?s(R@1 zxDF@mHX?>BTasqvTl9-4GSprkQB?iNdl{|JWxgufE^7mf4eEym8 z=$}gwWc=y*oU~$;fCab{8i#fJzJs7uPiqvDaYs?lFtGGr7 zC!LX*P6k-0$`Z8ndX;Ym8H2bgdb=oIiN&!YiX7|6pJXAa+mP3YzO!x2zBQ%Sb9P|y({%pO!gCN!la3teU8a7TdzwjtH%es zdaT$saWW`nA}!;ek_pqwm|MFsZH8MRIkp)h`KTnLC%G#D3jr)}HlxEQ;zBp3PXMYS z8++7THZSKMDQu@Rn581bSv5JU`wQxh<2r))=^S~X$DARU9o5KA{Y0>Ug8r=7B%wDn z$*LiOE!TEh&O5s=?m29Em8c+-sBUbRDePuD367d=&BAcvK^z`JxA_6f>txsq)2$8T@6h0K5 z&~39*1PR>9d3vtn3dW{}LX@{gVKJ-?DX<9VFVaJTicOE_9qN7v2K9hJ(ka*a9yoz< zf61EnNi*LI=72TFFb8zRCM7OCQ!?i;aiIKxF6P%Do4ugUL5AaS-K-Pgtox*FBqa!? zXIbV?0%|YFB-#vREp?&1tRL@mzO*y+f5*R1$@N$Mcu7LvH+S<1dt5#DUR6ErHblGC=yQZ;KMST6{MgCV*q+ifiiF4#{llGp0*EfJ|6M{6J%Als8b z-)EGG>Gfwy9Uwb#AJw-~|4!jJglRAuH}m$R!)}mDwm;U037=V=8uc zP7gCIdEtW_H#eizbhi)0QkaxfPioTN_UwG~Pe4N-5SA*dD9|dq zSxHlEKb5JrzoGVlIVHmBj$;mO+{#!1D=F)Kdsc#(>0HOEbD5#&2Zp(7YwH8uN;&dn zI{yD_ll|cAEFsh#@J=5u!*BWWpI_}?K7#+c{g1ii=vl)n$Ux^Hhj?F<{g{DpPsNeF zy6z|5!z3n%VQ^PfP4Wun1FeOJ=VX&mWhQ1bvhOK`WRmxG;VpaUw_l4!Tsnm+sAE%KGjm#*J%F` z{ilnI0yh+SAdY&$UV?FA>Jd0-Ru@X`^AwoT94%tcMJ!EATBuByykf7M)uAKO4pvRZj(d6IZggTPJpzys|MsT zf!m^tFvBFX>eY?Hd08wk6?%wL%S$&@i~cep)2KW5>-74T^{AS_&5ErUqxqUxjF8ST zuR2zf*J}lxt}Rr#iYakN{du`Cn6NqAX>+)zFkp~8Z18A~Sp-!xCJTnJq<%Oe$m67w zc$+fSyno(Pz|B{w?InvdZe~E2yx;&~cV)4O`6#xQ<1z{#^8#2A$zfi;B{GZob{K$H>iTW7jsYQ+1Hv$t;k%wun z7v(Qr-1Sd2KjhRS|1}fb+>7v!%MrELQJ!M;6=UBvQ)Z)W;q z2`?TC3F~9EwM6D+P_^sV$CHZitbot+6d>*>olpp9qWID}Eodx>ns_MUF*?8kU;rZ! zjKv%I7Hx`|qsv8MV*#{c0zal7bDa6Qa60dnY?t2J_q0viE_UgVFk)8--8Yh! z3+$!7uB-Gm3G&tmWN}*pR=fSYW_U1g$4KdMd)Re@u=c&qIW8f|!PM&tGZHaOy-tHE z!_*_B&dWCSfDs`*p3>uCBSgxF-SL16**vPa&=$NIeC~5qU-be+@Rj-Bu7Ygg?kO_x zLsc`NYVuz28(%Iwd_{}oZYW<0yE^W|N^2FhDXz!=8bt+pgU6j*{{^el^@Gj{uwr>tX9r`%y#Wkxvq=0z&G3UZE)1z zIk8@6lj63E9uFc^*!Z01_NYywNrg?#)#kf3zGbh`-sctrFG3gB#hREahjJ|-2a(60 zfN=uEGuBFvx|7#D-VfW0kVf;Se&+S*O9Bw!<8xh6-jaO%OcxE*WVbF7&F)2h121Q&NbZ z99$IGCk)f{af8D&CHMM7QC5R}hG$0Oo^d#)9KE zc60jCAhdHY=M3Yz^nI(jF~HdwRn*o_#0mVBdPyY1v!2o!{6Lh zes&(`XGm7>SItg$x6OiW3kByR!y?-kZaGXClH>8h?t;S+=gW7dbA)Eb+bg{8K zh4+t#m>lN?J6fL2`5f3#u9tvC_=(NpCqCBVfXRYyrYP?6q9x9?lq0Q#E zof>kTDtyN#+3I0>A#3J%J625X#E(i|2-2ov$K@-42zP++e)9oA@<73zY4*4SX3l71 zONVWho#w~5@RY%5*w+2JL-s&uGV0mz?3~%ZHrlTR+@>~t2^U5Uylxfc%{aYa!P{K} z)q_^eE^F;dgFSRw3FnW(l{1P~*lb_z7`mk7{Uesq_3fl)&fxcMA{6Z6V4XYXA+llT+&?w;~=y*uCq`&q&UJkO>^Af6CJUB$%Hq+%`clouT2 zC^{^F9xKnr6+?mrz1*f{|3H(R-{}Pp(aj#crfX~sX_B@0deK58$9cC7MN!%p`I*z9 zXu<6bH$*r-GAH78PXWdsj*uEKR|Nxt1jlNt*M1$DbBCbQHWlOb^+pC=E(iA>`?7h! zu>akVm9+G+CC$jr!Z5zm10h)=YgcW=r%WQrKAuP>4ECFB!na#Fx3J>&zTT+)#>U3o z_Q_(@F=sC^05_Kh?7f>hcYV2IZ?@QPJpoGs4fRdK=Ur%}9eynup3#B(7B{buw)dC4 zK=C5z-IOoL>CA3J`!uO}o1+C%Pn9?G+uSQyJEEEdjOl|)8ge8ptGqK5LgzgX)joel zYt8QfNWuikPsX7O{ERT=OsPeU8{Vm2ZC9hk|M;Dkyi|kSNf!v}$y)1Ba$T|ZcV5CN zj$Pt*hP3VLhLUr*U}%~&8+`Mo4Pw!$X%%d>eU_ToHHP)#fT4^I(uHlisNzOQmmnhv zr;WY{Tk6O8dAU6FHw~jeInlIjL0W$x=h4}t2g$aepH4%e=M071Bszo{#8nbG?>h>6 z!KT{9dU162C6##XZCkn{3TGP_Z0N~FpT4NsD_o3&HHHj3t>iv;ZhP9MY@K~@gksd* z>{K=R!d3g=GFkMaf^)*;@F=TeWITTVExWORk?|k6AiU(b$K8eV`MX6qhSKoZl{}>@NZ78}G+A3)2;SS)_)^dAO$ z*RTF~)Bm{q_4~t3Q0og`ym)W_1ug^rhlS#o3)j7t9qHGReXcHx(9J5Awp6ZjdB;~f z*GYYgsI*gXils=0<*e%k^32wABS%lSEuYF3g4b)f=iV`*~je>`(mI#(n1y$Ykct!s_ucs~ocF zk@J_2o?iZwFW%l7ZasaT!G7=eMmH@V{;i*lJvGAc%H5SD_+&{3wDs(T(;Xv6Pqv|W zKEHr?xH$V)ek8cHqcpY?vWJ3)U(w@Z$BsUq^84DVhqmSXk8Rx4*NUp~WEumxOk0KC z)XJDl0n+r|G(E?Tj-0vN_Lp}Y2sG`_%%Nc@Am!Di3+~AhO^2LAlwWi`2dJj#@=l|K) z)_I+&qe`p~OaC;p{L@=s*f5G<4yAkS?c`(u^n-aW>%>rmjm9TZN+!me?J&n&fNV{<8tipjK&jaGNje6 zDe)|SsV?2TeEr0g_-ocRXCMGJcg#pPfaO|VjTnGB?eVofRpgV}o3znzvMCKr>`rM6 z#pGh4^Mco$N006fYSgBhC#4F!zD%QBhoU>8E4MPPEeTMHvnF1<~0+18yF@STrbERc1bWCrhB#%zQIXv)EPQeqbg0a>t*3V#A=A z(hIOpaWF~^YE(nPh;2stj5GT0=;*h#mptf)T>bR3>Mib|m6 z7H6g7tX44cl;WK=MtPeEUnQjU?t^vaWz#x)+x)qMOt)n@pnuCoe3dYB+A(tTP--RB zdIGNqM;Rq%7HBhSIz)1E5G1L&1Bf*W(Wc=emW|Iyd^aVy1Ld(>(jzk66u-wz6WWK9 ztRnsu0=Awwe*RjUP=jVZ{~LSO<)!TBn+)R+Ija-Jjcu<#>_rhJ-FIi(NXm&&9u>KUUHEU*Z16{&h zK5FFDGM1L5{95hleW`W>d$I81cY{q)dN_lw-9m2p$S<{S?k}OWXmgp0tgJW`(oZ_; zQixdj`|{U+v3=hQf`(~F`T#3c#aJEkjDWptPf%9CYP5G)9w6=j$?n0_Wz26%20hDN zOAj^%Q)h}__@hQ|;Blf>ys&X0xZWA=cK394_4RcPn0im`s!oY0#=A_1C(=|EY5Lso zrhM_rZ@j~w0OA2cwbgw$)Wx5|qo;M(+CyYq&W?|s)+si?QBNN@-z|w}YN?L}1B3si zDeyC`IzjH1)24k~B=n|>^nNdRkc`75iS&EWr51wTp{{n;x$S}A!2v%V z4F(UDTHF?JY4X2}2Pch6cje$saSZYyoliq4U2mH9?yqhN5IC3n5t79`V9d zy)Lr;KuzOD9fVJ8tZm-7Lmv`}Xh*aq+O%P#-LzW^7Ah`OZ|sxW%fT8`f5(ua@Cbix zx@0IIs**2w9#ok@h%f%U9jB}8)Eo}R&B;%CHk%m*Oh@^Ct2%tdV zJ?Ue6jQF>+cqyJ=$#F9p#?z4k5i9>|F%N$hE}gCkqc~amGFlVOn_QS3h(0RwSWSqk z{M_U5&`PBlf`Z{*+hv=m31eS#+kcv@^|0i0U#3FAd4k0r6#{e-L{w{t*;3t4;VF`4 zG;w=F5uAo_79ujFO(ksMG}P7vQV-L|H#ZsnQFPut4SKzf~R1Lzzm&XKF$#W16iT`y5f_WR&5? zkqw72hS034%8y0xkM~GC!2V6!BA!JAAJphQIV7|!13{eR2?|2`r$SMSU5SDbqs(={pnmRuHYlzwbh6{_o-Gb{0##6)al{ zhRvG;_^rY3Rc6AWiuUXZ#wI5*9<8YQ&0x*+EK#*{1ekE$|EL$`6vFXwvh?O-!5T%N zUFpwT!2p3$j{)hXWP=yN(vlfg14QV>gsO~!Z+proTJnmP_?&*KbsKFin7m=PxPbCM zh-Fjd`19u4&X$UXP!$f|1-6=?SG*8Wm3@4A6|mw@&*3d>r5rJG2dTXe87_J6$WL5Y zse?*&Dzc?HXMFUWYK=x}HPzUL{Yd7g-+3o*r2pZ$s;cNnxT~kD3vw^fL)z$}v3~c6 zNASp!`;9j0JG?{ao>JSqU^i6qIz5QTaX6|9Nbil|rW2B?ayRhvsVc~gFIuRpRraiS zRC#-Q(8#*pE}b<}eVy&+@P)?BjsmM-Z@K0|72I&u%-iumaNu>nzMX-H+$Bx3`t|8T zuy$;bb3AYZE16|$^i;6g0?(w0-KrP)LMV!W(0%L+hRsbHkHIieqNiu@KXzNI!pioF z0;PexJ@t5@Mf{iZL}OjSI2L2san3quy7)Odg4GMMUK0je5kw}V9ISDrYR^5@UKsj^ zOD6yOq3X&84nlTilwA6HvbOT;i6DLuv!l$t+P_WUuDOi=aLEhfb|=kxw^pAHhOkfb z+bpyOtK|$PJ<8&zWIk{z5FYCv90g-7_l{r`%79hr{4`N=RX34uF_@V0ht7+n7rDJO zO6*EscF+(3?-QRjb@nUJagl%n;nY_-L?3F5DKek#H|+g7GCZBF&{<>0N&~ z!fk!B^w<^%kI$zk7NGwc_G_^~7?U#5NHuXBN3CoQ?x8&xpL6jjXXr-7(V)lK+O>&fBQl}z6r#h|x3FmAwfo~8HS1$r zYwEoiyN!jADxp{_0D=Qkn$>t9DxILo6~GTi6q#GyKf%6)-s3`PDU1Ze(wXxycl~*V z`1q> zc{E>3eT{e#l;SL!y)6YMivv7027|#krU%@1u>dH;3b`p;5dV<_@N9}zhdoTv+|$-b z9WxKnCN8b@y2*=hb)UtbxLao%g4HtT$=k_C&3&xe^KcmHe}0~ckXf!P{1Gq2C%0k) z&xJx*5c}|byE<5c!&@cza+EBfY7z@ZWPn;CeVb7zkb@g8u=ovjo!IQ7wGm>mz%G z7oU2@i^}00s89k(HS`yMR745( z#j>7vd)i0h1J%Kp97DqBa`>lV)I(a9{QP>ZVeZC=kma}1jE`Eh(Mwo%CR|z(XG6hi z@K5vMV|juT(A*@(C4Nr|{lV&`$=P(KG^BF@qA`q)PWwoOibbiFwve|nHG6|$Y)wi- z+Y<5OI=LD}F4aV6W{7$^k1HR!^LO|V^gKLY_zy>e)u15Tm%pfTUiCel-)y@AE<=Ip z9FZZIZwm1IYB1u=sO^z8Q&Tc=;zckN3@P-R%X%#6%`F-^M~3hW?clV*A-mwWDaheI zZOdJcDaiY%c?r=1;LQuQa`I0WSJ~x2XdzpsiwA-+=4S>MW@V_}3J^%%jIj;QskB8m$@LBK+NQe1I)zcMud5?6J1%=08!gX z!M-`jVesJ)GutN#q5T}yxw5bPW9M7$nY=SCl1o93e^%tQ$+({(_bHQLDm4)FxI~v! zxWq$v$etBIw*?vK5vjBISh{Q5MXu630q$?4e!dRwSltiT8pBOCnrfM7xGqt}KO<5ba@J z($`Mcr(q%KCevbb8gJX_1mZtkgbMYrRj6EdvybWw?cNgIgZf6ukPGW7KTsd^x;U9z zKH_HRBPC`zQd3y-aa8=8XEm9x*-_j8e^fwzC8+Fb;I!#KDm7qm6FLk8Jorm)@;+iY z_4aw2P~EfVZN>$oV*v@hAL`n9y!?5BGdnMp^9rmHI-`Ca-+IMc zw_Rxy9*0cJDpWANf>5pL>x8bmTzM_ZI@1*i?+-?edjTWP_tJm3hG-gGxX1KNeZ-@P zkE1jU$I&jpHpmN{U@_cf-}1JEUex6DnHs{Orv&_GJbv7o66|a2MrWn6rq^Jx z!%rxu6L>m32GbF_LxFtYylO1$Qx2z(#nlDk1>c)p)K<BEa! z!0cMwF*)--G@AM$yG)H@zplCaJL>G8Et{ka zuz%-X3s1fOWSwdB_KVeZrfyqvk2+wgI{Ry5wwU*q-<)X(Z&4k!b**@eCt|FR>x+=mSw9~gSTX?H95E$=H){X z=XjSvsty#K$g8O*ZVOywg9%Ujf(hUCvRLx$iZ_$r(jZt*k7Hq z^xIKW!7v3}dovmxRM}*rVO`wg$|H}R{=i~7&SQ_^1AVVqYZ zcxsyW3R6ty_pzV+%5%3NqRs2dOP3<9yVG+y{ERBA*z$NJ%WjKgiLn88q*$Ew;hPbsUchM) z5|F|%Fa}tXYAB`Hh_XYL1VfTQ{3&PW5nLgIz%Z372eicmeK7F#UH*W?%y*H!&CLCH zzTA>R=q=8f(7_y>P?^i<+kN;QQsl=~rmtr6ywc&$?!Qni*rcRqZsFY*p_^=eR+?%( zarT_qF=ocijIq=%_9pOH#j&6WcGBf0`#UWLGBz`eaaCQNE17Ty<+tc;`dU$Oi>NuO}g9Lv1)V(z=n^l0ulBieWienF1D-LW35rNJk&f$hRugU zO~O%cLChuXWlh?qM@1Wazy2F?!cW=o@uvQ6P;3XqrAbfCMexKMzR^d^%Oey_7bPvkXY}E>_=!L9rg=tuAVH3A1 zm$36x&#HQRK%Mbv;=sI#WOy3v&&0)W^pccEY;Ir!r79QacNp)O0AEZ#P9AFaW7ZEe8Gw% zL@L+anU!^F#n*xrGbf)C3f(ReFJk#&uwu%3`VaIBlm?*AF8}Go?{28mAYiAf$ipBdOK|a4Be)D$%{Uyy zg=Y!i3DFL%{Jw;zm#O+b1Xz2=V>s7)jhVwD(3GA zS6!p&=T$XT)ztIj{(J_e_zmYB_9wn+89*L@X@YI(*%InCk+tOUO}Do!5k7?kOh5+4Rd7W4pN ze5c#d6;m>WBcWU7pe@zf)753NOI&sM`HH&-E5YfmJF~!tdYLdh;6fahvo$R#sqWG<)2@w%aV;l9YlBTU|$|Cy5cD(0iyNxmrq7z-aL^gc{_ibX};@hHF}f9dey7&8G>N zMihk(A%(R*A8JF-k-)t()966qI9@DYQaE#jR1KZX4`cmZ9=eV{RI!L2=gP3V=;<)r zs9C~?&oO(j`%s*kW%|nlpXYXioP@Plt_t6=Y$$lRom!foTEf!}qhv|np5h`Qk*iqB zOm9AQoIcUlX?W$5LuX>RNvZ5 zMg5$YAz1KN;Y?fZl}8ZFpDXybhGB5iZk;$VLU9%Kw(0Rnw}b{MK>-Yybrhx4SQejWcwa+; zL&01QN4;!Mr3T1;BAu7mC^dr5Ro~w+q6P}V2*vm8a0Vp{VoylGK3zhYGcR749_qzfSKkF+#G~5swrWM1xRN=Uddeu3$=ivM zWpd4SDY0{82eX_A(N!pwPqslRuu2Wyp^r~8M^?++Q|z+*hYqby3lP|OlLw{pl2{_7 zRE1rGsl5ca1H;(@{qLpEtBbQ~nmASJp|lE(_rFgN=AtB}rqc-Bos3=FlQCe?K@eS$ z$Wpbfc~|@ba-%FOLkbiq9_y}zhe>HhsAD3+F2`7f7{5K`WGfXJy9e6-U+&&KPOj^^ z??lzBrEBSZ#o7fBO9SX`boCB^B-mI8fY=ujBt#0VMi;u9=eE6YS#KK^9U#F> zoXmh=q3XT+?z_vm=bn4c@0^pmsx7Q++Da|vd=ph~YT69hsU=?0N1zIET*9pjS}MAS zOZy{7z%6G*PhIk@g((tHJM%eUY8Lk#-Ovte_V%0sr6+w1MXIM#&zZ6jobch3cifhD zSyp2#e<^(-?A&VJ8S@Ug-wv*#3Vp+7s^>VizijT%HH_oz^iJYnysK5Z*Qn0Z(4>ih z?q8_G8LjBKyPp29WPVTe7zlz%9YFK4j=CfV{39}%+4D7) zUY{XetlEC7)rkFGre5Xl@NICtNHt~PM=CG68*yb2zRb#s7{fk0nX`G}oo>}!^=*&k zX*z*c&bIP14k=*RfRr7IeAoal$~at#)r9m@UK=bmhZjlZFUaVwT?}GCq>>bI!MMBM5uL#dKBub`Usd)@>TPA+7NnnD8B`}=!au$5Kz#Dnq zE8Ou~5)|bpW#4Y}aZs;+aKAzHD}8dZ0S}-d>R01bJLQK2u|m zCIqA*4meg;5{)tUaD@sIU~PjgXk=FCfP|Ow-hEciFQFU{GEzWV*^O==J4yt7s#u}bGQG=dRBy!veWYa~>>Dz59lZhPV z!?K)USNXZ-fWs--+0oaHbpAN29jv1U$bE%JR)7tnL_|VrH?gzj<8{n)LqSm46f8 z5T&tJn~q}IbmC-RjLYc?;Zi3ulwsBA&1?`C3H~FsI(r_PJT7Ppc4vJ>c$6yn zc8(1X;nbG7uUqqVEfhg@_2eQws`_AAEvBeaXz1XAiu|jFtf{Z^MpPd?S9`DS?=wXw zdXo*WwxW63W{Pfj3T|y{Ym@84{c0zM28M7^F?}!byv)L2+Ru;l@ER#&RDoP~*d*UD zNwLzJp@HEiKbr4BRl4EX%5x}JDgn-((owWzPK|1PtclC?l=A3Y%2lG9^`itzf4#Q6 zM!j~>(UzU;Bk-4CwhH5_h_qEbm8KX?+4&DH0TrC=GZ7f=xvBJsQddh2m3~Vbetuoi zr<8;m)|6DZyeHQQNu2NF6slL3OXb&E5!4T~UnkcW+gM6710O;DudQxlIi`oL+4{RC z?AVBFW?l-w8jZFZzziV;xyWASc5W=igeZ!Z0>o+do-iX)HJ6KUa(Ce@*OfE+9~_{S zJ$?K8@XS#PhIOP+nUz5WS?xKvzYn42!;0F9pLz$x&C(r8x}=gT&9wB0QhCC;-b zagoOBg*}Bwivp5{n$Nlb3;WEtpR!LwuROeBxRDvV@+P6y2t?r`7y$j_$x~Ap_FuB7 z6^nd(^95Z@$oHYZRd8Y!B_M4PFf8)O=1}RUiED6b(Bc{p!h(nhixl5tQ3_m)3t|@# z$;1K{oY|$St|~&oSm{6T;N|^oa3|0U3JZ216e#^I9_>4}nNmBtKEgHpBM8K@nQvqE zyyCPRchNr7`hs~bSS+%m$GLT57az}+K1Y0s_P}sy@H?-12Vc;&gvIRG&bKXne7tQV zHL;s2!USL7742MoU@$WCrnBF>g`Rls_0p%Q=2XO*-d*}Ne!LKt2i{Ai*gqkHM3ToJ zy`jbo(}9CrdNp!RKbuNFz>iZqPgB;gWNrdmcJh0#1*%9G94J)!Hs#*PgU-_^j<@k} z${Xb?O&L-Aw1TcrSP+;UJMmH*@RDAGXI-)wKv986+T?q6Lm_^y+QY;&pEA&BH?W_? zg-CSAvo9z*RVcYVL`XDYLy2gSB>oBUB8ZL_3)dwY!gXBJt;WV!V0R$Ul{pnoh7WIx zhwH=JyY|#8Dn>q)?Q1#Qb}G<@D^esmv-jD^ko*C6)E#m3$-V9ZQj+COpJ#UyIR7>S`*=Tq`6h)qC4sfr^1;)2T=Lm_~xU}-N9dnstexB ztp_|vlL1Q=&ZuKMW08m30(m;yI$9Xs-W}-THP40;^{LLSTdoG;QIJQyfo1+7=wCQW zd<+HB;FEZ5>X&{;>!S9*ZbXxH^+X5c0#_4tkwjpWXNe7$Ofo8oMtw;pBk>4h*wRe6 z5!D>Z$3oGN7v)3$)rG>LNSJ@>LXl8}ztK>Ah{$o_2+{T!)_8rq(F^f69*u=#$*3aM z5#G)Vg+)hismA(5n5c8K$3@xW&3wfPlMe8Y`=h8H$z%g@>XP}!I3bg)DPgsQcT%}~ zKVR!Y39d#$G5)LL|1SQE*GIUj|6=w@5IpYbZk*ph^LZj!Pn+Ych6PnkVv}_bo%#t)(3>O>XQE&7Uo6&0fIyou#oCJzEu|swc6lhQ=aDFV zi6!z1B*_1Di5T^0>1di_5d~$5)Wsr^Sd`Hrw&ExCbbVbo%rH`;{k5+QDldx18tjYx z(8&0I>Y}=wfU^`rHX`Z}v#ee<@_$}mnr!~+LY>V_KEE~Lj6yxrrux(mLKueYh-zr_ znY0@X3F02oX-!->($D~_Z1A|tTA^+Go{zLe(prHh-nbsg zcLyH8Mw%G=B=M8#h%u^|h}JXWOuDyQd`HGOsq4H>0VwNu8!f~=gvV_eunrX7k=T*` zzb@coIf`SQ*Fmuayj-y!%Ml*)?n~Y7w9tv0j~AX7J8sdB)`w^n__w8S?Yx*nbN%5x zdm;AlUNNXtU19t4y^Wo%QHz>-sU;M6p5BGKH#ap!lKj8j3o|Aj!1lKAAu?md>*d=0 z#m#|FH}i(e7Gy5{MxO7Z+qEH_lBDs_g%P`Kg2+jIKCHLzuL57Bj7G4~JP_|_ysM@a z-h6wX2`Db2?1e&y7+m4)P7QD2-DI>sH-1dkP5%H}1k+yL7-l!*=78 zeb3qFNxS0i_Nn^A1^2`1JNA|pYSib$k6Kap*xk|}WuMubFNEpgZS7z0c(!}8a){w1 z8D*;#k94SU2a{@Xl-QdlD{a-aBk$_kc4o^2s}6N-jPFDSQ>e&oCO_%hj*}`L*w0tD z^Iz112f~fvJ$de&i#@0N>;&x43Q=|C8U5a)nZ`$xP-XVIj%)nBXB+V?-5+h^_nf&@ z#|_HhE7+7DE1vaOed>Ez(@cc6*-TBiF@8*oNJNu6+_a z;{7T)8s{tHMh~vDQAV1ZdS9*AGi_~Ddgx8_&7HO$UFB+YKo5<_^|{&lbz7kBgU!0o zX0yM?TCiK>GSbzdAX5a_g*|pO5=}~bYDc`gg-adD4x&~eQnc-C?AY40vpo@SO0+k% zH#Q~O+SxHW*+rW>w!tQwsG)s(YDf1TI6uLt>WM-e$3x}ECJS?0w|BSgPR84}v^RBh z<6qLWb=zjb4yW6;raFX(@isl)l-Lvc=%(VgE>FDoxyucMKa4PcvL#p8-2K{*kTSVl z%EeqYFb@v6`1fG-d{W}%R-7UpVkL_K^Zld`w(P;_V}}M)JtG5q_H&RoD3xsE z7JntDbeJES)Am10a{0~c`}Kr`wLpxA2gb*WJAWbH*|LsM%2{jE?-7FSM9X}kv-`$R zVuWrLHP6>jv(!l#uAW59E!WoGTu;ku?|vvLuPgq0qvX|8gQcpfP;&8K{@La&d8M&h z_nschu8c=s>b%Ui7VK=-{VZ^mJ`z6PBU9miWuI1oYFr(gX<@KklEr%hlmO2HS0sdG zf9kp-s;!|~BicM_ncLXAW|jFmeRvI>u5A{PQ$4m%NOvZU( zBCKWkg%qO%7ID>; zJ9`&vE;h<5E3>!nYRUvu69~pqpua-q-9Fe6nl6DLXg9bwLdvOO5RbJhMT9Jjpv*;? zi1gMnek$WfB~u(O<|lg-cpA1x44pE9ve(Ssb8Z13ZS1{@$0qMCUP_{J>tK#i$?zD7 zMcgYYL}O^j<<+CczDnOd_@9CuM~Q^yl59H6=01X!DfXbFX~75XffxY`=vOs^P0JP; zohcR?zS4FueRwpj#jX`Y`EUHZd*Gsx8MFyr>@FA~(h}b;9s3Vo3~bHMU`3)d9V!!{ zKTrTJ@V5p6m<3a&6r49uL9--hGc=3nfb!pwr%Ejy69dX(AZik7$(s}?gmT1z;{l|= zV3qmH9T4mDHUJEI*|m;EJ%P2S z`^VFx>9Nwce(93e(V~3C8<}*+z>mCw>u1Z|LVNei@4Y)#Xclk3TjlLS5avj)Et4G3 zq{-D{>d3F8opaIUHTTwW_O&-ZjIpmPT^{!*ODO9K3sENULXN~R0L|P4mHy&S9}Bd; zy2Pj{ULa)S15kR(Ph;>VE*qdz%-X)C*EmLny!-@;YqtoWXp7(dv(24>rP2$~=9b@I z+Pp~aTQTf%Kkg8*K{#V;XO(N0y96K(zD6)WRtIL>3Q5a>N?{0V$=~Phjx##$2NQzT zD0MC&3_&%rWG&{QHnIEu9+uy@iG6_Nl^(6M0bX3~g*s6dyj}u_qIZFO8tt`MdWW96 z)xDjquWoh>O!1c*u64GlbJH^{doZEP_bu&mw%Ff)pz|~)^=p3gxhIhqHh29k7kTP1 zmAEKHt`C7MW=IEfWHSJRHFjw;4XtSonvmokLH-(Ns?7&P^RkNg(%ASrz`}= zo!tF7my34`YO!dNle0M)@HiJ@?C zLHx_y1(*a|kk}y~Qess({`G|Z_yogb5p)(<1O{A4f=$+>RVJ=1ANs?zFLigpA>fb_ z;qn(u0++Bw!%CO`Mu*px#zjOjoa9Ud?DBvC)?+TnFQ0wD;*etqZ6$^&*ooq;&V5^6 ze-WPrIfGOR&V#NJe_C2znOfB}%m5e1j!fI&5q69r?(~A>e@20VcveWz%*qP^e4!kD z^|Hlfe|z8c;i6~p%m4ndvp=`j()UJoo*wHb66xT0>2s^EdYuh5OS{a=)9>9XJUZwO z+n@I~9=5@Tkw+7m{t4{6Wn%5k^&EWd-4A8r>xzFcAAjeUtY`n=Cx|Gy^y`YrawKyhO*tUBoVQq4L+u*!v&faz3)!E*7k zgi~E{;=>lsTiZD+&Sbr^7)Uf_Tketqo&1MWvW`SV?gbZ&sA(sKR1eEdr!p-nU-T}Q zK=L-(+Riq122Q;V{+7cho;sDYqMy#(vXif)>*CkLEgc6hErJLGX$2F}nmvJ1g&N>4 zm*7Q2?nZ|S?0Xpw(_3ur9PcRp^6AHk;%B#=O9=B#)6~56%@#qfdz%oM5+QYJwo{>< zFnG^#7>`aCHT|;Yo6xx=$ZmN~{G)^hR$_JO$mV|(jOVKg6v9~p2$$#5GN;cqo9_3t z+YXM7)+!p;cL1FPDv63V!*6fiFuy&R{4Ik#hXKw*-=E@BV5Jqv0_SmRb4{*NBtl(f z7aoI}L=udD-X?%&7~iFp$ud3iv_#5l5-30$0CnaVI}_wV9ppkK>byfAQLf~Z%Z#=aETqCfVtj<%V=C~lL z1}N+G9RDxO{A#SR_RczXf1>u@hcWxLh0AmCqyy6TdS-5BrXjoXcFdamuXt##?oJQ@ zDd4^ZqqT-EjoeLq4~LQrEmv6;>I; z2WnRT%PLb@XZ{vhJq|x7GTLyS`u#gHi{#sD$$H}w96a1VIyO8;D1@%Bcdl6;<>hzi zJpybEy4CiRC!Vz0=5T+1@@lKOvthN>-23p=R$KW0->Xdv>o)4sr>?i!p;))xo-Dh3 zA8YPnYG`DQ$q(=O>LmB3(nC)>9m{fe0?N!9OLss z%Ayh6o1M;b#_w^ZGbv+SQiU(t2FT&c&l|#C%`@ro@xw>iMdk31j(iH=NzP?H9++AIHa{X`RR#s=9T=n6h(SDTw9OW&QQMqNOz}?@IFp4i04)TPQTAW?U zyZu?syFWXJn2Nl>i5X!6uYPOj;emmp^3;R?GbjOYsjRAr5a;~v93~VGF6+1r=q9anw18*Ib362VtW1t%)hYW$0t_R+4qEQv0h0ir3JVYTk_ z3Wjqp2d=){N1R@*T6RneDS)eEpMPvN>tjXY!E3;+VcBhWyJf_*Gq%#9JVk|D{K`LT8!kG|Ub80Gadr|U(Yv96(Xrw` z{Pn-o*#vo3*Ke7#fBs%P^2?FWUi5zZmxu$qWmEm1i2gue%U7FIq^M1QhN!wbT0T+; zcc1!+>{uZno#;oZ{$2#G&aU<$vf%wA*TdXGG2NaRXtC?JxPGg0{e}4Dt_8a;5l4}T ztbBG!?pjw?oYaG^VG^?`CcE-&^XB@1+dWq$rj-Qj}2uhI*Tx4!T(teIXURjQh4jEBDLAk2Lcw&I8ogmGF71Y zU8#tv%&O1mSTwsZGm9oAFMXhdbS$c(8?r6s?#YuyOYVMd@h)dCh6N(Ij+QX%x5C%r zurwD*^n#=?oePs?o zCe-rVsCwq_=@GvX&O)tYNBKtSa$m}8&!bo3+(nZ(7OVP2h*?>^@Zdz^HeC^Iah)

ZwM}OcCtFve1 zeEeW_eTUz`7mAzeGM;twsInFM15F(IRx`q5Qo4^Xzxj@5QoERDx%}-)aV)$uw_@+_ zxn?iISL&&+!IR2=i&ToMbJ9)_=_}P^`U|IYWH@E<$KCK=Ib@Ut1LM4kH~ATI&Jh>O z?}ohjRG1!Fgt1jZju3kfHr;dP75aj<;;zPXX%#0gh~;*5c{A9&iD-zXeLR;{1jUOG zG}dQAyY!~cvuE|;#g;mU6X?RyUA(7HXI9x{$!kZk{?s}8Pb8XrZe}5M2JM2>3_hp7 zAanS6 zLUpjs*-9bQ$MVvVl+iBXIm%Oha)KXjTJ)76w8g*(6|el6$K$2Xc3=162jQn{_-1xV z=DfZETx&+I<1IHbc4Po`=xBP>w{8(cXgv>J6AdHynZCl~?T&^2`28{qudBH1Zg{*{ z_{Lw`?^@HezBQ!@vfOpO@FX^V9ZIiZu4Nvn#u>wx8pj{6rQ)GTyz?rIV-EO)+v{p% z4DmshJ1eZRdRUtzRZ$=vb*8fWh26^g@TF=!RRX}*SuVj5tod)fNUWFpp+ z9`Uz({JEtXw`Q?$u@%7$4UmwrWm{&Tjh^MJZujq?($iA%i!#w~E3affF#^hzQ$tn$hG@wQZQ(KqJ{8r-4C3HYTPZ~z z=U!k&wA!{*>nU%>7{DT>zuK(xZiiPZfh1wdt55}F^~6iX~zisFM-N+;Ke0*+}Q-1;4>4R2Cqh$;!M|pma8G1eTrF zg!QLhR^9~2>E|D}K-ATSn*oT;Slgo6fJGy=+Vs+m9d&X?%}CEfx#GsQh$JgdBg&Ua ziLI7ujN54umD!+@`l0MWu)`KrEelOf%`*Jhk3dckV1|E1hlc08zIu;Q=D{cN6sIG3 zj<8#7dNrMs$ao#)vV<~}?&X^y6F>t$(lqk@GSfFUa6{yQ8t=y7r(Y~Q-q!MNVNZAV z2NGk2osx&&tzrbQkV*O?9vd{qlZ5gE2BdIqY(Rab!jTI=du(QvCYuj*h%vV_7Gzk*by?7Me z#jYHz3ufwLHND6LDXAlF<#Udo68!@P4Z$z)oC_6l={9Cwo4JX(X`)at6Z};=N&o9v zCBItEPRii1>cV{d-qoPZc#Cy4z0b(VwhG8n)#*c@PgAivuaj2QA+>;TvWR9cfS*C-Dcs5U|0kw z0zyPc6Cx22#m^8%#VbGYN{6BvjrwA{?IoGiNdLfKYChGI9_=4V-C5r6=zvYoB$zTl zZg6bSRyB|pS0}NM3~kCbDHFA}rj0GrwVIwNs!Vn297C8VtK2-{0)euz!$2=Sd%FW; znlU>&3!12H3ih%@0@)s9E}|Y`KT;Mr-d*zxR5v_@!^2=&XuiP_zyJR61QPj!Wgm!l-*^SAURT345riN-rq^VV00oQw4(u0g+oM6BPS6BEqRR& z)HD+E+AITs=54!D5Z0KHLolqP=h*MoL|GFyLz1l)98AZ@N}I(=sO6ZpU%Z9!BK zknd=bT_Swqk{#I0AXv3esWB61zHhH8kPbnHvX!qQ#>*tZopM)-3%i#)ihtwVUy2pq ztUn&gTa`X0gH1*K*XfRqL99l!D?nj$pi`<8Yhs&@v@i>Hi9Xt~NbF)5e2qnv*DjJ- zPudO?KFW>CY&gQ2%4Y8^F>JWm6NtjjrJN7Am|9+$%p&E?1JqHPzgZXwBg@{qf;0XS zG36!}7La?Uh(sjpC-NWu?)$BslGgkT%Q}Bl8{D5dot0E}7sgo2NtZHn%lCJ~sMtbD zAZd6IqUO1MB`|@m%F9!_WV?E%n)+}HS3%?sIapq94^NDM+b+~rElGO-Rr!$ z_OS|&tlbj5u=woG-z}dlW&Uo~8|Ya3f^xe`KhMps{MwsUHmg%Bvj1FWM)L{7Wspf` z%<@xOEp(3X5`;3XnV!oQUsW|_u(#rH;3PKS07zN{yfSmDtu$1LGGCB|Q-g=tl-FAD z0p2Dio4&z8%OMds*>Lap$XJ=@h~uI`VqaxCz~!LWtz|lHGlqb~k!nsm5}0q(KBPSm zHYUOQ)0tO|6IG56H+XS&`JKhwDx%kl6b?&79*0fPC*tq<^z@Vl)1jf>(OO!AJ+hTM z{z#+C_7rtp4Oq(N8OEtTpJ%c&7#_CF6UD36H{Gwot?(18) z!4icQyX}|hIpMm4*tle%eU5s>8%I@5*UnPd#Fa8~<0i*_!B zN`&$!NMa4O&X&IWv;Q6sen(uz6Mz5C{=Bxu%stL&Y~a+z323OdX1}owvOo12hdDwz zOBN)EE>r3P2#Y8LdNcK&h{4CAOx#lpDx^N)bwi3`L!$&1E~jxMio zoW%ODWTI+iPn$rTGs?Y8Xi;LlDR`q+9-4Muh`?zSt=WPpGV{7Lu?Q-UW(sTQvU@d~1rlvCoU4 zx5RS-Y*OKIH&-4+!l*r!LsP$|l)L4zMON7rQF>5J0&>CK8j3k&Ak|N!xdu&Wj+TU)4L_(YgAs7lqQKE54OxySqX`lbzxE}oBgAS4Tq5AgkPI4a4{a{ehD z?(5-*=t%k7n)vxlIJz>=nC10$^SJF)c13kVfmr4vmUU8NaMEwX0XYWmCi)8zVLrk2 zkfzFg$OX7gPRUK?qdjCE>cinM``H2&YIt$?4`xV$caZOw2I3lZg(}%&Nql<3QQ*Y1 zjUH)Ql96DJvKsccqG1^M5<{j=+zizLx6+XD{8lb7@wUX=?N_2Md+DQ()7FRmIP0Ta zwTM*|7v-FayYU>=gphA>ae*|bhq!Sj6q0&}xz(N1WI^Tl>l$;1?2>ad%)G#RLP7Ot zC#BkVMWWdDz`{|v$ZI*`Dp$LfpgZJYh8CKbtm_;Tad+tBbSED#M9H*d6qYAXs!|&9 zLDpxw${0L)m+BwR1S5;c2^y1jy3ML#=I@i-(t*(fsSrcdku&*vSmuDWj8Quehq=hE1={P3u_m?aRPID9MIQXCJ4-XWDa3zrA4Lf260JA5rft-R&ne%@-hu~QKxdWS!G=$PFaP=uX> zq3&%Bq3wI(qV-qx@itw{2W}Z@ycmpTP|qwbp?AuAMM4Iu=rfMPu%ZUgWj`933m4@`BlWwj$Mo7sB3> zvccQio4qn201;8z6UQQvt_W8&`LlIN)H9@kS2RCPKNa@WSr_%g3_@NMd|fm4kmPk_8F#Db zu?O)j?vHKu!gHBbt!?py8=;U46FyB&YC2yu;bsnjXe5Y5Z4MA!Jx8XD<#3V&| zT?i1;2y*AqC!yJwww{D$5j!C=UUSil$rn^Ys`gh3oGy@wk4A{W-j9m*^vzONp7O%R z-yNO39A>YX^oezhuLPdSE-#3?}S2g9O~T;c`+2ln21LJ6Kt$^7&dKkm4wPUBQdde1wec& zq`}Cai-r+sw8w~dFGPbmHvdsx^}>NDB0saC<*|n(;u80HPZK{ch3m){fRb^FY1QFi zG8DNj4JF03hCinHC#j>1wJ^@VcvM_T0!+7r&Kr{Scka-*9?ctz7^K|-PAK`dnsJZ( zmnaBXH)`VybgVlPk2Z(vOjI=?Ok&qah-Bk;)R4zk)lGdqJY=$*wr|Pe+vy{&xeSW& z+MZZQrctXfA2>qp$tf)WlMOzm7d9pNxNgbn^)nk*Qg>}D+GO?wz4;}wa;uBo!5~Sg zIW5pVo3fAFA;z+v?pGxVjr&&h^u9!sEjRR)m`bFe7VXXj^UBGsejM=XCf`8^xpbE? z)EF#5_PkQ8b$0_F%U*yc>&~*85%!XtdI+$9C}b(V?Y!k_&lX3tCMix}*rGstEH zA_l8Oti1&bR+a4cq69vzX;a7x-nSOnk?NC{SKZ{l3D3*q?=Z;8&lpwgHg0g#BZ+zS zocacGiR4c)w?kW+<1Gz}_1BQt(%#bAq7>KhWK&~veWKw&W0FWl4dlLV;a7cqvMJf! z*4Uu{Mhzs-ZX|$MYg?kJKACJyG&DSu>}*c9wbnPcHtyK6xw+w@vR)^fJGVEJk-H%g z-<%-Pc01X!+j>U2?sT*@>}hIg+}zfj;Hh|HgQ}yV#x05Zwk@=yX=`(Hyn9z;Q+sP` zOEXcJI!LifO74buV{_X9rS9%%XsqvwHzY?944N7{NZ*}Ewj|UOl6Mo~v3^J6*X~{N zLaDl7@P{_leJA)sn7iHy9{kKrR%_Fhce{`NWOVGl43jm1*_EwfuA(_8eeBc4;GqV) zSk}4D7bigIkz)`Qb;Y1{K07b%&FthPsu{c%XQxmkVSP8RKR<<%MG+uQJIWsvuD;2_ z@?Aio>lI2EUHm$!1jP|*p$s86(89Rb9i^!s^}MG1GHNTi^{Be4AsMBsX{AhWgp$`v znc2PSR)luE3KAfF04kq*g6Mz_b@&a;vx}UWP^2L#!3WC4@wOpuiNcn6f6LU zB)mtKMj)5YVy^YyfV%3QwwLmhnF~`YJ%C}Db3Y?3(3$D2?qvwv0<03PIx{Y>Pyv7C z^(Lj>Ync2Q#U(sp4K}%?Trvjix`Q;xa7zzb@tndSvRbx9qmP?MElFM4X#L<5I1n+S z3@}FT^iRLkcF01LgF2C2hS#9bvnUnBDOjboW<4ArL&zO$(paA|#fjOkwC4?B0y+oQ zp6c247Wx=Xo*K5a3m+}BuARI%!TW`_^g}e9ye4Jv)=KOG9T9jIxIn^hwjmWH|RI@SFuM4DSFe*M#T zTJuU5tMdfr!v{uC^rGC(jlEFQvG^)&$Mgyrf6SEV+FfP}ZauKBvfzB6VZ;p}ts1;L zbk%-CcQ%G7LGwmBkm_|evQ%7t0ZT>Bgg{05Q|ZBhiUmSdvG{!bv9Ef*JhQl}MU#={ z7Ueqm@@#H}CWPL6i*eN?hISe0JUdnV*S{5MtEW0z#Jg2@@#l}k#)_%8T4H-OAr%I= z(HJ&3)IT~paJcmKk6iOQC)V=NS{qpC4|X7o81F6SecoF|*j1h@erx}id+o*bYhGL| zymhwIapMZ>Eq?dkJm1!^mKzs86@9bq^MCVa<0N-Xy)sKmE_B^|y*$Ig9-{Ztf=PM5 zn7hlY2td03Nb1xQJX9HIP*`JGVHmKjPU6DXV^6aB^^0seGqb5zv6_-GLUie3H)+YZ z*<`{YNm;(g1Y03Pd{$={Z6WlgMuu?GnnX$jFb4n76q1&4dU*zhWFThNZ#8t!)oRT! zNM8>m?g%ToaE(xKJf1#0Hp=3?J`BIm^@#<{8FS}cH?p8Cue~xnKngt>T{C1C%+OH) zMXr}UXY7Y_69uPaSLvo%HtYvA6pvl{3mqEJ<4zHk(TLWL7@&Eq&ZqiWr*pI7tZuoU zUd+ssjzCIjEFmnGau0w@+(!hZtB#ptL#(h022yO2DOSw#~U&j6T?GbHX+ljrIba&Mh*8 zfT;yKqj7N86`hUMT*FlgP&hkJHu65d*Su@Vu{;LR_NX(N`FOi)R$o9zl8 z7B4I{y!VfT9iwXt!oCPtg{Xg9`GQ!rW;K^WRpw!Cd$2@|-xs4ZqgLtr&Agh1|hgdXZ5D#WzTp1jBQ=iQ-(!rFrcIH|hmpV_e zTxot4swc|Ki$D9E7;0tCIO&&Z2vat?03gz!vU8I_PpkRAlJWw+fH@THYu`yH9`m+E~Gp0RKi6SqOC27y#fxVz+6a za?7Q_$=AJs*2c%LMeWMxaq4Cbf^ z9qxwu4c?0+_+0CWndRksOGgeJx_|$EKUhU3c)1@zM#i8`T_{ibIK)Hl5VuQk& z{xAmlx7~^bK9ep6er?~;zG{!Fqm8O#{5M-e$xodPB#5;iOc#biOYO%t+ddivG(%)Tb29k9BV5zR8yaQn0xKU zM=BB-5b-MbVuL5MWIJX}0R==Ia4Rdg^)rzWl<_N+WH2J&1By)s zh>Oq%fU|tkve**90}wu^U~@`j4v2#Gh-JX=;e=3!wu!R;IJLOwK()@Yer-yiVs_7m=^BpFaT)>+C|%9h>AGjFrqWb!E2w4YRBfYNdol?&eN{NdGhG~ha$R?$F0 zu*rK}?Uwf+98yp`{bX?|lpJmbJm}Act~(^UWPqC2<(D`L8cO$uoIK0jW*%z_!2tPt zQVL{A(H~Uknm=ykuqQROlnJAZ^}WXEWJ>>lIBy9T=Pm8SE!Wat>O9k9eJP(SU;}>h zT%+?TzI_41(^Qy z{Kf#&nCFln7nUpV?Q-BoHKoPBS%EEc^VX4H*o~Ff=|?+`0K*bvD%Wr|f(@`eT>Cf;jN#A8!7h zLHfn7|MTx0dJ1^7*!*k%?CIFii78G764yB#kj*^~Kht#yKZlM3 z)+jqAXAXz_8w5g$;BrACw=n#p`gIeRbU&cdX;?H4hk(8z0 zkuq?>p`YAAyZq)S;(C4jrGt;w?qxazv8Ay(jW*zWILSSL0Hnjrzr-g|N3Ln*r_QkG7HBw3p%xO3bkE?-p&MN0d_Gjgzk-{! zBN}z(eH=1+S9afpWq6MNu8m!=A@S!00JCAI^-ir0)MpG~xiiSEN{>nd)Z7mm84^@K zZD_8q?3-o&=Gdk+I5OPZ1ea%_I{$i!KkbBXaMO+g^6)6(RT%-@HaGs7#xMywOKota zpgZOI4fV}2n<+7XXL@XG40kt0FV3Pw2hdy%?OcB5$!!`lQhaFzwYw-0<}!=V@C=H` zOkS|)?A^*sIY*-xRu`_Xp#IdkPc-d1QSRgDh#cC6Dv`MdhV_7Y_wqS$u609hp(FeP zhCa8RXb0eoo%t<1_|pY#n{Mz`^_z{7|T-E2hsKEdx*VoCw(U#9n*G(;%e zfUZ#rGB8q*3hs{bok!3EfhC2Km&ise@3vjCI!Nuz{)MK6Jxn^j{Mmh!y)(DE%YIrR zt!SGth4F+W<*$H{CPL2cvKP5Go39-~8Ah!QhjGbKjdTd(x*Enf_}!H{Tt4SIjS{Jm zgR~o_<&|x$_(h|yx!HGM33wTSAJrKbtAFX6|1KOj@_Pa1e=m^GQ21-#yyQiiN|87J zZ$g2WO0WFXr}z^nUHpvxjf6J+a%$72#;&@7sTFXP3z*IX$2l5|`iE`bzWOXCQ%u<0 zx}tO_?|NOB2Vd)JljZn?jD|OZq%?WF2_tjit>^ayNw?=9nyW!_m)P}(;lVtHRvbB; z!MR?KZBvz9vb(m0c{bJXb^``Ikkd=DA#!EDtE+1ZZ=6nrWw=iBwGb4nNA|%C&&?-k zNm~JAldKfZR{e4)z~cvb{3D@*i7;>t%#c8L@__?nc>*RXWBH{SGbUnQm1ynyoel_;mHep5d9VT>^_xZ2`FLG@Lw%#llD;ZdUrz_gPe#@k zKI#+vR+EA0xvIJ8{#dW6xbmkp8m||?lTjkk82Q*@&Gn6pRZ9%JWh~y=MwgqKJDTh3 z0Qpj?rFU06nM~w)71mPH#Ar<7fiobOqVa}C8xU(bO=G3l~E_L8YFl>&_SlIP50VqmXi@gz$F{cdzArL@+Z!kE`Wg%e;n|B7O9`5PT z31X!Q}iT77bs{ za)_sH58M>I{5E|N4q`?F#V+IEwXtBBn011Zz^e8KhQiVLdkT`InV|5wP;3>)8%ug1 zRLc=yAA!IR<-d9*_5MI0FTfHV3I=|7j1fC>O#>2oHxxBz61_qhuZ{zXK?e*N5h4gF zXazK(fhV11&c;KJJv^-{3a#Pr+$wvGgIEm}nzw*Nk&NhYF*hQ0WhFM1Q4?{yLNlEZHk`o77_O;NJ&qhX)@5Z^?tJ zD$KSYH28m`wu)AfufdZJX!|&36#7Pxk!F&DA^r-Yb2eBfh?-;sAZpvdw8sb9;%#un z15L0_A8mgWbUrg*0mtqL#xM{Nj}y7TL8S6`f~?$mL>R!KLI^Jh<5e?Sd1&^k5zT{M z*p#7em0XFit7I5%BjR0NOtJrQ4AdZtMbwAFcBF8g4=)JP_OY0jx+wUH_QO}`ZaxrI zrw!g~-|Qo)Yxd1B?s0+4>R%exFrP8MgGmo-xTzRSU0zP}g)e*=;3;d^%| zBp()sKrZYLYU32VwMpPr0;!{E7x6j#yuJBusEKUST+JE6&Zw-snok7lR(zWy>z-zu zYccGiSU@6X5bkgt{4WBAO+){X@X0%Up<$;mQ;XIQ?+PJP@)Q^(t zcwL*{7ehJsgQ?=Fy&?g!ep0?EtWF3dHWLcK(4OJqp0tK%dpNR6T%Sb&*nVwZWm7== zoc)^RMryy*GmVK*N4p-r7WeW7U5u#e*nSo7)zCMF!LKt_;)eT!5h9D*^3=2rg*`+` zK#R2d+-RSAvE`V#&WMG#8M8bDwq55i5!nD&r&K3MTLDiT+_9idPhEvy@Ao1EOOVHo zEzWUpR1%HU!1joNDAm2a>8J+-taOX?!pyGP+k+F?92Pc(Y8lXTg{Ceqf@04Y zrZ~*ua76JhXx$gy$p?N|c>@c9K7D!sZ_95Oi)(fZJ)y`P*2l8<#8@ce6qW1?+7#d1 z5f`$$;`$Jc$j6|(Zbl*2^7jsHkwi$NCef0HHXT&|-xL{>Usd1`dL(+-yIFJjNx*N5 z269xZuWAMD0rqDI!<5=~Fv@)H+L=sj8|Z>y)J9`Dl#-WnxhI8Dpw{=~Iq4e18)n-F zgPuUpdFNwsB9JJfOl+70hs;r>{{+99LmsEJ3MV;cn`{$R9cm#rDg|QOglSYnWw-tt zov;9Zdvi3lGv-C+G4aYrL!K@#u~I0PR{ui)Jo&zh%Q%mKUS)JlN=Y@Slh1}2=XmtF zfgu0xJr(Nryu}=}a!@ySfbb-OnSlCYUdMtFcS7*7udfhnbh{NR?gJwU$ z)!Ets-}Tr=i5TrOf-_znC;BM>T8ygrPvJTEE)yi6;dT#q7r!f)f}z>0Tz$08Kk0dQ zz~dWeI4Kn6YhJ8k$@32y&+#H@Cpk03;eQVgGF=>!X@+2uNDB*s?)V+tLvNRsHIpyW z{e#hM^+vAUq8UqgY7Qu`+&3m_xt({4bTYcXO&?qI@p0Y$n8pg$Fzfc=2O)AeKhDd& zphGX_wsX35-Y|V$P!g36D1~5Gm-2T5IffND$;BY4V@@=}-Hq;Rp)Uoa?A8iKP!W=z zy=EsB+a#Fkw*mUvkO~qFK0GfP<6#Z(IEiu5dpN0P#bcq(IzTctAC-fVFS^|n1YXA( zwdqA`!!}_}lj_DX9Ec>R$t3I#_%r5GAtpj{@uudT90Q)|O0?D2@2LNQ{JmySknyHg zJ{p^njbIPAG`6+3lgF{Xy{Vz0>EY=PK$LCG4K1828tR*qP3=hbJ6q~^?cEk{YH8Zq z(9qI)VhaL)eDk)Jc(T2#slJ69Tf35tZB6aq9m&nylxS|;+}hYevexZwt()tc+JHhf zwl+32K9fl7=3LQAp;mHRH@7y`H=b*3Y;5aDv?ZDwXwdf7ul;LakWIiKOPgYI!4fdY z9}lM9J5zZ4l0k7kpYfqM0Ge^^n$2O(zc*7#-)tlt)Hi!hY%AtT%o%o9|HV%?cw6$v ztK|%P=%8Jz7vyR%N9ZwRc_Iw-q{l~vO4;=aCw|lr+0-}wobUmc?=Z>lV7fcA3a9}! zAX){AAmdKWVfF%pCENjexfP;GE{f*l!Js0z6D_5VFNVMI=N1^F4|q@_mfSIGfEi?bk#Z%g+vi?Ie>579n+3}!zV zH;oF~8N_Nh0(LR1H7J&p5k+P@dq@fq;sH(12r$VS)AnLL0(<73*8>8Zn`#9ejr2JL zrJ<|@C!j`Fk*^z_U9cE`ljsu#G61?^U`&)nY9J~i?IhU3aP!p`A#99Vfcnks@mK}X z^(~gsh+xsI4N_EQx|g&OlU>Ot&`lKu#0cNLv1imaaW;q1?O;7P9fJ7w41xn2I(!(K z7#NT*T-}sYq zaZ*Q4$yrSO7#^k{H-s5tgcT&_n9-)i!$Mn!e(qlJQo}-BvFWR~Lpyv8utXrG#TiIT zA;$3oFzrg5&~7l$qN_^XR`1sx0Q_KG(^ytyt)88>{7WfBaU1xAmE^Bg2FJV}rv( z1L=bU14jl1?oOhi%`I%;lg|tUz4samkIy<_`Nt~2@(m@6pZebx)^OCnehrQ~`4o;y zJQfb_OMT~aD^Sk)Ea?UpZxhuZHxK6^Qq}R5J9n6p9>9pASrQ{@#hgI^&Jh|y!4QyN zm|-HIm45CtRV4?SxUlKQR+lZmUWye8_ zJZ(sM@hn*oFtLaWD?}QtNG%YS0$R&0!pSc|lrs*mkDm;*T_9M38=N&kW()v{ zni{(Btt4g@vLJ1SE`~)gcnYk?IHA8LofC%M;>2GmY`M-z16)`9I@X;J;(%Xg6r;|u zCK#-<%h*72)L$liDnp_n)v}PvxX;vQeT_nPk9HUudEKzJ^BLqp#q@azr|7=p3RaDY zLA&$7VTc7ZD+d(G_u14t&OpbSPUTj#6B%xjZfiqk$>8DjjX&nM38qwLzu)*mYHlBN z<%rHUZV{cHBEW|1Zz~V_QzzjFE7ngj^a;zLLa=8d<|!NyyVnACHOETUG#U7r-{i}) z!l)=WX-<1I^nU?nL?&i2NxD*FU(|6$y=tCWJ;FO{`cf?XW~41|jfC@BtHEU(yO5y} zmU=NWxw3)1ru$f2eS?IC8R;9OGa2!ARw5us&P7K_)JfEn+mPtQ98tffQdj**U+M7? z+r%z8zIfeancI1LW7+l$)xgx|Q?FnnVGC7tGNmx?q8TE8+{;2o8XC2;QpyUI>tJo# zYNt;Z9V5s<;FisUyU3YKBnyVm5iF|z~mt#{^^EOo0 zudZU_vwW~~ltV(1SradqyMR~}98+O>#>%b#8ZNJ3P?)qFD#_?C_(AmCNt>|FWiSM zL+j&|(BfrfGOTEdz_wFN4zObe1V|W8GI^{1oMo7U^-iEOWrIR8a%TLgUnaB5d^VtTH% zG<8Equrhf-X4F!%bE-wqjCwhRq;y;WMfQWds`*! zH8_*$74{K(=>(>AH%$x0|9EnG%Mr~cb=s^uo{DM!i-Bs(`r26DQXNva9rIY}yFYr# zYn@!u!GaY=d9@85?$eE(`g{@OG^bLH!Eu}iIPa<|6#!DAtfYUwM#^tXbYiLoO?BmIM;gJ8RgKYyUFtJE!iwlf_0v5yuWzhHdt$LpWY z_fo@!wS2F1<+mOLTT6fc|7-{(@-}-F&i5RXhQfmlY(XJeY)QNH0>m8TlmU$i27W@b zYWuVe#w8|4$a;13I-?>){EDbS!{mZqF8gO%#49~}Ut$n6IiF|eU=`R2QeJNgUw|zD zK?!kvJ}aMVVCzD9EV?Y`AX$ASv?>Sr>3%~d+GwEPiuhGi($MNNvz)2z;hMtc|BL8@ znM-nKwNL8H1)-v~I(d`tl46UDUD|eKK!Ds)hnyFMqLhj%W*6>NZ`trkfRn5^!6v-s zHO5+hx9|CommFUqF-Ns0;%&sZtjv&;S2Iq~Py}KffY&sN_28m7`?FQ4OG*KA;$s+k z%6Jk%%%zS|v@k|S17LHE9Kz;ifgJpZqSOmxc4N^8fw1$C2EYhQxjvrW%Kw~=)Fe@# z-^@JwJncl&;@l;;JTFO@b4=}+U8hriOIfVeJr2RlIvS~(UP4`*c#MWE9sJq>kyDJ( zdRfY2Fvcljs(EwQGTw`8$YN^OogC+@x5?4MfcL}1F+7=nuUlh8@4b@EwilZc^D&TP zK65nxTI3Bmu>x0uaC=~{q|7maf_|#geh^yb4Azf~=#Pa`50+OJQ>m-9SJ=DgR{8A5 z(t?HiD>Tm%Eq6`I2x$!!n%fN%CvY%770zJ4G@b6QQ3OHska-nd(Fc~%QieundE{t+ zS7r27Z;DjA{YVvLlr@4zYAU{b>G+@tb|20(ks<$J^q0afT=ri0neZ39-EVaQ>KWJ+ zX?!WrTX^(5T3@qTt^07=>2ayP*WKxj4{#22?#zWp7A_#sM=|1blv4>69t}!g?3Mn- zS8saTOX(|Dyv;KN7+Wa3f0i5BD8aE73-25H;0XF?4597^p`bX2Dh}BD(-hnruA&&; zZ{!^(Z=&k1@499Nh#t@*fx=leu}NzC7i6O78!eSGH@v;2p+9xg>+g5ahDWmdz1sAg z%I}H?u^zntNqtXR=!-Ah2>j55env~b&ZFB)lRVn7^9EIZBIr#|V-DV<+hbT0vV@X( zmLC@rUbOTs<&GW3#ARNSg-0(*55F^nNkfYGFYXTfzzlVKR2YCoFG^w{CYIPKFR3!3 zYm`EhH@uytzfCQBnx%rDHZ$5Yvg*e+m;N8F@8~;Ao!1*9U{EH(ClgZTeOXH8WtYI% zfk-G5_7Zl6$-<3T={aiLdNgF#x80@pi@4d0&m&JtJ!xKp=i+`L@3{9<8y)()^#kiDJcJH{Q=tsxuS@xq-3ceOY@?g=Lm~|D&p|-wVtZ9vP&hH>98= zgl;XozoZ67Ly>pv_qT5b{)+6*7xwUxCkoLlp@9oue8%Kg>I0vq zOLc)A^^`xhz4Z4OnbZNz>2snfY$F;=g;M%NC`pP?=kSmGTzJ%@HbzU86 zofSw6LXau(1W~)dXDk*To#5BULt%W>G1EOd$FBz=uXORx-1K&R1S@Y&Cd@}_(2ZbV zq44M?Eon>yu{l2M1nuR8B#9Jkbx>xf;vv0%ORYU;APdz;^h0(urjhR_4(T57pVAU< zI2eqCN^`V+N9S)`2o&lAKNAT2(LR5<0--4!Eq?3Fm-dBzU|(RY2$<$(@ymC=6ee*6X&u$eT~fv_5x+-zNwUl+C=2 z5d=!);&vA{?0p3QJR!8rBa!^W0mA{@&?1^|!wP)3weZr3fkZfrHcns$%~UenJe4I3 z6`^Nx3oC4Gd0T2ZUVe9HZwIvhNZ*IwxEfB{eR%Vf75SJNmI%l03CQU#Em88Vtvzb; z!|M%tc9~a1qY;H(#jOA64Sv=~8t^RzC{>9M^hk^LVNv*{FDs0Q&mNF5@NFWNW#`Nu`ADdl0f=XUf?Ja;#$VMeY)!sWf!(DADjOe)SX_yzLYc_l^+Gu<&PP{y z=;39t-iLjm0PAp`R~9b59153yks9{p4^sbKP2x4{{C)>ox(Wf`s(-k%-U#Hlr==*; z9(@KJ7H7)B``Rq_MWQ+98|pLUeNn<05tx?IeTmR{h5a62E&fD9(^zB*kIwSYjcDzp z=9jp12?_(8^~HT|H6HD1X^La0Ox8CIwX`78^b+)!8_t&?!Cs&)2$umvyp7w@BOBRNJt3;D=&>(pqj6V%=wdc>7o(EKitQRZke@HW9a~xWRlXu`L$&FRt@}DVO~) z2N=Ix*}cVt&x*&y2FIp;XNluD>+6`;dB5mXF3^7_&vB~Kgzv%g<>duI?_4W{zL(}e z!lB#;x$Ja>GT$)*Xh>?j*90!2i0_++tSKYR!US3JIH4ifZS>GHue!2w@~QrCwaztn zt12W!!J3z!XCO?Ux!zC89s15#RD+uG65DV1VcrKvIL|ST9EW^FBC_i2d@1#ZE_v;x zrqL_jvrW~xUGG~p);}~lfLqSj|MaeoM0upkJ~_ibSYLSD)3Q|9-u=d>C&mh!MMz6k zLds1|^)2VJQyU!Y(gta7FW-Nvb85N3_wJjz;fV^x^*HZLbjh=XLwDYvgtE{n=xK!L zq1P$?%Z0AaV^1Q94aD$tS}6X5{%FVV&B^hzzZI<8TJGJN0jr&|7>-n<{R1Q8!^Lm? z&hwp>5#BHZ9lh_J0`cSgsXiYl`%_it4*EyugH&E+0}6zatXy8l2&&~jj1@d}xD}6w zm4qhCf3xpai#>@oTe&>TteG~>B|$|00-wk~nNgs|@;L>JqEdq&(&vMnt3Gl%!g3klpP5K_d)QT%ift z=6nGwFLm!69>TVr2f$vvE$t+!b``I~e5oq>7=O4%HIFt28h%pb_MvtWvY@6V*!7@V z(%NG2^?e^IO|j*NhLG`MD0I@yJAxY+p!+DA?YqS6mnor7>etL9Zg0@WIbv6# zfX6b>a~`c1UYal_raA+8$R^~Mga_wPv!3z+A zKjo8pZ8O%r7)NK}^$5hon_+on;&LlHJ+9op*D+7y93^d*^(57U9S zd!3*wn_kX$AN$GN*t^>HUtY6yz~uVG!m`t)D~CT598`^5yX9Z|9M`rqxoZLxIM0{T z#91Jh8!i{W^_z#YfmobGE-tTN(ccnn#))0KE~b&2b2Nq zq%4BMD_{b*J%K4PB*zkbj*8_22umqjj1-o}fs@FEAqyctVb9Dl)4Qfow%zzo%3d_P zu!p9PR+^5A5a(RX6y?_QLqPH3$67nuUL72&6s-2%y@fITfDx=Z?t58#x3sKZP~26rkrppV%@M>*NJzWLU8d=WpxZ8MamO zzT~iz>JEcZ>wo(dWDy&{7s;4SR7bGCi-U9m*g7vQXw;;C!dOdo3&)&b?AqSi2T z$l+DM0_paNnU%Y|Mdd0CvB8^1X80sEK!keNLUo5UdbIAKS+ixqvkw&y~_=I=$9cRO{_NLv0uh-_-tX?A(^!Qh;$E92zI*DdoNC;2HwdEkPkuSj z7RLy#5EMLK`pVfZZ>0EzJ1w!E8s3R@abx(w^x^*Tp|Rm{7f7OtwXMfHeq0*=R?Nu)l!@9w7V2#`#Dt`9=Xb*3G;<5BP$f9D? zk6mlSIJD;YT9)2*P|)G~0}cd&5;!0&W$gf`ZQWHTpq+&=u%ozH?_G(~&iua#w(hrN zsV-`n%&bCq^pU?$rvD|rvCOf?Yf~?N?h|8eU8V>iAfan)74=t~_)NO1_}TePq!>N- zC$<(Feq&EGe_G-3bfVCZ5KIMy+>%*Luak44%!XOYl74K9NRKJ$kQFEXgD#p>A!tG> zJv6{lhdYSij5DvAh&R2!`5`qjOhf_yyi=BM@^&P$qLmiwOd_3#SoLBS`4mFXzMPxL{2F3*yp+0=v;$G>0Oyr_GiJNE3&Q|Ntn9ody*Qd z)SO)nwr(a?Am;=ZPs!zQvVCkaTRL|4^TCeN@h^Qc(D^e5|D+c$Ci+ju^LFeij~6Xb z_0E+avT^87%^LaE@fL7dP90T>q%#j(XkVY`U>AV&2z#GJu7pLXmX*WfWcRC8*? zW=MWs800F#H^(P9z8sAqHve4A0hAa&WQ%kMW9=B6N@P_Y(-{c{IhD5iCS;44y!wZPwUQu@}nGQ*9=}U^Y4xw zb?mCK!mer+B!EiND=49sE zqK^lFl9VRZN|nEYrcFfXsHlU$yb)!|IqT%7iYgBi*w^;Tg& z`EwR6SCD+uZfU?~!Vv%g=GCN_^!rZL;m?=hWfq}+2e!(}k4QAE0G@cZ*}ZL%HaVm& z6aOz$oA<#b0GN#g7pC!Cqbr5&$)tMt@L4k-9L<}XSVuo^f7OyNnd5fs5Wja2QG$>X zzSm&VI?zPoD*0R6j{_RTPEGeA4dt^Mz@fqp4RhO7=bI_R)g5y}RaA{=u#SZ-q$_kG zlT{>?4^L}vF}FS$D?c6zDNn4QP3d@D7?%U3k=n(*j2Fzx>5Q*rl)@d)rN3ziMSwJ0 z3N%q-8;Po1R$lki5L8DNpBAS1#Mq98I+aPPR z&a@1Pgr3uwM9ATS-6-VY+T{2Dv@E*!U-cS6gu((rKPulZR$DjHczuO}^4vF1w2S6h zyi;|X<#`)QJi-9PRwdkD4XhA|Eui>8WO;xPEhRmYe#sq2M&mdgg-H zhE0S^Z*@{I(LxR~5-_B>uniAyaBlvZdjT&}^lKu_SGajhGmu|_Lj9x&M`X|XNU#we zcALO0I*nTvokySKdLIM_tlDqv^WpG4P6JHLGu&Gac?9Zpp&`x^Pej3=+#TE|NdvqH z#h9`9a8N-SEJ6aqTR0OA$zqHn&pu`Yzuh$QMXNr^pR_JrgmakCqDOZeb0_b2<=iNj61v z@6--HRxn1Zu!grqefY>7-J7io3DCy%q&)A3PMVLitsPJH#eOk_i#B6HGUO;SG(%@? zZX;=4Mlph&qvgGjhsw|BKOuMj_T8Py1^HTUvkCuXr&Y2^bU0%CG^}Pt$@CL%a{rlQ z_Dfdm5awz?3g&IuX8j9AT!Y!H7xS!ZQ!&V011#$C)r$kT^ELXdJ=s04BnA?Q)3~>b1zi z`#f)QlDQLm@vy#fKdXV*srNVG?updoLI7-wQsk(Xsb#p^9rOb|$c>!5HS|&bvm=;N zkyV{{tz{IcQ?Ko#zVgiiCnU7m8+uN9ffXEZ^}g3a9?Zq3y>K{|`+sSB^XNM7^u7=G zeeb?6xY$WtfE&1h07!zHxPZI3i=;$Jlth65NJ7LWfD{Qzqw5!AkDSD7HY8n)nMoq> z#92Ib+w}CLo_c9hCr&!k949BX8!w3yJEuuz?3pI?n9@vukr;MkApW8nZ^2)0v5t>dfR$0#t935Atv?$ z5hI#=R@slsMk5hwkuWz-?DH^iS?>g=Tw&OeOPGaU~RQ6G7`lu9+M?|NUKeJS=r z9qNZY4X5%8j_=8J``#QO-C^3um%W&v#uy$EmRXleMLX9tZX+IxeaY! zI_#5Nael@~yjz|L#7SFVZzL8oMU0#2{x-oXyq=6jBTwAQ z9>cN@Ev;K%`H1h&KAv+?+BwZY_oETq5!_T@d9u^(ZkmEmnT(>S$633{;9yXWsTVF? zkduvZ7-QPm-&*_Bv^u=8MvjYCko1tYi*VJ0R6&DsQI~sSmb*<(Cx!i*%Y!bdq4<}V zy(mcDAwkKp7m5*3M?Uktse55?_=#v5HoQT^T_&Mp(S%J|(Q)NCnv?gy^M0y){w#1K zF}$2a$o0`+8ylbve}Y77SGQ*}nZaypx*3zM7~(zp_j zlcH+U_8jfX#LQ35ljvgYKE6FTZPGusY)Pp)i_;-hY+UK~W79IvxK5kHp~&)0#jO05 zYad1YD$oz&M{;bYyk%T!Zwtr?gz&hnZQgeSf1Rfchs0n;7Htpc({FJgL%(JMqurL1 z^nIfOds|fJH~g4^-?_qAPaoLEe3n=8+3qY!WWf`Qie7XV5{DJLf90yWe(RXJ>%5Ws zm&CK2u66G=D$|u7)Gf=H)}}AD6<${V8UcMp_y|L-7iuCHixc zp+Tghp3-%xbvqbT>E#`5z7E2~JQgzpdg&5U%H~vyM3_oI5;KMH_9xoI%Gb39wI^^$GADg#kz7uJ^&)Mcw4iH@KR#8@7Vj&yYNH!EJ%92( z{Vy^(9}^d(JHym3=o8z}Bnu+LiS)Wn-6wmbD6e! zwoD?d!p1Gd=Ixnu31_7YNDY@Nog~I8w36@&$ECJBiL(mDT)sUcG=|K+)?#O|u%ovG zOhdU;OqZIorOsS>D1&QMp*WDMmZ~k~N-jrP#awFJw-(abmSUxxZO)NBtE&opM3$PA zI;ubSH5M~~hu?VJ@2w{h?}rfYH>Cz1kk&}it!rJsovf6aTPz{X&-1bGomuRuGZU<* z4I<|8jW@1DyeQl~v^4DVLBPz67tws$NwQvUXz{TP0n)<|zh$^#L0skUB$KJ|Ssjqi zHRD{idj7)P`)f7o_ehdF#|X<4cAIvWOfUZ_&&a%Y`0|J`y{vg+u!_7XT40_ zqN$#0qG&X+B@POfR&v4sPELx}9@G|mL>WFOQps%|vuXH5yY}h9SWGJfxrc9R!EK29 zkM4!v?~D2*nOLjaVLv9_58WXG@J^Z>$86*z8(rUaj(FY&qM4emJNJ2Muqi&X+uAl! z^)tf701&gW$&qMJS?!Klj`BAW$OG%k)w=(3dTjGf<4sBG3`ESe zm>fSPL$WUdFN{BD$kLbN4g^j7Xa)sFa1V&WenV$Dn}}&kMJ-^=FmRSM+xDj$y>T%l z+Dp!u#G#{8aaczndK9m))+Gp1Pf0eX(lwe(?M54n3@%+3KGM>V@d?|+j~!3O#Mx3) zr7B&zSxzSJPRu+rS4bxvZcZg8!_1SmaW8eH;*TFKl6lWna;Z0&5eAQJ*+{3357%G} zzn_XTjk)8lt-STm-uAn9xE=hXq(43p!ome{B;^MPq-}e?8*2g-nUi%{3%}LsT*FQ~1Ivc-6I~K9%w3 z)G#Bec{!L*;Ab&uaC@KVvu~!4q(~%73MtH74S{#uPs#HE`Eh0)!09EnM#Oyd@ox1E zBA;5jY(Z?*f`lRf$R&b&>n)_)$Z5|TqffMKJ8<+CBh8khz6`qB_KMh?C$oG z7E&mwaMgU1i_f$^-%3Q~X6RPtYYC5uVU+oy7l8$pFfiQKnoyC3!qeLCv7X4vt?%FT zyh&W*nZJ=>fc*fv(IvE}gjbwK0rrfcbXh_h5=?+sdl*X+qB^!lQAP1yy8)lYW9$Vl ztkyG$v|?mHg0VElE_Eaywt$bGL=H2;*yNlxgmq4n@1IR1q%awsTc70Te1C3yoj*BG zXM+iEj7K@0fEBo#5)UoiK>4Vo_YQ{~rU3?!9h85jQW}5jaRGYUAS78YG&T#5VqzzR?a#zU1MAACj8!7WARXi2% zyh-7aGi){G!jQ`F^kd?Pafa#EHa(DTK3$2WFY8{BFV-XN?X?+D+9EA2)yjtU3vH_F z%csQTc-^guww_|VdK}2wNV+?{wJqJeA(LvgO}$JGY+lR9ZWQzBd@9NdL-A-fRT!>T zilY4+q-EXOQ_F7lG<9klvgIwsYPzgXcUe_7WV`FHlG>Q(I#V0wj27;ey0`7-!Dzw~ zt0q;QizY(!tAqA-pXm3K7U?Fc`)wxt>m0K=7eq=O!1Crfpr;@JpB5n9raWnEbSDd^-9)LQ|&@78huRm zgtfim1}Tl@f~+P=+gwO0T*_F?KHGZ+EpKtkJSl`QiT)? zZ{R1O1fY08l0)A3RaAM1x}q4*rG?vSqOOicNhMC?-3!D-nW!V^AH))G1!Ph2{!%1r zE-vLzt`4eDw8>CsxqXrbTMwBHTyKwz2c9fv`9tGf{S0 z5{J?)>d3AXd$&eRB1n%|n?}R$`cb0FB_V1BZpzkupm&{wq50PvP2s>efoF|+SmSsr zr&|bkekIZ0vB#=>5^J(f9Y}0f#@JxN7)yra71gjn`A{#n+ z!)+pV#}izEIpedUCGR7%-Ce8o2Yytp6`_*nl;@+6b!xAhYdg6J(ne$En!7N6a9`y> z8ARdOi#}1OZOe)PY|91{BD%q*ef85@^v=#~MJvl!3{l4;4JD~v_%Z(4ujt|EbjS7$ zBHMnU(6Z-EGXok(tFIj_db9nE(eI2$ak=2MO7-8IRVl$yy}#jbPm7sd_O@8jd3&PX zoDf;}i>0pcgKOW;+l}rA#z9AQ_qJ`B1$*(8f;NhsrREEXUQK};Z(FU^X2f|KUVJm{ zdt>XwXaWU=u{>SUi~1sSd!k-l(z)?Kt$qeX13VVV>c`+aCT)v~UV01h9^O$`#W*h= zG#pSU3d=+O&+c+yu$}YKcnHF)DJP`Lt?8wa{e10-ma46qVl)kDhf$fDg8qkZpB2yc zxmX&fD^Vb{cx%J|AeO=1XK@PO46B5xcV8yAI6gpBUk$%38EpbmU!#J-DGX1Vf3Inh z$G2-k?9jLb-b;G8OFbBz1W6qFAK2#lrX;0}8=6hubp35LaBJ20LCuR{8FUwrKB0P< z)P9}4c~Ct#==qPwm}(-PC$*96^&%gHJRUs5duvU2&r6KXfe#>QaZpt}?!|C2nyGUx z(f*JuNSd@J*E7RsA8=xOz)|0)9GMvr^nxE#_Lv)#9d1HPePJ z0Oa0!E+Zh?%#PoCAy2mwRk-xOIFN{Qcs5!a2~)j> zNnz#AGBSM^s5oS70wBn*jd_^>^pU4j;L%j0YHKCoyenvf<-x!G-RfByiGnGF%sAI-Y>T5(DdxV$m7zm3#z)NvB8?hzKZb&rz{ERYx_%;Z{Dx4wyf1{@%m1%SmcAevog zyS*wGu-z}@2*&a$9<;yX{{t;EMrcdkroSy(xE=Y-fy7uhXbgC#xIn85h&g_${RX3Htg z<}AUl>c`0Z$~WHnw_dg0$QCq;uMbXGk)fj?aDelR&lo53T4&cI>HEa^=tEW;pSuulEj3LE z66z}J@){8n$$(kHsdymJptH7bI@e2f>5#ugk$X*ypEh#-0<2=bp^BhR{qA>&wHEe zA_ell6k>>cCfA712!<8lqiS7CoS492izxxY%41 z8v9HLh-72!3LuW+3GU+1VkVKj=oV?%r@#OSVuxrSgcm?%klokOy@XVZ76@Cs+f44E zRYY@TKBWzh*0m+-Vr|r|8lKswEKH^Nn z#_h&+Tl{O|wfx2Yoz>;|?{yVV&H$a{9ukxyLLw3cyPn(?iSk+#Y(V0&FX*~Pc>T`8 z@;Cpxf8BmaK%6qjjnlHn3l8s+k+ZB-{WYo&8zGltHjVX-LLF#zA$XyI9IS2ziEK(^ z9j-p@K=#!&761}1oivw z?3dPd_EYpMz8Z64th8$AGuud1*ffc!fw^M0Y3M7XO_hL2FLP&(GK zwq-%$4ub7Y>>Lp4*g?fy$`dx?pnF?BQd|)&Ti_`KZFeu zgMgp^)Z^vRU(YnZZ7F&ba><~{5lD-cxeJ5vz91{dJ~NjzASA6OGRW2e^?EYF(81?u zb~UzMxAU%XLI>AccY1ObR0sDejLE~@6X19Jr{8W}t~|JZWSgzm23?%~4?_rs_Vy1C z4;)(g`P(=A)-HScKT49l=+6~j@zVod{M1j5RFy33N0cNiWq3l-0>}b;5l!hR$PUCl(a_zx= zymdn&*IeEAeE1Wm@p`Nb2{Yg!hJw&RKM{H&6Y?M#ip&Kv639Iz$VB7t0gFoQvZnYp zLH@qyk3V*{0cm+2d$_O4bZ@d1j*@dyNpa&XNvjk|Ocl(k1P>1=e(4-uavSXk6SQiXQQ zM)9^6g8`j=vR2-QSc=J+=gtveKNpS0@!AP>W$J@y)O&(BEvwij$+=sl@>nu;LvTxS zY*zY>?L~b%?KA}(?K2%kO)qSzOWyC9vMakJCD#VetB{~iI>bAA2Eo-lzQZv%h?0Tc zl!j6WK1z7$yc4QXe^FwqX3PmP7>Uad`zq`E&ql+BsPLEw~Zj-ds0$L_m%P^*yQCibggg$2WYl}P?6a! z+laBPpS5K*VKdL4v z3{|gNJ7N)#dgS1@be!ZYrlK*G$4jw97;ou5x*4VAgkrCy2$oZw|3O_fG*M9nl}9Shb1Z5?>zwlQC5_-YP1S?G)>kJpAxPybQRj!wS$~kr z$JbqFF{X(kse|!`O&rd5u+XQemAQna{LBkdlAGyIu*u8UM?R%q9;b1P;w*x0POlG~ zlFl9VcNqN}j@BV^zaiHMoo~&rB}q5(W$T=>A47l<{c&EV=Dzu&+~1JOg+dI+UQQWPPd?|-BJIc%n>N*1(d$dD5T#sHX=Xv{f^9b6zM4Fp|R#z)&3WW zul#oOpL^Z)B7I-&O5wE_78LA=;13pwZBD;#1;@5Y)6AUHS7Pmr$NY_UIcC2n>}Gsk zH{HLi9;T?Z3mn+B3_4!jE4kCnxvlP;_yt{dCmE@EgU$jT2waS>{MOrV`z>{PBc{Gx zh*KOLlddx^^>3^9=Wb1!Z;DqBUaH9#R7BaP^@M%e8m{tV0aL z_svS&I~DQhG|qS7xu>kGPJJ3&^dhK?rAZBju&OG@#mpjPr-v(di(ZrjklYs$+U@|_ zY~8f@*m}!7Yrb?mTs3F8QpW6gprkqbllH4aFh(px_5H^RRR~g|Om5HJW6Pu`79EBC zboPuClv{+XTP{9HT$nNka6r;Onf!Ok8Og(;V4cS?qr->nkB&=1pFIraG~)~3sdy== zMHm?EkQ&d8@u-v};V`sf=(iK@_I&oEH?Xfc6@{#$A+c)6LE_}l?&qz?!IJ3Rej}}s=Hm2&VJt1 zsTnH|n#%Db45 zlUgzFbjbAbCQJ&jH*S|6?Q*2-i}lc$8-r;PU#gxeMAJC2p{Lh6a7`Wd)%SF_dT1_H z)M9IEP2vWN`Pw9d5wTEorUsM5VDz)7&S`=}3`HsAeh1Q?=$rVSoNZ}!ut-Iiwpn7+ zyzO#3qDk3$U)cEZ%!OFW{%fMgE8#?tReh6$3@Ro$;Eo~)$>7EwY2)X6k7=)bUZ43f zd=ccCtLH4fuT>qk2S7#Z!&}toa7TjQpx;K^)1l*vRMwcf@MGP%YTS>SdB#hOp+qwP zOfAa;x@|v4;0NYMA&lZ6UXkSrNj|hvlXO((4@bU^)PcdI{!~*mv<$~4EoDe;j+$Ha zeFC+Nvx>)3^a2_sGhp>l^wl(LKNv3i3HT&8T4L|EfHLa%M78~?SY3H6m``8QCc4Ik z{Jb-xb@%|84qXIP!B4L%%BciT5xTL!Bxi_J@{JfP7^)wh9`h5Vo(wyswXHNTK4~G7=m+I#C!%_l@mji?OyErU0d9p{pnryw(Q%7> zx~}O%(lp{_jR@T2d}k?{1+sN^k*F|7%*WKh$qYI!bR~>~2>e?r7tq5;4^XFK_~M>9 zA+9PO@0BFd6NonwgsyAs^X5qz>`A7qUd{qNb z{d`w?-EY%DSoT>AVkxMmQ0pazOrmr@oam*wm1YffvAEeU{O;A;e7G30%6Y0zh zdMhls$oO2d7x$-gFL+qmqpDI@#&YvAF5=Ty-_SRXWN?=V8?W+=s?Yja5<{T`2^}d` zC)J~u%YODDEgBoGqljg(IpoZxA+7Em2~QWEsLUFkmsq3)dCH}GT>AWBkXMo0u}e2V zc@K+A51L}#X_xf)(?gO6rIJychl&dMd{;a+`3&I(&)aL92OqPw zqJ$4tU)Pg)X&64A)cbc+74&zDQ-s5=j~lhom@oC^GoQUk^KJ!~E8laKVmi`M=XU$5 zzIG&)lh^I!xrUpin+Cy-RJ`F)u&DAMrV?buBl{E|ysZnPsm~TY$_E!)vMXD@@+NtR zl=l?PHb}}Z@yW|jADkp+QMd-H@9^NA!7&qLUyZ_oO-*2grby#V+AP#KA$2Gj2AS8mJ+6eu`r~dy@Q9APGsv*?wQPQbom%Fkp=xm;!oY3xZL-zg7(bna{>pRbf7 z{Sa5O*^`Q%bn{4nZTvl1&up{wlIP@}y9SCo&$G>t%yg!$nBI^swiICulex@s3&5`A zNc|kF&ePU-%Cb?<<3hO<&8FcR_e9g5fysr*4z3(XRnu*_AY>v`^#PaeH^*`@q7u96 zF>QE{q|pi8#SkfUt)ON%Za> zGkep9rQ6L`v2hJWM+Yhk?5Q?%Mp7PHF78n(({n*jRAWlw3tQpf#EV3>vhY8BpQ`O& zIn6xjy|{&A;u6^tZLm(4olD!7Rf``~^<$SL9dwB43ioZHJ>S&FUY7&=R{6AifO90belaairq3Uah~Tv7 zk-g%sE^6IgT>000=zL`F%Eb?F`P<^!X|K1h%y6>3E@j=o1=Z+yoIbwUn=bTm>3mv} z(WhhFI9^GS=Jr$RIC@U;lS#ndSGq>FR`lRgaRs}IeS1|zL@ZUmNeXSmqB_j&RmCy9 zi(XD+{KeNJUpUBlP4PLc$5JYypi1tQdm+B(%s`tpUXk;8aXuE9cVXr7e*<#Mxz!C#>d4ABX=lefvFI#b>cOg5vTfwql^f;i zB~BnFd{glbK}x^?pC0GpLu${mA*HOrb$4f^kg~(YXj~4s&=pZWhybS zMOsS26e(c0`-qs(-XHHC$aKtJbR=ne)1#999v?5DvUj15P#|7%Eq4s z3BUCrmz(86`*G+kxhiIJ*UCQb9;u(@I4gHv2L6I%2&eWOK^**#lQ+a#l-tOPfWXN)VCoWchDH@Auk7Kko<(suHz9q%Lr&D?bKk{itOouCfKrPyaNBO`n+dg(i zlsXragtT-9+6KXbK(MBFX@-~m0kfR_-EG}v*lLNp)~Bb7Vypks6{Z@c zeXbgfnRiXFIxM2s6;GiU|5QYZjNHgIs$|{7@YBIQJ+XZQu@MZ3O^A|QzQ5e;rpr~) zj5?wvOogq3SRY?F(i$a3{Zr{615_Z|`99TrI~9l=9E!%2W&sNEl(QpIPl+aGI2?bE zpN#r3o4cWLvjBLDyAPmJ%%aO&JZXV?$8^6Xu5R&i1WIBHoevuLJfzyUZe02BbGQ73ZbdkMdW5@0 zKc$RAQx7n41fSvs8Szt<;>!Pg?G@B@q;|i@2eldx?4uop*{I6;beap*Q(Opk$$i&S zYy>TVRzuJVh5?p)Dskxwf@}0m_Mm8zSsab}I$ZnDoyGW1o{ZLcmDv zFXoHYYHM4Cl+CRLV8|=QO0~7Q+S-||bmY>lh4u|C&H2`1sijybw3iF5-Pw)hi@Ve1 zu8rABwJldF0*l_6-H<8wmzrCurDAPU^SxreJG;NIr6ac?haA&PTIo!>kg2|!JGe7f zI#nsvirJQ)Qg&Y@lR1#i9L)A1SpjvP>By8i^JyXli|N*ExtuNKw|2GWbGw>z*)j|T znCj_tN2y#Y52b(X-BpM$7`5Mp%jyMaWJRY|ac2O)3lm+eIZD-?X7p7n~08%ajg+LMf3u@mV4rIDpAL7?gS#Xs>sqCiNrmDrf6kL@3lFR zR=l`EJ9X)qCdB?!Y;pGKD5nZ8T5_=;eTg;hRsl>)*E7i&?}_D8IU5oQ8R%h*!`g35 zmQAF<1Yz-XPvMwY!i`#vBtF9nKQ~tO?MjsNDG1LJ_Jf!FMCe@TL~SS(qQ0>;13sTT z?tuz2KZ{#as1HE;m{_xjo`x+No%+Ye>!I7YAsKB+`bdY)@)qPW@$8FUcL_F~`$ZHR9E_FI05%JLk$}*XhP)+QXF4#u}WXg847X=pR77W{- z0*@amG*alW(c7sqyn?Gazd^E>7<6c5PqwoyqAp6e2b-YdF0!p&5+aOW*t!kVrc|g> z?ljE#NyQ`2N?9$Y?h4|e{6%mw55saq4SUyqwrT+sAz+cq+KvK$ldo!|q|Ww;iKmh~ z)P;le+3XmRY|;zWBZ&(DlRRw*C|2|*2iaT?7LS_pd^(mU*){p|gsvM}zn;LTJ3zLu z%nlT`jq*339%qF~WPb#%me{^Cnvi8NmO-a8knc%y<#<{VDI+MSN7d2&TsjtYzU1O3 zf^^8hK=W-^#|r=j56$ZMlG=#i(;R)`GD%&Q%8A`PY#Gx=+DOWWb159 z6yGVVHiNwia3K3Ib?@P|oI~A^$HmKdM}rHCrcEaGJ)XBPKP~O7$jG%}aj9 z`2txcM;A5prr6T=)b`H_&}JI7O=y&U!Xh4ph?(p8j=CVQG-Y~u6pgU_k=;t`^iy&X zL~zBDFN2(#{7`*#Ddq#h=$6-5Oyq3!W8B}*<~vfGQ>k1o=qV%dYe_X;E9f;8j*Bk) zu+xJQpFTH5N*1{d=>9B%GTKBzE=j?676X!e2#gDC@l!a-j!nLxRZS<74ad{4G21hU z71plTE*nI_y6rVXkgL_k(;PV0PpC)aELlA^*0*SCd~6Hpa))|zpWH)+J^2FY>XL5+ zM28RW$PTeLbufT`AzqT8V9lZhi9eU45$rTvQTC+$h2Wf-AvTaRYV;AnLt4S5_&(1! z+pMPGE1Ke})2Kc$oYgN-3OIpFs<9Eo4B{N=+@x*M^n1tPylND;^FSX_Vi>q_ICJxj z?x@eR@Fdz?_S1}g=)vfMk@^YI!kw0yOA-B29DUgfe)MjZwwvRCT0kfgKo7W%g{~S1 z7f&Bip0j?xPB<=$W*9y_aUruIQ>;1{rn*GMDHOr;NMMa&!ssb#q7l1=n8zXr17uDo z8QoOSQ!_&5$Zt=|IeAD@Ew>7`#S{#h3l-PAQIl4&E5%!cVdX z5XF5iRJnV&?5pN4D4pVU!*F(Za4V?P@Rzml2}1-xxI&bp&fyr*$~pz+_l zIht&^K)QZ?6(~YSB{qXj#_pw2y}|QGYyspF;XqqF*Vd?k^fYUxr!+O@6&G_WIt-8i zdIdLl8;syLWo%{+8m%lxSu10SJyF1WzyijQ!4x31n!)jia9&sU_SVH%Z+ZDro|DJA za$a>V#ys^VmUR8c0;6%5QE%gCRaHj3fTxdOb~%-Dp$7yyaqa@sR|qS z&&e2K=?`2@v3oi5hsDt5i3mc-k88o?uVhYCvm(kzwJn)a1HS}nlF?^Plz$Wk@#=vV zk&4x4n8w{d3F9f;s_0ld3J*$BI0o^I?t}5Yj z`tJ+%v`_I5Bc88+c}@~7aeO><_0syeZUjdbc5MN_hDTDBc%eBDyVhZkQ`?;j^SW%(b-q!uX#DUd|?=I{}Zpe3~t;~2= z`c@>X*V{^wHvT4Z-TO9n0PJID@#bQ2INRLT97*b)RXB=Ii(UY{kqseLO2x`m02Szp zL?V{1W?HNDn+!rMqFO|gE!pNqm9vqWO2{54=5m!(ve?p@vo>tM zTm^_h@8xS9>E77()<~I?!OlXwI&4p5w+?lcUCra2IG?DPc(R(Xm*TZ78tRrrJ-ptU zA@EX9v|uE(gUz@kZPby^@vZZJ4Pd&fD;-a#+T(bzZ8gN$STd1Clb&pi zCpKmQ>;kNTsXYu`Jh~&1>anfc$aW3|2}{M+lew1I&vtl7$!p?A?wC@j(}V3WzmDx7 zN-!nGJk-f`MvIEx96@(3@A+$Fk?zbNSYM5j8@s1SC)! z_KF|eU&^$U(>=QjKlc+i6SNQXngXfp{6A7MQXlm*&1<%iO z_EW+0v%G#Mcz%Yn`VR%qPxJR@gXgFC6Ahk^@P|F~IDdlR`BDCSF?fE2KTm__XfXEU zt+}5+e*=GQ{!r*3_5CAQa{l~#L`E)V*mC)kCRrR8{~w}O`SX9ncu|WYQ-`x}L&|vM z#|g{srf3j#U_>+e>=1&2CKmJtU|C^fj{t^?I zvu(_qrlx`JV0DpC{6owjoV^^ZKIYE_5*ju&?fzBroi;Ufv)jJU*$)Nv)j9tDAHnJj z@B3s4y!U?vs}sC%FIXMtUVE@Q z#-Fxe^=?yB3p?JsO--ef80ngtHvA#>Y2N!M82oso71L-_)Aolng7Mw`b?lS;`TN+& zxJg(q!#wabSY?<8t_G_N^T0pDbjz3C$F9bc{|NIY7k?PrIfec%*1o2u)^DSPDx=&FIw!+B@PolB!#lveqttXaEj-Lkd}$fq{vcRoeE0o+ zu*&!rsT1Q{{Kvs+KNo*5SOv~{-*1!Els{bT9xBLv4+3)_F zNT&h={+t2>A}d!+J(fW|Mu~-VWdPms{aNBL0aSotpK(GtL<8?S;lTXzOOTdCuqZ+6 z6!^FN*&5sshm>e*+XDv0J4zF=>w!3OLP?ueB= zsGhl8I<{T)EvSEwbsf@i+4|+Y$2-mYdh!NFus8O$%tZM;t<~tkq`urzRD+I*H#EO0 zm{$%hgX(TTYbPy)UMzpL1DINYgxG#$1`_*eQ(t7nR2kTaK_6_q*RBg=(!M|6K?Tam zpwtdyB`Lm_J0GL36IcmBFYdy;d1>!fDbYAmkvW7*<<;CAPfRZGD0+jsZ9_1DP-0bh zub9%;I&X=s~DCgf#QT+kF%(PvcB zKr||`%1Q3^qd?0VT>Ui6R3wGfTPjdys|T0o0V0B`64pe#{r#AW)U@m`s*;V(79a@F9~PHsvX9#e{yuLG#Aiq>7#M;$+e_n{HjI6=u`Nz*nNQ>N7ll^alX{Sr+=XSMjIQAUKJY<7vr#QGi6t0}O6#&FkT>}fzirKYhzsP4 z%K7urB(}{(hgohfP{^iedTdrf+KUp<*NQ=&bf{}QayyC_!ebD{O?Xk!OE{@Zr|HJo zNX$`5KEYn3es)g|rxr|7+9XM9+>7I(1cT_Lkvf=?_npuvv)eoBUBYMx@Mfom3bcHX zuSgYSbNVKvi*;g(q<$YyBZ5B36*w(f%r1iG|B%7!(dVxTN5g8_#QTI47~HVs87~pb zg5RAq;dLqC-tob*cOiYD^Iw^a$oR`3Luoae0udE6K9p8;9RG7h-Y6!DMB`|mQO-6K z!NtX%&|G-Ol;Zk|8T8p87=OqQe2YnPk|m2#|S% zOHH$V;9)rvicoHAD?H8qJG2Ht~GS%O7mawg-kR3QiAt}+&ezJ==9m!i1Kp`?Ukkv^TZZ34oU~1 zNk3%Vz70n&3hlKNrf$t5luRVY`4<3-2hEDs9I{&9a=j{@&w7 zAMkxAEH~GT1gp;!l7xkifV;pienrrJj(Y!A97Cbf!()FqkaK&2MpvMLLGp2Hs+nCcD@qPGN2qJU1?4 zPco~ns;{9NI&(`onR6V^`pfE>;Z#}$PP6ivM~3?N)`m=uKtTCkY3@JF#n(QkH`>$a zz(e1xkLjp0`B!qulrYhqd!MVt(K=q0a?V>TS?^|r70HKatE#>)nV)f>&kb}&_wq!+ zg0rkSQ|Wb_Mt651nMD^#G6#8PO4A}Tus@Y%F2C?K#y^Osa5{Ya!CF(slJfkRe8eiwwiO{|^6g=+or-Hnb@WWYvgRrN zP*{A%d;-U&`M;C+1h;#?WE=O8_12MC98=_ktklL{;g!|^zzSm#?vj>Xo}vrWj^(35 z?Sr4OVY+#YMo?6XN+jVXKeMUk>VC2TJ`+6OtTEV_Mjr<&wiV?UCFXaR&?Iv~EEbu3 zxKu9MPTwne|)i1 zsc4p*3M9*7WR0VF#@B*HZSmU0wcn#Z!b5A#4)i7oYH)%vRjW3LAso^|jJVhI?w(dI zzJ>Fbpi9NOPjmi;GA4`((;y5CKIr_c`4&2lPlDv+REmtxk?3*8|RozrM;NR z1G<$5db`?@ZY^)fv~(0(TC2HYrBW@l5smh5y2nk$rwl@F1adGE6gHO>zg2t;**JSK`b#x;5H3I zW0XW?f`wq1L1&r4)nT_X6)OQX;s9|dpjZH+BQ8v^8VfLdh_R$Gn*AdGZtnH|E?o6!)dsV}L=1Z!tN(`;;&r$0o3PC|fhU z9?%(&K!gBNXmG$vQ<^z^J6C?_ul_5qRHxc_GTvKcVblPTqHZb)>@cen_$uTr)I9-O z2s!F9l8)L$c|*JQlY)>ASM7yFLPrR>k6e7X%oyaz(9o^{o@qd{Se`(jJV^75Ws}cN z?wA<2EU#y<_|qI$5`ChKn81|CHb1inz!FUC^3K1vw>zU+SQ^fglPmB1n`?eY{b=nX z6$HCLgDJ-spg67>zz!Fb4o-94rrY*m^TBF^9ry2HZkrUbtkBldzU~bW*hfTF3H`KEA6@)&=xo7tXj$ zeZbjRRdjg-xr;=I)9OEXAm$T5Y*UN$2s@va+4HL?pfg3jCkI#&rhmR*?=t|6VSzkaPD$JMS0 z@J;F~_te6~V}^IV4QEkbO&W|54Xv{Y(9+-efiI3AV$8T#`WhMCfu~W&F((^HH8yli z40~29Olg$qQcZgz>l(uyu0b2`?JE7Gu)F|y3R}Sy*A-{n7dgLyncelZRhz*+2kU^m zT61+5A7=^S$LOc;nc^!0|EA!#))_HoJ(FunbH%2;xu-Bc?1jsZiB?;z-RQ5K6o6D8 z`QZ;iyvTyNe|zmDKuL?Wle1I8aXSwt1ncQE1HGULIXA)62M-MJG`Y+Nx7S7#gbUal ztpJ>hd;1Rl&O5rfmz%dVh@;cBbF+`9#<_W5aKBzWaEM8KQVHhI|Kfi?6=s5{^|5RW zv21udsisk_k?gj=c40zrk}7y`Q12c*FtifPZi?(Pg1k}Fe`sK6c=y15{@onFiSoeV zq2d0a!9#;X2baIJV|QD#o_PVg>qia-&-Z{&g&)r}yv+5AlgSns$#j=sId1)`z+bP$E?ECe`g`(p*3Wd3Pupby&M%WeymN zJR(?J^OhNv{hmNr2UkLXA?%n;ZYW16O0SPaqik)oNt%So7|vHHYs|4ai^hY8tS|85 z6-?Ng>)miP`H-Ffp^zseE0agYba1AWy({f+aPmV^%eW_|OnH)xCgo`2V)(?REo~Hk zIIcX5_|G@o`rZ~>E^KC1^d*e!GKni1qdjH5X*OC&1Tb1?yY$~DQfURpOe4SFUk;WZ zcGjuEhT<+U!51G&qD$orqIf^tm-83Xr_(v^@9PlfS;os!vF_?33(GJG<3T27=)GdD zCrS7xS0dxzHo!BIF5PKQP?ORP^2qEhw8qJwII%#F@8q4s8@!B>tQY-?o+gCttez7W z{7QmeBKj$mAA6I;5{48y9QXpbs&_36)JFHHIODDIf^oGi#G_>JMog1fwsb<=)(jc<+bxmY3nndFl24!komb%aZInmwpoJ$??3J!oT z1dWAJpr$AxF~s}R=p+@{og}>%AOaAB&_7foX9g4t=(dC-9jNywG~?9~17hV*3Mko& zr7jk_uV}rJBC3JP=UV5xtVJ4)cYT6Wq)IX^K#esgiBH4tylH}QGTvEMBF*|mypOmo zADxd-{W}%V(i@wNMfbe~WET>MvgLDIaZn|cEtP5$HbHaya3xi?Qg6rs%~s7(KRynE zxhB;n3VhQ=W?3^zM7rSfZT_}4gn6O7Xa=c$DBVzUN?ouWx0cCqO$^KA=DeA-%0d2- zR^O>0N>WeCM^oy_o1rh{>NEPcFF2Nrs;y_Wf|pvhn0K5}oH@-ph{ZVEPB>M!MNPB2 zlN&co8K4v&fHF7r`&cYZ2+jQo#g0&232dMXgJeM$n}TFJ(Htl`;i|7u%ljQe44pFL&9CbQRXZdb_P>97~jdfKT(zb)q$otOyZpNH! z)Qu1=0MB_sDkNYnj(kS{|9D%g%mlSVo6_Ct$Cu@v-8TH1Ao)WfPy>mhBz=@v8TpC- z%B!qg(IHDt## zQQ))eRX(HA$o0lKpI;S;I&Z{$zX}P==Ce8Qv9l5X1a6;O!a}$*MU37)Bw~i9d7Skv z4bZicp-Ls?F{nB6tOE!kp@%v{#O9W>fIJxFX-K#6{nwtPIc(DKF)}QTG8feYOw2i@ zFl=l@<5G$@Jl`J5citAKoJI5X3CngIpnhTp343cR$EQq_zKx>~F}s4Lth#84^hhHi zdTP`Da-K`5eL})6z0i%Uh*PgGC6$ejQTu!{%tRs5dtD)`*14kfX!r0g6IQd^D|ZS` zCmXc3OCi*8GX~Y$QmvgMNomU2v8=^gpwSC1e~QLW{r8$}1-C4XihB79Z3QZnx@rr) zW<g>zb;ZnAH7n|1Kbnr+~X9xZ`H zA+$1E&Ekm`Vo4~R&NWxmz>^ARcofDW5L|{%W^(2+U)!k3bCnLB1V)xQyPH!C&$8m_ z)YOm37}-oY(Rl3|-|Ur$okc~2HNm+CjD`l7;Ej}GK@6)loFyls*e|KUl9PuI=mxdB2lv!RParS! zx9yXgoJYG&rn6%0-olq!2y~B>65noer_dwukd(aFQw zI3pd+gt_P6q^8I71>SilwHc-HM@fa{C88}+*!5^=KO4~$>>x{~Deg6J0Q(qCDf0Sl z97w5#G~_$yKvxlGYVyC4+~o>D9gFinu{@&Oj_P zQAs{#$5b}KQmG9+WuZ`P&SvTr;`(zW{wp;Xz~abeue4<|*(`pm&G|y5InyS16`t;B zt`s&DdU{HkLOGWyZB0{5E=?$4Zi5{9auxCel(<=JEu;NR=e8AR04KKThiaC@hD|2rZ{OZa-n7`pSql1$^XmMBV?&NahM}DPcIrnxV zWl+^?(GZ4RYhMGWSP;iLMiVkNIY0JzQi?>rV9@3-erBw}>Fu(29uRg2BzlNx-tX!g z*52^T4R9EFMJUHFIjxGRTgB-Lq#B~2`~*|%ms&bChz?Xh>LOKX8f0!1Cig(lUViJf zbVq$&sx?9JBbDntvjt8A&%ZEvABI6t$LQeD|Dzn`i_`>F!5&_39Iw?id{mm<21fRR zP@eBfEjo{$cxJad>qldvFXH3yBq^2cEX`Ry(f${!SI~x0O<6_fO+|VVS_m4jX#-yz zM`?6m~rCOUw2j-fr(lP`lf{U5vT%9D~fjZ zb@wCrT-4?tEIxXG?i;Y`DfF*0zI-4gWHMMx08ENf^?RH7J$GcbM|X=jCuN&G{Mk!u z-4f2?;(F(~E6ZR1iQj8Ugm+iI^jH3sR{@yM&EVyC|BK(PF8}`Wx#Fdlr>7qSRU>t* z8vQ-h2wz_>8|MLeK)7nH)gip<2B-G{;MC*uL`S2ESK2NE+_uhb4B1NUr~j4LGT2`` z&11D|3yUaht&e~k*Od{ps;K*9SFT-wNd)s{Om$cu?Rvf44-eYTvAmR3U=1MMg*X{D z{G64k&eQS+8(N=mr%YUT8b(CzTK=tPzuvO)?qB~+&k>&G*~ymHywl_z>_0d#GZ!?yC>!^=POH=8?`e`ex(W_i;eeQT#TIrs>7CwyUl;A51L&u|ND)e;(q@ z=S5QKs?*EA{YyXFvi!?`_^p!9)#cy$!*9JZqHa?SHEz&XIO~2H8-SLZ=DX_LHDlUm zKDhS1<$;fTs~I}W(Xg5O%isJn`O5N7@BgvXCYhSxz%{D+hG@n;tr@sDxBJYDFMsLL zueL8YU+phr_Bw?!Uo?-5AXWi&AYCxe&MfRG*^p{(wlTt}f@ZcYteua%eEP;(*YA=M zQu4BLf`s~P+d=>Az5k{AwYA6Cb7yK708y_E4GbLGMZ@uDk$54?0nnATs|tK#bCRV8 zJ`N&7N+In!>`<5-PJvp_)ZSIQ+<&@%d9-ltrH$(|{rfG#ou;Wj(7%5#_z25C|Kk%a zFTC`9S9xy0*dIU9l==&P0{-VaUiXi-5`19%&!4HUCGJ=^_pWU0==EBc?|l1@cR7=< zcBYjt{;9m*vix`Vk7nvR7fBN_69GQe*tt-$8RXu=v`FRpb?w{|e6>|#!Kj^^k`oU) zO=mFHEW0-gf|EVL#?Cl0e{9LzW!tWeVja5+{nbPmomsi|@7w(3%3HU;?qzoDstF+~ zER6CrFD29C5Qd?K_4#WAJ`?6wBRhlX0SNR2%+^9<9dN>tr8Pq17Tr)5>v z(jk3%jj2FlLRR)#Lsmw9_@8>sbudzq=%F{HZ4ffu1T*J*FWDzXKC=huGZ*J4?(zk_ zr1|?o3YkV5X9NvU`(heQ*~i(`N#gQmyW3kBg=dK{h{j1jyS@{%D^v5 z2+p`T8H~^v%qB(T`fw3rycTL#MoznhdzOPCmrltgz@@3nwbd)tmDzt#@e3;>fBKT& zwY5Qc#lg|@;H|i{nJc?7q8n0xr*d$uEH`I@TKeKtEayjN$gS$*wd^E;Z(%4LTSWk z|Cr^J=BA9JlQSz{|BZIPy=;;N10wd>ZFDPpR)5vo(9GbBkIpN3P1qMqo#h|+yI$M> z&yyv;@@Gd*j<*)y$*9vUR-u?YU!$SuL516@grCS87$B+NW>%sG5j?hKE zKcV|t->DY~-8cXI_a$^U8onsbO+a*SefTsCea2~od$R^meM%oU#&}nF0b8Yde!kX= z^VI_X2YXYwSqM`H6~7moGUJIso?U->!i1>LJm9FMNQ%gik)|U`e#Wdeyb0FO6HO!K z`!V^k!S%|5t_e6T1m?$N?_esa5l>W(n@9IXCq>`p35uwXljDc_V9lRrLzYGd$0Ej4$=pZmep(-q~U6&of zmlKh;b8_Qgy7J>p4QTutjm*w{v{IO#Zd%?MyZ4rYwQH;teRv$!wWJsa=^7P?dd@{i(+kTv#UNWJEFqqLRI>UX@3^K6{3gJ2%f0}}hg`G9*? zDEYHfED(XscDS&Xj)`7T*G`N}m~sQW@)HmCc-8CH34IF_;jD7X1L~ywc5A7v=xH}| z^|Z-&y?o*x=(d`#y|&6+60F&o-sSIp`%p_Ab28ciR;H$b zN@e_=Y$`DY2^L_kC=C^L4L2rD&Bk>xDKAVrEwQ!Fxr)~BOQ8Z|s@zPh^U2+A!-Zj` z-^l$4DX@xBDznDshD{(os^JRd7+d@5hS@2GO!+YB0EoOQu+~EO2YbO#@xpHFCX1D7 zg5oITn5->Y#P;!(pZxuQ=^a=uUPz^*`tHhqip(y5w>yp6GyVrn@jv*}&WXyjfird-%;jPltZ)qizdXN+Jp+RJ$7tsxrkBc7haCY>O7di0lO5|q+Bo~-s zd7BqGs4KF4?(n^XJUGH3idCFgbo9vc4-M>h$LIXIxA%ZM24-b=pS?+0*`8=*f1{Yo zzIPxjX2KPtuYn>nL?v`c?grINhhY9&^>ti}MkxC<-#iqJ910)k@%_O;wA{K(zJoeJ z!#d=9DvhJFeA!(i`^ymJ3MHf*iSD(2!4Et#Z3qN98jSe+5AqHBba%u%I2;}mR&}WH z#f=en%=2$VBBN^67OLl2N*|zPIgZw3Fs*Fek*FxA2SBg!`0n&zS94LP`D{8-jkoMc zmWi0Bg6-Mn_8#5HDh_9bkj-hKLp@j^NQ0moW7Hep}o~IBw&?`bK%+jEN(O5@dLaYh-f*f34r-igiwlkmAw;qB((b)IKmyB&JN3#4PFuB zB%&a8zL)f7k8g>8j&r;>CPUCsKRb)s6OTy}FE{EpiETn&*o~IH=RTmf?$r!i5uM9WC!)s9&V^y24TksldY&_WZK`5*cz7y*Qg`;99fd3b%X@vPP7bC$B?G(BA@l>Df(U8-^K z;LBppqi%dY_9NKXMN8g_@H3+y0tT>~2IjP|S%Id-&M3;&&$J%^e|UFWDjL70nD>MM z)BwE&@C+P>8}PU3R=Mfeyd^MWfuM;4l)f*B>PsKUs1?%@IWq9)aQO~w0;<$hJgcF` zA2BSZ<{RyC?v3cKL>iO2MYTUUC593=v$SFmaL2tE|zKf;=vA@+ym;d)Ci z#EAVt&4NdC_U;iP=uQ42OxT~=^MBJGnYFnlP9^~{oGSuIlJm`A3jgb~_uJsH8O zHbPs24IrWk-U?paX01M$_LC5;NoCYE+Vm&mKND_kf3euql>EROfW+UXoHL$3V8`aU zMD7bn_-&Oy042MW9=YIqgV6rl`qn1wY33s)W#7ye|5UnBt zPt~GBd0UWsSs}{W zvzSt4;k1HC(;=5~&O8QEp!}9R@HXjXf?||thC1@zTqbbCf9A$#4qy6tlBqtGYQgcb6 z2kyyxK3NFi(Uj>!Z=Uq9%0naF8KCNuXj0G^uDvh~wjb*J#m4Bo>?O$=IFFeEp9VED znP4oib3vHGn)XKP31my8|M0@=ehPmW*uqCP$b9xgFTZ*a21V8VMrBI0W^r!zzRc2U&5W19I)oEDdi0sbz~BRUU;ZXGA}qZH z`Xj8^ZE`Lm2Z%W7^;tiGbp%^zcuo!-GQxy?b3iVwjV2OIJx{9XM!i66KwoR5S>@cQ zd*1zUP;Yt}B9O+|0i->$?|95`G?6mqSRK{WO9b$1cIh}1iM!wf&Y2}|BvPp=D+an1 zK9KfOaQd{ujkey|&#p4zW(Nze4oCnofH(lz2P5YJNNcp?7ztfmIrBM>I5JJxa9&SF zy!&C(Pve>b(NVXFXC`FGBXfgN-*Ux^gKLat(iNV-b4s*KEsxVLqYp?7p%LQzK_vEI zf&dzKHsHl3acK!Fwb6^u&LL@r!;cpLK$XT*=*_uEdM)3)o=_t}{IX~sSDNRg7BpDv zbM?(g^1V^HC)ee;qgQtKMpCRP#toa4du^BJoP=+C9w-BIlXnM)!s0=JTU161x6bv! zeXzyh&5d4KI*S)4EMcPI#-U*f+B2Cn!-PZ!xP;aBEIEVLM);Hmr>9tIweBfBzrdP! z#4dLm?l*{+Go(o{hj4o}g7=T9QQY&}B58E^xVE^Ymnx#mOOfOYeZQLoTq#DpSs0Vs zWncSGQYCs(MZj>4LG)_}^O4*f3wIH-EVk#y0(nIYAKJIZ`6Dk4DU~(?O}hKOWx(T5 zol^A@EE0UU!VU$&QNhmEu0Ah?JIMr@=@%LlXS0{3bb^?~fH&TG7L7k5#Idms4|{RE zk=KT3f207ph2mprk!{)D(x*>EoY$k;f6gPQnJ{2f24O|6$n^^T1^!PDye}^(S7qQW zoRfsrl7Ua4c$yh+)TYHxkmnmmAdwjoqQxMjRyBR|0FGstme!YAzn8(HLR*9u8-Ds- zvGI)--vQiZZWclwQZ06YM`S>UGPzEA93}Q#B{s+y*^p$L=PvW;)F}qeD?Of?;|mkw z2iLlQMqQ6kmdxwwa8`PS%``rFe|;l-%fkV$F3oF$#E(QkB9vi~H#F4}ZemP+F#41$ zYT{5Nj!zI7kvQiYuM+j|KETOKtXX`2!>T`tWS`C2A_#e8Jx@9;0J(GNTq%QdO*Wk^ z)C-kTshG}Yx{8H#1_P5rdUtxkOwbKgH%8o-{c;dos>^~L*yXJRLc1rxZi~eFSRIn5`lb4Wzuc6)nQhB_E%V0-qIG_4_>RhUr{I!C=()YDn z{+nO@VSaO2&zoER`pexfE&sni+>-t3Z~n$Df3vsz%IVf^%h&$J!C3p6!R5}~#XEDr zL`sb^JJVcR{^nS6)ACPz%Zsl3z_+ja@s?5LQ(O3+#}dmwd9c`Pk6C#+bBnoS(FB!0 zSo!&1yX9|P`Pv`e@~dC{?r+}mr}&VdF3hXYK{=li_B-<9m@^pO9lq~-U%zjt4r z_kEw``!sZ8Bz_uKy8@v;%uhDF>yB?RCeb}MVSbB(w$Rj?L{a07=cRE-X+mSb*73E~ zEXlWzukV3=ocZC^?GX@|HmDL^_9V0N~&LI#AMxZiQlXTl>3rdP6mLE)Z zVAUnng-Ac1Lk=RIp|O}@=RJZOfzZw8!f|~Qa~wI;sCq}% zMXc#OHCMQma%@l;>{K_}yBAl#{PVx#wIuo~H)fy+Xi)I8wcvP*I;GhXw8=#eIYzX! zxcus98p>3tL#>r9E}-!;#b;k!E3{>^$$&Jo!AP47bWt}VU!vNy`nUe-e+*@6Yce*5 z! zruvx8=f|=!N6(ET{PdvSH=N{j63L)AxYbIheeA5D5r#Nf=Es#T&L#fQR+xpA42%0b zL3CndGuIgYfMFYq_R6u{-`ZBgo>q&_EntR4WbqMN`pl)6#4Ou2H8M?#6FBxZwjmJg zj^QjLXr=}l;W*N;@>vi|qfXLgpfnu0$x611`vSUW+yk*)?yeGxCBCNNV;l6%OeL-Wtdm|FSfkBx3z z`C@c7yGJA~*b&EU*))iT$+*loRie0KE7$fMEw8pjeqGU1)x`f}`iT%pS`e&KB#9De$peBE189XWfI)3=noT(khkxA}LkE17 zB1!3XNNNKavBI>};b9^Dpms^ZO_>v_k=wm9+&*Zg_oFO-uA?XqQjszQ8Vg3`{S(2B z)YR7|6J zD!T2>_(*C)TmeBCZFa4LL9|@gY`Nh<1dt3|mChAV1 zul#m-<-1=zetqRzzjnEKCA3;>kM~t>(Yf)}f#}C*t<^smxwrD&4@L$us9iQz&&t={ z`unYUn?<#0nkk%}{FzL(dF6}y{@#D9h@b~kPP&)DtSL2n}!#_Tn z?a6M-wtynBA@c{B?`FQ8`JK!^%6u*J%b8!ud^z(onJ;F(kXg#y&%B#?EpsvRO6E{z zZ>9pmL^`t}{U6fbO@Al-JL%s_|9bkD)4!1Za{8y!Kau`IdMW)NT}|IgUrfJ}KA7I~ zbCtc}*6g#?pHF=$^<$|IQuC>apF6oXymR#*eeM79GPN7YSChw+gUQ{=O`rnD68|~z zZxX+k_}>%XO#DXTR}+6N@fQ<6oA@a4V~Niu783UopGn+ITu7Wq97uF0wkDbq$@ur< ze-Qs}{5$dAiT_so*W zjeI-uPb2>j4XD5B)#CM!$HE($qV<1QlB zqS$vVxJkjcEqGnQw=8%`!8a{D zyJ^9<6??;imf-qY@Y-5%#DcFX?Ntk2Rq)DM>}3nyAh!1LrM2jb1S9o?5?>$~u3JCO zThMBL)q>XGa~8Cwoh2BpzoKksENBT%6O7b%X#7qweyPj)e$pcMD>!VynvL}<7RHkd z{P?xt%NDe9kFUkPWI-FLV+5o1E2`qCrf8c&M+ilm6*{cACn|J^gkjghLj==xd{kgm zM6edFpH}#Q6;)7hzXj6@4qDJgdVpXA*W$$XTkwK{`__Ve7Cf(tdsXpXeeWSM?sDz5 z@8=Y|hhVgRQb}vwYAyyr*uoQvcj^1?wePzWS=HyAgkpOY+Mz5~{B}!dBim^~o9Jy8 zv{qLvXp3~~T7oSW{EVuqZMN`PmAgrGwJElP$awu#MQ$WA@)?EN6|()%<{Cg;t3sBg zg)CvWmYc1}i^|i)_t>zCEL)__e2HMfO+m3{(N=vy<&P>?o=`lbP_7ZmHbR+3DBTF9 z8lhw(lxT$FE<`J0R-Mgl)Pgl@T!e7==>fGfY(X1G&w@74A%d}|870_Y!Mg;XsqwL= zTAPu7CVR>X%I!DsJVv>Ng3u?5Ezd}P5{1(y{3 zaI=CBE%uRuix!+#aKVBfDEOWQs|wC5_~AYU=PXu}@NCv%5t0+0v1rkxXVYtmA6V=y z#oo8z=M|i?1hAigXtvl%1t%?N9ldJ_-c#&^1xpH!TX466BDb**w<|aru4x3{Rk*6? zy0+^x=q)L-EP!Wsn7SCe8-Se^`Lshp(c9REVFg8RV;|-f6upf-wE{$MV;_pNJQKb3 z(~92u2}EvV9}ar)8u-r^y-kTlZ(~p2R8aIb_S8mL^fvZki(*A@V;@>0L~mnHrxYuC z8+)oX^Gx*C&n9{sd%B=rKyTePcqVEauJqDGIVy{TZ~@Xd*!o+h~1*VnuA-N%Ks!Hd?nea3Z{+ zM!2FBBDPWav;e1Cg^6Z76Ric}QIXKvQuMGQA+QCr-O)Sgi+q}GoVrS(gN(w3sOT19BpD2js666{t`ls0OV z_L(Scv~Gh1r7cCQEznt?em{fI@*N1i`m^2azf$y|3V_l=^K>vggVeGVPb-0FZDflg zMQbC}MI^Mg6d6#YNNu=odtIc~4{o)fElQEvuxp_xttcb~h|p2W6NIT%AaDK#HskG^6N@p&%) z+(YXh>-REnBr<|LMtCDQiQ+Et${@y65$uRI`R6o2Q-|^zbjxHlBzKvTMYZ* zq&T0*WnEKiDsu;hQrdLbyGA2?XOax`kvr~q`^6dn0)!?Z6PUeJ)M+$(}4 zP44POMve$h+A1%byGZ+3MeKv-7NwA=-q+-Cd6nqA7oL$0i3a%qUffLfq#xLTPEXh7 z9=n;oi8M#8kbpiMrFY?ZP!cKd74nQG0D^hhQxn3T(!yL%#K`-K;3 zWG9-$nygbVZrRx%jX3oTt*B!{jM2m>#cSc344N5hecFmkN%6|nh0*}7zHP+>dQ+Wg zgS?auM&H4gzX$`QXX(_h~Af?z*`aiv_>doa}kjm|KQeadO9cvS1`_Q&h!jw zq4rzH)$Z+m%GN2xhMo0@!Vi*G;c){rPuhJl`6ti#FIQyvv$dFH_D8MTR>Sv zG~$9t$Bq;lz`YK;Q{$ckwt^j{m6lJ}ge6ei9NiQTF$${71Jl^rDntul<)_31&<^C= ztef!TDseO7^1$|hMNhk9nF{j@i-dxd;y6Gf;}SL~>!L6a#}QMrnruotSiIGTNUSvx zrvT*!heW}*QOH=Dck6wpEox=o88KvSwIA0ytTf~h8j5UGevaKfU z_fpFk?(<{^IM0>Yok*bMfGk&Xij!DYhw4osO!l?Mq!uw0)<#m<$22cDqNdN)?h)>M z)%9OP*Q}XpelIDT;xc;__Lbl5P9eesvwhAM?l5Tq5Jq4%$<`5h>U024M

YS&i0S z!!?**h9~QHXIx87h3zJx%&tSNNSnkDaHI7uqxFEA)$%RT2pn1UiXYd*&ItS@Rkzit zf()j}w1eR@8LGN?*f!JAxXkSj#BH=S2RAjU@2LAaGnQqV!oED9UvHEo9zUT9VWvqROGk+-KQ>FCL+-6Q*y=DrY{%LAKQr0KUgo;-RK&ygS= z6!VuuO{fv|rgPM7Xpfqw~x~Ewrap0rVCE_~|p%xu!f|8}OwtYI^Xc+*};+9Ff`q zPDwO(tg^GUqB6od3Br|nQA;4&FE!Bo#+QbgH0kwNyHVHToQxbxz^Cv?Qc*RiKVSYrQ2Q@oz_;Du^75F5xE$Xt>OU%wa#>P>Cdo8)o$_umG zz(XR;ZQC`rBiGe>++dnmp4*Ld&n3`R@xut=v4e7B{gQfk#Ea<4KQ7+_Hw3L5>Z{|Y z?RiTXH_n@5F~@v&6da5=QAzcvH5|rj&5bf%5PbC%n^U$Di7c3vQY*J+|9l|dwHl`} z%@{L~b2Z~)I3;hvBtrem4bqH`cM4ZUHzKJu!IYc2I^1J!V;X>zXzv#JL~qk-FBQ0avT_V}GQU!}ey%ApghLn)Lvsqbed~(%D_5IRH{p6DrcyGW#1hDo2ez z;b(#>Y#O=F8=YinS?(kL86h%%<3ThQXmy;Vu-ZlL{-fMSsOmW6s=XC@CHfSJ?-aqA z+NvML<=v&~fdbtatV?J{=n!QA7;2b{**9VewZXm)RIf~P$)xAZ1Gu)1x=d6ctQ zfpXKGTHScbz@}=};)7xQlb|T$UphWOpBF*PC})d5PzMrRIxu(*NJ4)s*)aO>kAocz z-_&YPcgmA?mzL;ZP0BvJbaU-myBKVarKA^MgA%w%5`7Q{(+XoHH?C}FM$`_HE|%1^ z9ejEMJc%a4=|w%i7&g1&YJGbgYn-rik(XjpISLU=~h z!~I5ul|1M8oE!Q+MH-Es@A}W z9)*^49-NtMDYLhP=x>U|(+Dgr@=TgnB`9iHsq4Hr@EaSGWoNwKlyRk2WCJX>F#cib$xr-p#pgjY^ z4Z1V{d6!aq2;#vWpN#-+)0S4+M8U-}&hB!BEC@L*=|VQYJJW(A-C6xAKQ^W92LfAk%~pQt{`sce616#Ll#4~0>p%`}O`$bqx@G8p^{n=1{)yLC z3-lMRFHKHjz&lr&5SUCKcI^WP`zn`As^!X2F_#?045arcuL_e!FxFU?&N@`>Q}?8_ z%89qM_+(va1EVIp8_`o6cOZb109t&nw#=3SKNaC0FP`Tsw1%Hsd%IXgRoNZ<@QSc~ zya!U83=_q(2u4B8G&$q2aKjfRZ5^JixnN}%_I{vI$ee%3M2V+;ku0YDunmMpzJN^% zt*%PYXvXbm8!o>1Sw!5|K_SQbuT`lK`evgpXLWi8$Y;!eQBZZ{|I<0guyD3~S2e+) zJd?+=_=Qy(?L6g7c-Ob^#?ojYSq@sF9-z2w714>~H3#Mm!nB=A>l-3H8r6AOO397Q z?nn9v*Pn{_%L%#)1c2)+Duy#t!fCas4@T*DrRMi*?R$__7~+lAuXS#HH#sLP)f^v$0;wf%`1v2tvrgF1pLT;;r1(b5ho zs#(ijk?X#{nDr*N=((l$0kQc34IHs0yeMsV_=T+Tb;bENouF~rOQ@!=C8}LE`&>Z_ zx{-8wgZf@<$7|D%eozz6H=f*nMOUXEa=}K;llrACY4;lc8{;Xq5JuM^A%G0iXz**( zbAnsI5^Y@+53a^9S_NNae(s*!mN#OVKP@|Vvio(Mt^)Q${JLZ(fqQPWq_JMW3-H&( zrw8_wJdvQgJ}pmH>*{mS&sRtx)tO};PugP7C7zx`1^9U?Vq*>fKX;Kg8{N1%F)n5P z^*sZHU0@MB+SiqM6C7RqCivZD**7Q<#_=)|W{DV)T&aJ*KD6?M^rqwvJFn(MO+F1& zzW;FFk;D5B_pf~N&66z&ch1c%tbXsrpYxi(8XI{%{Qv$WMl}CozFAa=*^(^=8(QP(9kziyem~U;Ccvys(|Vr%92yfMbCo&=Xp7 zAKNkfA<%#Gd~p|`QfWMClzE6$s^c{wo!aO=HPX}=hp!id3ykR$>e5uNc%vAGTwf#5jh)R4xT&Q&mQX!`Mp1Vcig zSEk>{2FIWdEihe%*2cy4(1sEe6eoRBi~OZ)DsrQ8$bib2UqX)o7z7#NQPe(F8P-&; zGJo0pAteUMvt(#%VL z;FB!_?wkM^j#XDaIlTSQ%KUORIq-)Nofiq>p`!;6_Z>QPWZ=N+w|?C z*1L1~@d6qf#oP7J*5NgXJAh_w(@0|Y`ufMoH8qBxp>6QBZ z^Q{7gg-pBDrc%3j{>2!`4>y1Mjz%(9cja}nW9~zIQnrY-3(GEWnWJ$E6ehW6E058{ zYULr2ZA&cNGq&4TQ@{N$ywr%i%e>GI5ri0I?4!7qFnbVCSSW~Ni z;m4M7H8;s~!)fNPeCJPP$_H;OV|iaWDK{?>B13-u%xu^{E z9~fBqlX9 zT+w!W^?rE%Q?FjbHknvkvuPKxwp#rN8_$*R{kxaT9WI3%;2vJG>#!MDE4TiY*L2dM zve*Iy#0JG>3DGAwIs|Ppfx}1pDgE0CtR|q7Zmmwu`mUpZM=IX?-B3$dTaCQM;~4dAKS66=|5n=_V*nc7(BH4$=7#>Td%Hl z`?;a|Q5?aym8R zPmE&F@({Yg74(wdxF6C9yyqO+f24cm*W04)E2}q#60Mf_;oZf)v9ZyGz9o7Jc+y7dEmY0f4FE5>c7I#)KTI)Z?*Ss*?63eQ)U$XSM6Vn})iQZynRm=2G2;ev4@~ zBs?`Iqrc;)t*PdZ+n~GqWMT|UyFvwsr=ig^~HD^RYrS;vwsGq56bXUpa6l zUWtb`Vy~JmD@DHE)M@U0Q(Nmd!dT^}cEiYQ&%Al|Q?o2rmYuO!Z26Lts z%4H+*!R(IK&B>x_F{BCe%CS)mO-GyJnPeGf*debymWZcf(QLFBFE*oYLF%Fv8O^7P zdlGvJ(QG-?LY{as4Kg?q;vS?>@l>%Xnamb49SEeNF<|=JLUeCaEK`c-6Sd}iHoJX` zV$vpluGGHycg?xc3wu(iO)9` zG&NhcsX3WqI<=`STZl#rNj1mIMxzOM!>-JZ?eScDELuuzZ)zuNE#wu_lG3)9#xfnD zHVNU+Y|NKREt!lm$4mXObQ^vjRZR{*)C{J#Gn0Qi7Sita@OrU5nohLFKu?H+?+}ed zM>&|F6rbhu)0ZROlzB@%#bCt+Nnb%MfTn}iWcSsC@G@>LNSUTh(vgiCQ}YO9!axvz zkX8d=#I_Z#|Esv+0=g#4pUaUD`$F5m^0a8lmg=;HW)3&CBkdnYGfm`1g)g9R14&Tu z61pL5ubl+jW0AWx&P#s}Ma>l|3U0Q7uan@UI$e+M&=xqHmP%B;PtANuUAQBSjosVz z`%WawwG31Skv-_R?_me{40AyGCP{2B-BG@RmhrH9cI|RF23`v$#WX;PhiO>2--?`BOXxzhel(ql@Q-%^+ya^O@@HCO?`7?8 zxu!09`I7yzZDy77S+!WBjw)!N{jNQ)suv!PlwiO5KCXr}YCg?cF!vpYv^bmhX^iSe zBjF`!-3;glzzx_o1EcE>6P%%%lLKpXvgt z>qwhD!rAUk5)K~~IqHb_#!l{2s21NFJ=T*CLu$Iy>3c~AjI?9fgr+*Ga8q+lWn57B zVrrL)I=$_>wrtC(ZTq^lNfVJ{JKB=b?McOMZ`%5rxzgIKY!9>{61Q)vm0P7vvE}Nn z{Yq9&bX_fm3hcjnD&JhniP&Y^5H9sIhHQ0Zz-h^-u07649LfgcRmR1pu{mshmUbmj z+u?A~U(RS$Sfov(bNfO##z}_!&-s?GzbqUa9TR)_h=3XcvMPsXO-@$Wc2W zkY3L&R&jWUV1UBII{%(lVj0w=ouz zG9sA*FE}HDK%*_ftIMbc0dasYB|2^c zT}_!r871S&FIJ#88`9}xTL($HUtMTP>0}K+B&Tw9P``18 z#;j~3xNAo^2{(LB3X71657dvncst~2>f9BPHg0`?AIBxSqEY%(I!PATbZFr;A{PK% zfHQ0giyKHZmzF-6%}ZajmM{QRyK-4;Z{w()H4n(YGFZL!>-ajl$M9LIh*}bcL{zcG zIDjf>Jmvl?@K2K;P8~}}nQMF$*#Zkk!;{m&55CMV%g?>0xmIptqxhR)FRcS(P~=8* z=zJtTi_!@i&c5q6PJBV~l%y^^f2~^zo#OwSjw0eX=>X zHJ)jSgFeVMx9#xp22D@>1`c@Uv7u3TL6_Du#cY1dPMhhn7oMCSU3&x^^5m`$dKqfJ z7t81DU?~B?W0#(f@c|dQwm0UbP)0RYjnL~X&C7BQvq|aY#fL$!3zKGiJJ4z ze%=eAa4i2wpOx0uE_=<{d0Izaq%^9p za!U#&PjA~*YRl>bEp0BoThg(aI(;JFme1+#-I^@qa_KGU%*JFk($td9@f69Rx`9H* zHULrDP}HaN?{`~D5d%oswZe@pB*r`A9 z*8l9o5dQSh4I83yuOHQ+ci1q;ik>GV+;`Y4hdl2fuz(6)2O#$dK(Y#VV@cscr#(Rk zDy~12VGrY(v^F;?Nw15&<$2N^Q-Y+!gj5iyT6VQUSHe2Q-+?T(cc(G+ft&7r*0b?& z9C??!RVXP>OFS}EWuKt*>2sSCAxq3%E_Rih(Bw3VY1~DX_$|X^RA{?V28H%{37lu) zZ(X!h5v^Y0Q57IIVq8Qal;oz&rN}r!O7a8_mvlW924!j*v7OPacc2`D+#{2K^ueol z4RgH~FYF%hV1b^xvcguHHB5C^QUXY=AQxREl5szPCbIKDBEFY$?Fl6XeL1Qdo{QNG zUa3xgI}Vg&V>rLKG!47BA)ZGQP9JWEGMG}V!>uDyxOEO`}Jj=FC^o&*t{xPE&z=M~|y`Pi^Opcs!m?U?G4O z1dG89s4MGjr^u`R<^VTy1{A7fJ|th#HnSZl_@?fQuZC`>%wF_;Yba_yH{7p`mllUm z%b_uTC%Qt|f-TAt=ADfmI+{I~Xh$rbh}+FXg)D~hV99XrdZAVCB%;!8@T>Yv#@?vP zuqBZ&Ucji-gcWfIAYdSO+>dvG@iX;KHyC_=FPsKDmCLJCZyQTFQVeBhsq}>gpW5l= zal`?7&-@ZH*0oIojGu7e-q{Gwbz~vt_ac-;uK^t+gYeS;%Hnci&Rl}q0-B4OkLsHE zkZS8D=bl=@e2A+DS8&m)9bL)-r0l#essr3P^H~PlplMJ`3VZ}m*GJ# ztwpEFZS3^dL%a;DEE(H>O_4Nn`}_pGy3K7x7EP*sV><3wI4ZsmKf$(u{ei8T;JXR30aL{7`z^y@&xtr?TRO&wRloGy#574#a|0$aIr>#i@uGG z7V_1WWGD=dh${q;u83g#UFkc7B$`R3nn46aS+tnJ$6&Eok{V{drC2JqHJ4iCudo>n z(sHi3HPwcuX|~kT+SXhy)X>jNcck)7*=9L9EM^LY*6c@D|E5oE|3c@64e@^z?ME^O z6e|okAmJit4DNS7E*My=qW2nB>)RP78VofD{Hpjv;IopJo_7`vomG+d4GUI@muu_drSp$4k2_{K(Zb-qDBWn~!XgfUebY@>)^a|S z^+|=(gYxSSaSE`DC?k#W~m(WuK z!~hS*%TeGwC%C&J`_OxymF>l}^t?YM0aVo4~(4iWs;#|D_ z1@uyqdEs!5$(xhI9)k&27d6%ULNGt1`R5n62)r}<+kJfrLuOa4#*dD74{zJHHxzeA zf$H;OUW8>L`m5qvlc3?w;dBCS5-~LIK{&Q7cAq~SA7JBHm1VKMy&p~k1&Ih90xtTc z5{_;Or6BMK)g9EO(#>OQqKC9KIL)|oSg)(%Nj$kwTQ@=K7DnuIa}V76S%VU*Zwd~c zw^{p}vhQ{zcJeatTapaL5uN%IOpOy*5IH}XLA6ct7!H%j#t8<0yqL@m7s?%p_C$hH zujUujCqpX(n6$=(&!YB*(kN-Mq6Fp{lzs#6wR*p)sr4LougvwMsy_?Z zVLI^Bw?)Eb)?&%vV?b_4(L2NyP%RkXZJ`+RR~7QFhHi&3WmNGoEISO@(0#}N7dlNw z%o4;k3ZK}5!)qV;)OrB`Iu1D9$2zuBHL%V!1RDESLf-5k zVXD81DF|#38MoLc1PDUPmf?#w*yqdXjdt89try2Z_yP*Qje)ZlBB%m)%qr0RNOQJwc?Bh| zLHD}NQes@$NiCiQTBlYUYo^#SoNd{LEY9s9(lA-GI{~T&3c6;$n(LTP*>IA5A2iEY zs!BIQx+L2d+{q~`Umdz0NwV-8D_v1tUUYGwUvS@Q!NCyJO}qk8K1$ixtx3dg!=GJX ziXq6lmeoKP4aUEhS9h?MvT3l>XUF}GKn-my^~SA$I#^MOi3X19+a4D4_a-KI(5rsX zEa2j=n*uDymPgG7OrJlyc0s7Ac`t9d3!AY4JJwZL2b2;MykK4TW3I`?(EJ@(%Cj+CYg^eYqkJ+vAw0C2>H8w;o4jH5(U0srNbdI161?%I*y% zz*1$i8o?qW8p&o;*&3GyWS1!fmzbHz1f^9rAK;?4W;d3aip8c(6R-WY0zQv(#eBB8 zjCl(3z(Q#g?uwgpg;W;L#JT32>_pN9AXK?|U|PaO0}GOTxr~3}=4`Q$&lYpVLY5jb z{NjGnR4$7buo`*yKZZ8fR#$KRS-WzqUNOypESdooT&eu~SU;|CWbs!~zuHX#Cnnab z5ixJX6{?pd1mN0kB5=(>qTVWo$^i_p#D0eJ4Uapt`$D8eJi&=AoCo!6ey52WOstl# zCA>%MO=E%&?TkidWhNeYrY?k2GhC0&%N@)fV*~DtBvA!;gbz)fUfU=Z%WHYH4>FZ~ z`@lXvJ&D2SR{7=x8+N53392YQzARVawR%dzK|Z+^?cAyVxJm!+=HSd3`JX;@*vgV^o^qCT#u{EOn#|!u zQIgSmrQRH|VU@A*emk-h>PF$g+_WF!2j-nRRBKxZm!-`h>ccJ5PSFpXRr^{wI1`!)p#UqX8}^1U;HAW*qf!%Ut(O<|;0^-MGq z?F1%GLv$=!gUM}XW7@T1YIj3T&^vQ0EQ0Cf!~~QHTkz1O2i6k|{}|dfKs6xbduh=~ zFa>*^sBNWpeiQ&QKF{7(CUI2Sz0;_#Vx>16O zEObc(XU!)D$dM(tl>Eli5Z*OX|xalFbYpWRd<75xAbm5 z49LEpyHn#dU^3sm66Fa6om+d*g!3#gSB+-+>4r@t*|LdI-_##<(pU*&IfYL}5NHIV zs!QSU`z*U>;*Mm(-V=H!vA?Odbcl!DDm|X__EZ-&0`6&gY;dqTIM5iWkr+}YnOz~S zCPjtYJgxwkW3~4n3uVUS^d<@3!vlwtFKF{M&Kq`sHVd!~+=^Jfw$@EzUf&rDBW!Y_ zt#mj%wlLVp`5MkA<{Q5-AYMNdx1x~DppM&iUUjH3Tf!0CZU%c~ljO~2Nnao0*-F)- zJoO#zP}wCX&(m5U(d#V6#H4q7l&+ zgx#dB)h|Zb_cM&MhVwN@RbCjMIsAEQ9Ai?BI1c) z7@^vs^jD;dP~X_hsBt4xTYFSuNbL5zFDd`qu^K#nl&Jjg>fC35v2Yssnp8{Sq#t(EzC^BjH4xQekbDTY!D@CXDPT576qvfxP4%ftUV&Zb2WCG zaCTZE?_q`tXh_Vk`HMvDNf_ox8sm3L`g|NuA_eId&0+-Vkrwk|<=Cchh6MtDF(XMq zs&jkH^c(D$GhMTUX+5M~vSVe)=EM$)fi!qPoH4O5J6lpGFZAOQRc^MuHnf@G#>-mu zS5!&8Eg5m>6F4T3s-4MdbnI-3h0WAl$KhTTzgcHWJ+VtIf76a3k4xe{Wq@2h!ih+(Rb>wK$*p;A@RrfgQ7$ zz%MjXVM{(yr3@SX4H#8R#lz^(0WbRA;Qrc?p+?#{*4Gqit#@G%p}5I9@;W5i=1T7b z{%6wP?6hm%^A^`?o5s6_Umhd05DCYTiD9vT%=k&@$9HJdvJzh1je0&2v;IGdcy~EW zBy`%#xx(RN9XS~Rm;p2%`Y5^E=}20ZF2;abYV49O==mA}c^?;6+Af;J`nzlh2D6vE zR7xpj9nS6XjAm%KlO#F733Znc^<6^8f~$`S)@7I6qEt^J;8LhoJ!Wm#&NC}x59pA; zB|hu7T@`lFct&ii!UrRXz}K~}Q`3s*d1mhYW&ix6^v_2^wKc+2^Su*js18uXwYCfluKYZ;@(12v++HKm+vKavzD{Uja4%UdkG2 zJkEbCMx4^fOZX`_W|6jYKQ%CpI+v&88I8KEd2p^taUwSFM&e6?%l4PCX>4-eYMg6M zrDYSRI4T8=11+olaLamRWW7J6bH=otMxv5us_25Wt)_R`2Hn)79bHfB&Prg1G-kA8 zU$=QSN=f4TZJxK}sFdhlLfdfKWW3QxTy~}AzDxsmC=uY)=vQwfQF8`J8l{8m(9cDh zA`!=`)vnu&Pc2!pxsz-n5_6_jZcCnxgmE43*5>wTgYl~CEG#6Lp;3HqaDG$tW`1U3 zpx3NBM>I$ANGM~N_oTk?S&~0(mGgUY5Hoc7FhUE`o4oz3D-)EE>AS9$8U&Al9ms6Em$pgFMe##n?{yXT zbW1!nhoBlwY_xTd=PGVjG=mTa<@rTlo6ah}5=)wbh|`3zqvvWeCWl0`bB~N=Ynhv( zp1kE~AxMFW`^TBX;S$ntym0u66r005^B1t%Y#g!b7*J6Y3xU6$gTzc8!X2KQ9lJ6f z1&{&jCswm0+pnXC!X4DzsFlAH-oPWAaZKB)VZ_390BLHE4)Ai<;2-qxN2bT6-BSua zA<+ittKJAb~z&5nRD!Vlj<&~}16v?EqRzF)vwI`*Y`ZQKbCH0?_UZgs@{mnw>P84zX zc6wxe`i{o~Y3HVwlkL4J9h9|Hy|dh;UG%y7Mp1wraXW~ll#`A{CmyPrXEklWOLjxd zCk(=33pwh2TMB9p#E#1WW1{ukn&Z!?PW3_C!CKUPXnoY}jq;W!-)0)f0WadT4MJbP zNs~?jZJq8fiJBhJJLk9~#T4KBI`@Bf<8_)6U8=_Z^n|5*v_|4OBKS9H+mkIcmGYU~ z#@?=Up*2^`q8gUv_1%&!?m%B45s0VRvy6X8T;dCceX?L6P}Eje16TYm{orbeM_$u^ z($8Ko02igEr(e-n(q4Ra_jlb0ClWZ1^1FIBCuSa`>Y+?L{Z3rL`z5z@{}*o1ci*$;~tn8}nH+6OVf-o&vKqsT^{$+E8tVW6!Z{{<|y{yoncN#*~e;AR>qM zuA==WLdTLcC?sq^xJJ}F7E5(yg)chj&A2+c9?)qy{i`+7KC>_9CgvBiu znYClaJ+V|m*?^#MtJUzd;F846nVV9~BRzRPSON8YjHGQ6b?vNQ2ctT^rD&2+dVEQeX8r7!*S%m@)VOVE z0pr^;0_VFExl`BwiulpyAK(OA)0aMs4~++#(N`Bpe7zNdLTajm(4 zPM~};xL-&&;D`rn#4+Hkpk6t~b32P-&I(J6cZltSjdfl&rXX-mZY^(m5ElRKV*Ty5 zCyOQR;4a}$JEaVU6AQsr*qYlls(Y}}i!GND8TjdP;iyiZ289f!9{yW`c{&(K<244U zT!)+K8iaWy)wM&*{xcL)O$JFoba8>niQ225vYKT4jQZWbFqmnJ@Qzt`gt4V6|p$M+bQkg7JOZZXC zr*b(?+AP*Kun@i`K@-XXh zmByitf*?wRq=MTI+*6600Ekf((!}k7LJPQ6%lu@&G2`=*4L?7Q9>9foKb^h11Szz) z)M>FhCynDnyMYXaa8vd!A%^%j_?glTN!t#VKcuI z9|3@4F0F{Bbhlc-c4NvXQ!@LTjz;lNqZ3v4OrGS7sN%={(KQwCvmOi=N$-Nk;UL#u zU!6kl(%y&~ds2VyM{sfH%Q-vw-K#6wgEYm~Oog>gI<#=Mm=b&Wf&&K>2(v{C#MryX z)agjklk0@Ua99sJiNI_)fp>Z-)xs*b0qbXRvI6w96_@R`%`ErQ9_$XpLFCU7$MzA! zE!)ld6Yd^h3GTJ~I1`goM(R<#3I zP2Ls`8wDzrl2Epn+X|PP#TZ|VAic$GvF}bc_xEkq?R%h(Q%T-u4p4KpFHXXDrE&WtX_6eZ zYcI1V+gZO;wa`d7gll7JsbpeaCKHahAnMp8z6-JRKM93+U{StMHC z7hVf{x=-yQ!3Aa8r#kAW@h}@I>m)KU8Q|*KT0f#YA%1iHm*y#M$uQi_z`(}miZhex zu%1`-svCSi)0N4$N?x{Uk40Bx(Q^E3dAA0s+@U(tR_7V@tH+qn8%(2nB&l^4+3-)f*^1RMKGho{Yc3X!oD@DD%SB-tyy_t&< zPtO;LcYxbmQu|Be^>>nvH( z#~Z13$uo}E^F8{vRzHqY4>Ee8zu_-xhaR1!t{Y~Gz=uV{2)>PmrT>w+DxDlkr zLMB(LplP3bHCN1`!=JgFDx@|S3fUc*GRpKDa|btPH>Y__w{Qg*?*(hITuyE0`JO_^ zUdj~9>1=v`I+aG34+zInYiH}P&3AaK@ssc1aj8_RcW<5gA9fDacM40PwuYtPaA&wo z_KJ@qRjb~>*I@4qS7go;2dl8Hk@8NE@=lQQj-_0!|D6+FdG!k$-wG#JF8zvj>bh~}`sGF6d)d6unSfLP(ZHe|sEXko85#~=_gn&$hH>JD4F`A~TtWg| zCQuS!eqpUv>DoKPGY8*+A}Y8Rd~>Su#?oweH>f>Tym-p3B2vm4>3BQcUy?G;cqQln ztvbC_eKav)>BZDG3jrszk+~QgB>x(pn}Ctdg!96YtOQIv|$! z^W0s(&Pvx=I6=#^M9-n_g7%VY3xyar83d&(48r^VKfR}K^i*!(9~XlhWdX%LsPrlb zZfw?L_=yzH(fmrnO6OMKCm}t&=tlWxfzACz})DvY=;#^fmTE#sD9w zIyN^wYC}qE?gEz>49$UF-_EYlf@2NOn!soZ(*_kw z-P`!Bq_{@4N-ABAI(o14qWUIf>*eW2u|KRn_38=l+QxF|dUJg(hR|^ZFp_FMSik;A zt$y$9|Lrx`{{NTt!V`ZeSifLPpgI+FFQ}F8<19q`sbw)yxzcNKFE%{LFhTF(zOp=O z{vzK0sX^8N;d~Wd>@>h`Q;oIPQ#p6Lcj!?6fpw!6Bz&>HAfB>N(+egPMRe+xaAvNz zcA$3(6@$i5lM;>vI!){LM%Sh8-t{r0nVEtZxbk{{aMS*xxCz2iOb<56sq?*u1`m_` z%9T@<1K{oSA34|qtQXp5{z9971Awq#88C!rt`GMf8Qf16mUW{7o8zf<$xinU92y!t z#7?+@FvXF9VTvE>HV=>NjE7Szq3)Nb#tJTR|xVd)M+~uOGr39li!4iTdWrPUIED$~64uXnw<~r@U$>K$R;+k}NWaP}T z${UwY_73#-5B5|}UcS*gI4}g>U~m6Gw*YDkB518e_)PVc^<0B${w`FDg4U8|d=6|Y zHEMl}&RjPl;?UjzvJ(-v)qlh9u%Kam8UgRJGCE-xalC^maZSm+vc5H^DxjG$6I#^E zU^}xZS>2H6##pVR#LQWP`UT6Ifmj*-RlKr(?c&ztag>aWN%DuCR?_l(5uRx1=z$}B zg9nBVul{2Y$y$#!j=UdoI6jASV=%|Dk2b_U`qFUgSGRriW_T`E`>A^$`TXp^bQ3GM z|25Lj;^9!%U8yzf9YOEi!f8)B^A;eBvp63uj3W(I3lKoyHI0RkV zt+-+G$+n9)hio`pL*Lp zyIET~L)bX2qq44?sW4JM4mB31^zhY|Er?jTiCO`>Hu?N`D?u8=k`1de67KeL&mW+? zrxZWrg}9ztjySG#)~q}%3ODZVfOSa@XM}hmWdvp226PA;fgg-wWgyo&m5ho6`onZT z7PVu*C4RsyHn`@vn2y?di!Bv+T{vnqPm$WZjc=5z^A3%}9 z+J0_c(f}880+!;0_$gNKNiU2CXup;NUdm1+qg^iUz58x@Y2Y4Agmf!&#cVdVpp~(e zr@f23;-%KkeiwB~Mjye^?4mA5=xL2caf8&tHc3I;Kb%~W5#uS_#15iHqEs4&oEO*h zLv)GApj?xv?=hag1`tQ6{$c4-KTLU1yK=cA`$Mt2cJp&TYdd+Lu$Y1+au6{`eI&O<(k9i1{0%wk;Z)=eu8-FfiQxEk5zC2WKsKdh zq&%BGfU?)h*|M!`#u>%S%hNJe1a=*4?wHVx&R1~?lJM}pW%ca6P+JRgx*|=%>$#K9X4%Mxc z&cBz?BJj6P{W4}Kql;!kz5)`J{#>OQ5k!=iN|AU||;5!V(@HtxlKjuOUTFA&`~A}9qQNl2Ln0ZL}YGHi`< zx|nXxpap;>K{nrt*#VXTIWWf3m3Ew4G?6-0E~8wKE~kn)(!<5b87@9 zu?g#ebh#;m^+C4KtZXgiGCnPkf*=pc6w29jb8Ax$FBHXczSy42l+jrTr&8r#8+juf z{X#VQ#)jw{zfyeVf4dqz{L`KFkI$A2WAZO`1Q?Uakc@K$p$&2b2*unHr^b3m0W^Oy zSDo$UIG9+ymii}Nm!W-cTuXB&NOMPN7OE@P{#~jC%F`%>=bS5~;u3H@zN|a)P{u_Dc<@>Br&{nBMb>cdGVlA?ql{IhFN%yP|7v%Ftg0-ZXT|iCDm`Mj!)wE z_ziVS-LHZNu3M$VDilQX0#wVefMx9vwEbhhFpP5@o?{7^lB~*g^(;Ux9#!W7{8L{0 z<&U2k46Zd{QRb~mvkafYFAgtjuF@sO)ZgR4w8MXUq;+9I?vrCYzU{|d5D2D#s`9_d zQIQ|S<;p@86AzaTnCb;hy9#&+j?r2cNQqxLCjNfiEY@{HjO7|hfNrW>Uan3CQw_#| zzex$vWi2H1`3PHAj^pyH+b_74=p2hlZ5ZJY~;94^tVYU;bc}#SWR{&(ZoZW<9LCYFht)FfR z8&cPasRvVn(QxJZKX`SqM6XQE&!c>zHoLE|*=pFY!DFTdq|;Mwr(RjY#s^Bwrm$>F zGf`JHTUVjTOZG7cX;ELrlJ&hMM~5m`QC@*ixI~SxC8KnIl&_BCZdrO3E*W&f z>5{8`mUI%1l56bMNmNrS_E(F*52#kmXVrdfq^nrOP^T1cD_600=9Dwqb9G&J)`eM{ zwaV3b&Tv*7JUahexVpf~pIvrsa$&!Cez8m-ChH&ztZt&!>jxxX5FScBT)M+x|mG2F?)DfWLLEaAI-o4~pqy(LBxCsz6{ zS96>M3UcVGJdwPS>I^oIS}-Fhb>Ewq^6w!dC_xcBz2t5dBjhBzFfr7ynvxUaQ!9lX zxkm%UeOgET^>rH5MxXlG&nch8>j!N5;26_SkZ}7;<*7G~tcdxs@^#=Dhy96#&*MVDm zzxM4n!jS^LTi)7`zLoq^{Evm+`juiOeKFMYC%W(pR~oBlw_g6!=Z5M@3E#$?@NH4I z%sJoOTmD;CDo1}~VCAEK??qNde*Z99=D|1Ix2)Vb`Wx-5U%FI1eD^&*z%E9t!_f@d zkzvO3X?dN$iW#1}zN3+q?|r4%dLFd>+f&oyVn?s50O5_fRuosrc+eGpet=vz@RN$Y zT+F$|{1RGh6OUImXR573V#A|JJ~=TriKgAXWr6pbF#{?_u5G3xgD{T)z&vAd30(W? z;>stBPg-hI@(5X(pGLg4a16PjeyMAc6hT2AN~8qbqcXtXW@AXqs01_8yFuHuk=L3r z!Oa=Ow@FE~@D?|yDml5?4_pj;oWBv}o)AtrCF#XIiRM3SZ{;$SqRQgZs7x!I9~7F+ zXGq1OVCH!+IMIgO;PxKwfd9;FWXQT!2+-#fR0hYb*Rt|?1!7@;K_0;zYLNhG)ZoIcR z0ie}n&M_G3N#70KK)>^tqRexZfdj!Wq?~u zp-HVAJ`{|_%C&f@e3pBiLoLL&3MjHTG1rvKYX{IPq+fi>)YPQ6pYX6N4LJ^ zHF0gI4D=j6a-`?rVO-<^d(;1aeBn>?&k<(*am9pqI5pA&Sgs5V_3%9?012(%4mGc` zjPe6w8Y<=LfdqSP*tF_{lxsVb<*+pS;1!$!BOI0(Mt6ReCzRMZ=xo%(QAj*nV0t_# zb+BJ8(f?M8U;oka*z9pa1LTb@a`reJ$NT z62Y-+;qv3HLm$33v?yA6c}-DaZgdd^+J_UpoSv(p({G3OWrCMUuZ3H4L6n@+ zRL`$`;VVPUD}U-|f1_=s@SEeY8nQ&WanUy%i}X$Q1!K|UzseDQa?)x2x^CW^n$+qc z1J@d6!Msi_b_a_StHlYX+`PTWsYXz{%PayqJ691L8)cxq&^>P3{32@;pI5fK+2F&z zFCc=t5@2RFwYWOG`VYMG8rj6opiuR)`l-`u|6t!x|B)jrU;adC8j&Pp`7uzZKF zD_{H7Z#1ubbpL#!i7yrZ3xvV)O|5)uQ@ZJP@Cy=V6h}ib51laqKI?0JPWdppTe;xe zXtUb}`)!ogCkcvMEgtz}-nCD)=u2PyMmb|=_x^#t14jlAtz7#nztVaMT%Q-a#l)^V zxc~T0TpPP#`IE1GdRS&BmUyZ-M6#7H9r_ndD|5?3n^r#R{=H;+{imN>#*K#tWTmO~ zr&>zG!G@$)bFZlk(&{{4VJd5R6%PO8_ z37T7G@d;RYup2ls0)Z*V4%={LxINdh^7#MxXN4NlXfBg4;G@C_Y%o*qlt5)9q z;%{}_lPfJAwj#VZ($O!g01y%t1J6W!Z^fa6#6;l~lM&JH8JFyX9|12%UjSnX%=wB#LiI2}x{irKhw zV`_i7*PfbFvs_^~lBUKMD<_x6tEj3!tX!A#Dp?g&PR()2;F>?P^4^KqnNKa@)sgmx zUW>nl`uheB_YbZN|Eu3?&3tMLg!=#Xo8f3B8h>v?{5^17zuNijiSX5U?Mv~%X6t_} zp)&scDBD;1nM;OZ8tsguPzsaZ+B_JF zjq-{U(2MfD;e(4RTtspPK@%qkDTQL*_7Yt5*#1xhKmREwE7#Xe0FUz4V`&Cn&=vby z1h^x)%m@Z%C-y61fVv`2qiGKvoRffoeiVbt#JWFrzjq=D(k6 zJ9@EfdUmWIaWIqvC8q`tdloJrN-M#KZX{Tfs0N8I<)_6~kr%MPz(DEY(Jjgpd_M64 z3?6OA4k*Fn2jUj=_AC-XxDAj9VN==ow1>hNaw9)hXYoaVe^f03P4Y&>Q1AkR8csSn zvsP1j6R2&RJZAKxw7IgW?cSDtdc3J6iBJ=^6SwXl^PWHet!fHh2D0ir%W{}#{i!}s z+PLl9TUtM`MI>FQaQWj(-kX@xz`=7_Mx&SvO1R>FPVEXMd?i7IjH;<4l)TSNYZQ=DcHH z*bEST*FmM?dD2=(%sW7(u188$C-*14%!HC<45DvEFfEO2E z%`J4&og4BJ%kOhbF|aO6T?j#P#XWH>ao3dx2m)cV5YKOoa+%J|7_ylCYzEFxz1F8D z)0ox(Yz`&op!mFnZ0+;$^O&uoHGVsT#5uxG?yNVXbxo&V6n!`%0}pUHASBg`W!L_p;hSj2ObU= zo*THfb@FObU}hIzW?`;v@2x=2DmNQs4st7*v4*uPzYc%)HjJK7v^!_&AWE4p$8ehx zK+me?6#6?{`du@I-M%9Fxb#MFG_&9@_WEfMY#p6zL;%kLL^*l z;bX3~gaerj3hvFtJQCw%&{?p+CKC2=#qlM)g)OyIIO&&`n}hINQ58 zQN?-Wdt9-XZIqv&wqsWOd~`|Mu&xHLI}_WD6cl%2sJ)vrDvPtDLMZi|OZhYihM} zyii8N_wrrTW$j)I_a9DJWz-NPj8(#I+UlsSRl;-Q23(nYmEpU3FjOozqSFVXbBnw~ z^qBB3?6-B>JT-^hQI};a=T+E0Fd^rIB(5Y&BaR3yw#M>;mckBKX~cODm*tus%Hv$P z*E?0VN0_)5W9Guyckx@LZM-YSrodkplS>V1bk*2TT%oUv4Ylar`M9wk=S_vbYpJu^ zZC-b6INKG2?bhqQCZ-joGFNNN0n>=ZK@`lEK!aW18=1%>r^Ck5BgjjEm(wB~F+H1u z;k`aFFETc!30gm{eU)=sDgKn#)CZ^`ZwomBh78gzdm#rrL9(;$^fJ}EkVm3P1R>Kb z#Ra_?jb&72=gM5dI%52bO2hp+V%?iG-%p7|g$Mt#R?yPy((XmG;WTw!MoU8>r_)?` z+)^Z!40wB1N50z>ZmP{7%}@tv)WgSf6nUQvwz}x34FqvK!B8QF7v`46$lR3l^)+1@ zMJpRtBhqn}F>C}YX-un$N2=dQSiuXhVR=ew_3&JFjjp*yG3Hu&j8c4nu_7S~dEg4NbY9mjhKe&?8__SOuX4!ih!VuX6Em^-b_}d#`Xgo$eMtM0yHrZ)6JZPa#nn=C5R(&{6rVule8M6JPM#+g%yy zJJok%3Nxz8z>$MTM&T6sqk({!_F`b>3MCw5(x@HofnNo&_WRgK_FUN)5j;J?|McM_ z14>@=)2l6OO$jE0X<47V>jkP7oWZAfSpdg0JJDUyajdQW7@GE=auPA=A}UohNi)fP zTtBN5;vqp2yDt9Snw$0R%4yhw$aAqL;dF+`BH)5CdA9F5Cli;HrOK|#%|6caQBGqC z$CyzYm67E!_yj+={Gc23_7Le$PThr@rVHv?OE88Bni90+Oy7;ZlkkwCV~o;%7J_wq z81GcZuA39duh`+j1fz#S_0k)-JH=i?XW#~Mc`;Q7jto(07mMn)x}l zceOj1YQZAwUbmbvDd9o1Sh=xukAs$(RXGikuYxYmJ;C)eiW2hjj)+Gh1EL$t(A}gM z)!?N0)Ry$OPYq9yGpt~=eB7Q~w;f*CK*1tpBG;u~tTguI04r*3PolZO90rTAvB!c! z)i1Us29s+Y3-%c0ztG3)tO$P_@x^X6+HL-YQRm9#>Ub4W#PoKH5LK?~&^cPcL$-U9 zu%;~Dh?Gyg_=vA!Er>Pxb%R6cA-C+=%7cmN`L+Cr73@i>OVlH_upLMj;Kl|tM%(Yz z>fOm@UL=jgT|w&Z$}lY3v3qDzEKSn&!>p?taJ#|hHzk#z^mQ4Y-+HHYzg%$3PE&1b z5?jk@4t|!BV@uFvQrRx&n>FUH1a;X<)(V2WT?!>gl7R&llX#NtfcG3MRx0MBM zK@*GsOqhqgw^&arpCrdPxnCXm|JZvEAiJ*gz7y}>`*P^l5rGH|BCrv<**So*5eN`O zZZLrPbwHzuPV7b#Xij*3GD}t(YsQk*mQ_}d#x{XnZE3_($s@_OD0$>^(2OMR+Ahga zvSrKbt+F-R^4hXp(*FM6x%a)-2pn<7lB;$N&b+?i+!Ma@o$q|-i+=jFHo{M`mEC9O z9_Z@r#W8RF3mwFmeDa%Yt@rM%8@BGBzrdO9X>y|M*p&Gj!H%yq7I!oTmp-?xa_3C6 zq5r_H>V{rB(|yub!!w;g(EUk4;LdcPd^5lIOm|lu)k%HuneKAL@BYs--JkrK?x-;3 zkN-?}LCK{c<{x*YTi*XCeWXLxdtKHe|MN)q|M?@`AIrut{Ygpm#xvdbJXN{#oYU)n zK7FrVA7+FU!#eq{RZgGSyx#pgulRd%wWn`Pt^J3wb6Z>>i^ghUsp$D?ZoTo~4|{Fc z)q7b<<`#4SjV|ia-XmoN4Kd_~` zZ`)6DfQNM;)I_bqqj0ixM+^mL7!1-*PRXL%&hlq5^hPOV!kbHW0HWArXlaE;d_t<` zsmZlpIMdpaJwYs6MEa7Tt^JGNeycTc{M;z@t&RT9Pqxj$sJhatkpM-)6&&isg~PN$;`q3wU(A)X?*=Nt4xb!Q3 zb5u~dtdMJJxi)S+Ha-%I1{pCpOFqX#9z%4Yj@3=gB}CNq4{TUvjvSJCSp^(!W@i!M z5(}^XL&@{nU+P@KILbsjV|B&saed)2NgyYXXyWlz|NQvsJZ#)OFUr$!e6y>X<+`rc zwP+(muP?B6O0a_1(kvF;IKwyfAO8^tgg&1-&*&J0xT=0k?oBZ~XYrwlyD< zr?NdAQ~oIsZ|MgvetAGH{+U#?0M~xv!|5$~XT00jH9XYc+r9RSKl^Z7rUqSG=|A-5 zzMyyWrmt*jI92$Ig<}5Gx!=wm$$n4fYnh$tcT-B?TSifTHkV~4H2<GxzQ817BBb?j7kG9O~!4 zYR$*%Yc}D<{Xpz$zR&Ag&BI-N-Gf6TgVmak)zysTWBz0Me81PVng_cGo-jB(5Z2sv z`{>%}_2#{6bSl$=$e5@^4+6&n-q-3L=<4qs=^h*j>ppyYbo~pz^pCu~Ym2{MOt%oO zRK|h#gUEy5*DCMp8tm`y>y0|T_4dDdMxw&PwVQ}?)5OK(@-;BbF` zgkbw`KUKFVMi-HU-LHQ#WNf<6+giQdT^QUB3`VHXar;S!xT6?sbI#Q^x3QD9(3{+^P*;C{ckgfn&#v1~xVchy+D3^szldM=11o<}iCX=GT|H#Ttgg0$w;wkwGx%kj z>uj>#KvO8MtM#Y9@1oz)iZ=^5@=?1^8mAZPdyY25DjHdnI?IYnzAV|uVD3jV7 zSp0}3D$UA&bzyG(qu+ng-`DKCq$j2(Ywy>)fA5mNT@`nC4UY8pR2RaL+aqg@-<96$ zWCc5`^}%l_kn-fz8wy&17Du#y?YCO{ce#@60b$GcEm=2|?hz3pNN06<3`fgjHJ{$% z%xHzk&dgdGSGKC9^^4zm(cixnj}f+T!=a7u*G9koaLX2UkAWlILyTz%XoW58zdhuz zd$Fzo8MM9u3#9PDZ!FKuUSIpM-_PvX64ihA>-BGZ^zXbDO=~yHduR~xT3CC_?ZLIm zPi77_ph3qpPu$2GaERB|d;Y;Tf5)2IEN*-=H?tmVyx_M0{_ei6?h#_TM7v1w_Q2W~ zzV|;K%$s4R`X`G`H;;Eci%_GxhrM!WU^pV|iQD~aJ;!~vu;2gXTntOztHbSfychbkkcz$aE@q`(K?K7nq?L_J1X9_7PNBI}Z%XDiCv zZ%=VgqqQ17iHOH(?UheJY7Y~{MpD>65w*S3+M~7jAEdT-TKlpcNJ2%qJ9^`4`p2cV zzf_y7P-jp3|Gky=m+({irUITwzOxhk)t`vY{(lO1{(qvgH(Ge=6Vk%_$o+@AFbMBm z|LD8dyv=2*`vf$3gKQ`9c|0o5N8_3DP$xEphbieLj`$5=H%n(z5$N6^5deT(n)$$Mp@LDy>Xhmns?C zXoR zwW6j~a5=r~36y5iFiOpay31m%5v<_`uEyxEm*MB7>b-0}m9#J{4efKKSybMbeF^-g zpNovs4%7yq{!9EoZdZJx(Se_tdPgEc!ku)T?s{<*{|VJM7^=55U-jk7?O}Nh3yot( zsK3(?&aX^PUDqgO>`-sUheZMYoXY7g-8a%ayGE~FwK%whyZF3PJD6nvx=EYmmk}Nk znV|lIveS1SXum8qC^loXwJ?u*kZxAXMfEcMxGioRd$mwq>-9zqM3n5<*!y;5mF*|d zm`{{umdZ3ZhLRVHLd88gj3#`=w6UQ+o*6;FCL_wjhU*Ffso2x#EjlitD&45Ml*YQ_ z^4W72&R!TLJf{Ks>g?1l;t!PCU*tG}a1&dT2p(WzxrX-Df*r2pfqG*M>32KMu3*77 zPX<+I`g9zxcLdH0*RgAmDP|Q{HX<7;V`rr&H8^^2WLb#OtZy^(W%r~6+bJoRsbldC z9f-PEos8&PD_N(x6%hDfgn7A4_!Xi7$adjDrH@Z7zf)SdrHKUD#wJ$F;Js|@=O6gV znbrB}@m1kb&)rM^L9Lu4n>FQSrSl926WJGnr}r&gM)?eYoCcmx`so$!n)44TU#F{9 z3lx7=VN32?H)YRE$plTrZnzf+ol@*Oxr0`RTPClGt=g(893l7(nKJbZ_b~}JO;h#M z(dg8J+iO3KMqFPHMqiJw%p%MV3EbTumLm=PDPV+kDV79xL-{TOdv^`B3TouF<3-NR z%aG-gncA9>qllQ!GAg(JeM#7H_MKKbvJ_qAufnAkBAfwj_Uhx<3 zWBce!zusYiUfZfN4ENp%Fs9aj>^FYf+r0jN_B`)zDW9Aoj+i z;MgQbeK4&4CDJDCGVDkvLXZB%(4oHr3#a~#g%_b=)5sGsq&nO#*IwwY^Zr-i5thYN zS*@SI0i6!e^f9(s8J^V|uf9XVy}FFg#vG=UGOE^A$4Q=`ImFH+aKpx$@A?dXMg{S3 zb+{Yoa0%}m)Ce_t<1nTvtLRrA)Fi2~h*u*Jg*)=cbh8`{oiG#V0#^Cz zTx96-F`q?WE#hRbx^zwQf5G?}Oo1om`SHNM;VX|#i^`5+MKrZseqhOEZ9{IRIc?wQ zRHzb7&0V8*_~XE>BQ|tf>ACNjLA`@xL(>6E13@O+l3Z-d1lhoG{VL}0%;LS(*D7`& z+b`^pYh-+uc+z)usP+ZvB}-Gxgt@|$K$~aSjR^@-k11s#p>Xgl_G=Lqo?4i>woo^M zx_74IQ>ZLBCbWIJI^2E*%gBYBol~p#_W#1_G}h=K4aj|zOgGo?KgVCGis9NE>dFu~ z1Y;w*Iy(8){{>Uy4V`6m)fXii#}Y2Y6F~78HdJyuSlm#a1y)xchprWhGTIvp3)OPv z>Pi$4#uP*mwI-JxM?s@nKj~)OORV>>_ZAj8b2fs4)B|-xS=^Fwq?i6 z4%AgG&u7h;BN}I`cXi*~^9i;T6vtJJ;gx2;`eTbw9Xzf#c1dRnG;wBR*M2NgWGMRp zgB?Q!cbzeYg~C6s>{wMhbl=w(Shnb@Ls9vLB7)8WhUKOXbjsOU7se2;lTpKo@7p`h z-<*9w`*#WBqZURdC)nU-q$ZLomfL zACE1TT`(2SWT&VINZi#LGfe-hfC-@ob&JN^0XMrmWr~t&sSV&eqv%68bw?j;1o0cL z#>>PLuB!InZ|%0$?1l=DZcz3_;Mh>)SXK4*L*HF=LC+iR+6&j;=p!gb8rgPtSO0L| z@Y+Xz_~hoc2kfZd*p+PgFkXDc|3h-227jCn!hd(Kebg}8w)UGZec$mze|Bf(&e6sz6@S;UwdtX<D$lZO>SGuz-Ez7YiuS*yJD?B?!jVU*Mu++u&cT(yT2$0tt8W?Vc1<^k(F zf8rlvks&hangL5z@IiAi3~H5_Lp^4>iteq34QB}i!jtwVLJywD>gur26^fHXo90@9 z!2;ovuA$;~)7FlauxvY+m-b7Km9BF1P~@*;D^M53PNaMEbHPmTEfki4p#3J=EcX#6 zdYm^VN^3vy>94nSaUdelCQ%4h7MC9*s1ep8MtYq~sH4aD%(#eilk4A@8}r-BqpVB( zgb372ZmNgfJPsHdd35R@*YN;l8k!e7+E9wPQLe-@M1>E*c#4yu9^yh#!a>1;&k5d3 z1S(x7#wKuuK7uN1Zs?_yN)2(Oh5+lNFa~6*m+`j@GXm1`{m_uoH#h#!U2vW zpU5nAPA*Kt`Qbk1`g0j8YmHal32+mO)*+!?`2sp&bD(w@#aWnOP)JdnwUHd>aorQQ zRC|L%&`f)$TH^o8sxzuD9MU*+3ah~8zchyd5jc$*4VrD5$6K%cXYQ7N@_wx8(&tL4qc-pw^p5#Va( z*-X`M9?TI$gWfWZs;eGy73;eMFHucQbeEPS@inbg4UyqF8*Ea3!_Few!R{K~<19mC zf+^pnP-LirOG_(rhjptw*|%KV+;QYkLGx3CHn7y#h@4r!)(DOwczKn^ZQ*M|o>{@u z!YIPY)j865>m1J$fS|#!B0v>*B&f!PRos=~*>%tdCFmz4eUha0i*71Mu?1JGM|@jU z@dcO~cx@#HDDj~E1m4|?@b>kTj7Ly1oL)q(?oY}fi*jd_3uMh_F`{b3KZ1Fk!m$?u z3kV1jOe6>kf#PW2GG6z#1!6aEz3W=A-Vnw}bf^7=5>AgLg~76T+*EdKb&f&vj5(ZM zS^t2Ld;@D2{%(KjP_!jfssFv{IQj;=`uqC(d)7Yq)uU}YtNVgB5w|bYxpMt{_bYz9 z828efy!1~uw)|mi`;RRA(?7+(c(Ca!|tK4~F{iA>LJ+Yl-!U^o& z!4vX&g+JNunzw1?&Jdo?%_*Ph`j5@ApX%l=={I16p^3%xmPI^80D|LkevSvZl_gwE zXIUBUDWzvf4`Cs2Xp%xN_M~EzCrve3@?ul?P3v++2@xv|O7mBFCWu{k1xTnnhg<)X zdU`mX=Hx&uJ#+1Tl5ZM3d+y_sFAqY3B|NPMWc`pUIBCXX9YF$jL8M&Pb6)O``+?%h zRPH>*-Md=}zmC{U(E(Kay07GMqg-9_;@2QcRH=rZ49Kj?wcfm0%^+*N3X()OA?%0U zG@6^c;B}7h8=)KdQEpEJzU7&Hoa<+RbF4+V3cI}|9t~x7N1WlU0#czU1@BP}qst3e zcj}q$`f#TQhuqy*vxQO@+@AMI1g`!+u2Q5AMQk3z!H;{2kD>O5NinJ{0fNu=bi&8b z(cNrKr^}j+r}5#h?27|#N(~bvWNUg$zjNqU{E zg>Ql z5RCX4q72KW2~+P7;r0bSL80AjRvwC{t2>OV@=A~la}T+R?6na1LqK8kt1*6?A0q)h z8AUvre_AOHXEK6@3RK#Zr_Ni zP4yvbw?kPT&t6yWpWo@n=Wq^Qjn?IWA14B?a$^f?`z#-1SBiAyQGp$VtGJ4i#TB>| zB-vieI{vxF8q*;%^YvZ=bIcLU3aV{iXR^e;$%EE}&Q(^%6OE7^d|zlni7f>QLyN7{g{8DKmXS_+CO5U8iSSm=!Os^bw?ujBU4k z3HETaPlO5W`g{P<8cZe<+bjZwu&0}$O;0HayT*Ri_ij<|krY9KKt~t3j(c7;dx16@ z*Jx#HQ1;=G+yKUh;z`JwT*2J{$EAIr(qcqK2_@7u^0&wH2?gP%`6Uhb zWDsLA1c$xbi7msE6Z%OB-zGJMnHFL$PAEp(&Bdb?o1= zIjehb&+c4qdohzrJ#4jCQpxg8t=;6lHa)Z} zm21u!TBRdo+S{2sAz@-8LxaU!YcZnP!AX_D6xJpDQ+Sk?>{m@g72rx+L z944I#vuYcCZWr0!OYhL{(06Wfgio0*U5Bd;F*nZsfa4-x8x?VsdWh*M4CGr{G^4vy z54ZUIeWTDs0HjzsR_IszX9dawSM*yUv=6~#=G5WOw(JxpWmtJL_>(h4+vFOFuX8j4i{cgRmT&e~DMSK|rCh}vyAwnPS~(j+I-1vCiJ*4Z7z zEl#Wh>0=3hP9#b7pCwy3OsJxS8BjWtzR?`5(c{;Z+%)lUQ&VQAky6{d9up-R+v#Vf z2yuF=jy3p9I<6n?J+z_i?#gQQ~rz&yFW9td)1EEX58Aug*ev@BaibQW;s-VD-k zkzz=+&xx**?ZVh;_x>H<)0~J>WEIbf@KK^#+?I(5r3~k`1@4VUInHfpyEQSpf`ou8 zz^LBISdOHya`{vuWGXo>5GUaz>Tc6PO8Zo8TxDfu!V7>1;7WupI9_sbhRTMs`;_>!9 zJtU#h&LmLeJ)hGfs4K#_)6+l(1LFsDxyh28I|LXJQkAON&DDM}L{%c0O{}1Z3Nf?j zC#1R;rdns(eUb7}J~%`aESJw52&l{3;j0!R`d{fG2lmpqVKJ@07!T6bQ>p7MJLf!2 z*+wgxyf5x8%tveBxF5%VTfH!p>oz7+-8|;yOrH(Pb9msr&@4k5q7uB`QLVp9hR{_= zBcrOGjRiN2^U_YTOQfU0j~OjdiuRY{f{l^z5f+(J91C@_mCZsHlCG^XI(@n1`S1m9 zBY9dOu%h}$RpkhKg)(bBT~>9mF#q*1H<@uQcv6-TTJEUo>=ea%w#7)pg`Ik`Rdk4? z)EcfRUOvrFPY|~=u>%(5Q7b_md4c@aYFo+GPaN-4>nTS(4gWy`PD-xmRwmElSG#(5 zS^{gMAtVvTi^WakdCORB1aAN1>dLc1g$`p%DmitqM?aRpdUw0aJpBZXXW9yeGg||0 znksFUWtzBYBBYNJmrd0R8Y4gpq}26hB294^(3~~ch9R^)YumD}cEXw|FZ3wag;=0q z!y%d<@U`_?*YmN=yDqP>(MX}rm00Fie(qO4_p9&y%7^7&{nL&idCg1z^xh;*^ra~c8P*|mgw#J;U^Vxi!@Jvlxb8XE{g_e9%vAuPB zb5ov##XE{E`9d+*+R(NwU(97l=);$Vd@)mOZ9G%ydnntG&u5DbkL8;3FEuutEasIT zsI`zQZf19^aQP1(kl#v(zT8k&mvhD212RDfz^vwT~{0er~P3JzI=_u2{L#_u=Bmzw}Ne zvP66D?e7{H9O)feuYApmZC?M!PyI`8fBXwiR_^qE<;!pW>vvKQD0A?`VDS~-EB;90 zi~gQ+Td?WF?oFE-zL4!EN-olsx%tv^<+c#I(n&g|<;wdzbp3?q-f4nqPd4GoM8MaxN=*n%&nZCnLhDYFr$ufSJ*KY|2?CO}EBLC{S zm~j1;Sb<3+0f&?>z4BOtevb&#R~p!LEBUQ^cd6AuWs3i-AD=;3RI0q6Q?XWKL2p~4 zFCC?BRBjJa>Y5+S&z2S|@2k_5fgr%TXo@>t4f|=l@+V41?9}qb7h~TkRP5rENtA@j z?bG_;(Rg5QzqE~o{GL1FX7u9dPIY1Z%1^)SpXe^?iLa(VrS<>1mg%-Vdf3K+J+@f` z8__y{-Z+=->p#k8WN}~r(q~`vaZl%N2fGaA4<{d`*y#iS`jR-q_v|3>Y(aHBA)suH z@1_7PINz+wm-fcq6ZlW3Jjm~QD)y&~?mna=c>lb8rksUTOXl{<$@Tqz?PdRDY|HvnZ@%d7eN}Ur)vz8j z(y&LvK4V$v+ttC*i0n@8t6@da*w4lvJ#|Ew?Y9+wPG@ z?DiFXdTV`-rXD-GjT$EMJb5=GvXnf; zg@C|)snp@vxGuaxI+M<3^0{;ds=+yeAa%J+TK}?HUZgYbe>_fSV=w8GY=)3?=^Rh8 zP32s!(M7c@q!r+f&!9e(;L}{}vbB(Hr6g(Dv)NphHeBsgYgOm;C!0;h-n6pBvCF3H zi3(3PsP#&1=fQi@~LQFLqn#J&T&4;W(p0w#3DbH zOXu^%+trw5ot&-1yuR3{Ui5wk4a&tCK>x=tb;x`?M8+*jVg!I^EisY895!QyLW_X&U%1TaLZzzMxv_ zW(FvxXownIE|(U>GP$<4Y(rXIOXp*=R-ORKDS?tHS3Lp)T>{R`hIN-__)8@kDKLqh zvF`wi9yWkHDF%@)^PWHaPq>)|5n|Q#<-hj-aw9h?myZpegap9HBWmr5~IKt}JkZF`6%Al9d>;pBvQ z#ImIA*t|8wCk%>)X8B!xd|*H%2gZ3ob8pdm_7nDv`2 zq#XpdL1DBW8w>QXxy1m%`qvP{e`?QG6JH~p$Yh#$2aeG{1`9T1BXrS{W4ib*mni}} z{g+OQY8eC#XpK;ukYF$#{S)x4top~g%xB7crYB7gz^AX40Ma&iy{2>PcM^L93cE`88I@bv0FTh2qSd5+w2#aD(pe#MKEw5PrkCIzbeT}`KZn7I_ru6?5$i$o(7+IHDZVGCG;YKvg8m4j$qMYua zBlJ!nu&!jXMF7t~9x%_Y0k0|DL=j=Mp6eypo@UhGlr3GWl-TAX&qWGqb%iuTol=kN zAM4G&ry`z0f1xf^M)y+rbnIpO-r)n?))q!n^owN#eNf|~&w0LR*pZ27fmXZ-hRBfp zPc>4ZZWx=$p&AiV&~`RQD0g*JQ(9IjkqB-m6HYP>s(0ZNQ55UFN@il8b{`wSDHQ%Q z(1Tp|xB8H~@N3o0KfbpWMhSaY*5j0LNi71kG>efQt7r>d-wJfO1ap}RBLd);eUfg_ z1s#Ik2slORQwQ~u+W3gwQ0*B^!@{({iq(fuI=1yp*`{8-;R8+|tgs6j9~h-)^u=1Y zIa3+;Paown;cTn_)G6rK{sRG6m`NhVb5*^yXW)}K zv5b{w$;Nl6J1<_yM1<7cnW(ZA)!)ps=Y%{U;sxy;waEOp+ z1WM`>GIkg25s!~)14!f^fkk1|8AS_JZ>p}CQ3y4~?{Eh9jP9NqFt{AUY8$r=9A(U6 z-N1Ni<%R^eG7*YCiP}^#jNq$1tCgtp$B6uWY_97ZObF*VKY5jT;{=MO4~a*yDZ&>3 zgAKErbXOQdU@d6IFc_)7Gqs8x^YV3ai7%7IYIqnw0_)_N62WDOJ19$(u)HfyAvp~l za}`_k`&yBXs7mu0DZB8VGM%q?gn0|I2g6HEj!j}1ys_)<(1G($rd;pdF-CaM8y1Qh|AFd?>vA2aLy>C4MqHexh)G(V z-bu0wV7VL`au7)J1{Tuu(Hb@(Oz{}8YRu~!hBhd8uGom8||Ynq7Oo} z-_XyfOkJ%nWBa3&ZVCabpqm@#2djRwi@Mqc&9xp8y)tTnK4Tmmdi(T@49YjF=KrG= zheuWvL$pdsFr$%)nKMelpz9gue1xr8v^p?UiY_rd3tf|VdW7G_Ub&?qp-z>ofv+xX`uS4?&+<;Ax^7=vYAN>vD@i zF5(lD{|#+^Ej)Ti@EssXfWfQm=eJ2GU`+Nf>9b*GAc^Pw&iN8XW93f6rSeZr7?0nM1A9Lv-=DzbswFlN*7 zn*DN6e(@Tr_`9QRW8^GH$&J07#PSZ}fCX>+`Rmv?V}gt0HXL||jjiS&er#oFwv)zh z!Yb5_a(QtPvtRr&Ip}HJb0D!wxGUKyD}FV#N9%25&<-^>F_&4KgKJt_{=+99`|liB z;qgznh1T!ZiJxzOm1xTOc{n2ncE@&o-<8Up#-`~? z8FX9r7R%+lUK;*kuXX)U zZnK|R|EaJ1C$I4-VP$ECi0PI$MW9kmUqcK4qCti!hmYz$}zq zVZJRUd6nPeAWaeC_b;ukf8*uf^|q9w%r4l-SjtXL7iP51Cv&CimZxT}eTrQQ({Zw_ zf@E|Ba?SlX8=QO!XqICHI32!%VZi7T)AaN9RY)rh4i+XJzmF*$LJ=b@aayqtCpd!O znui@fIcR3sk~n0LPbLEWRowsR0AdJ;pBgO9%4*$m_2{%DHLtRCD+>S%sdqRWrE-bj zG<>uDAsQZ{cZ}(U~WkcKq8r9o6dpD?9-KxQ}kwTZS=o-&9O^syWhLm z+NwFMfp~^Q+%&x20D5gTq#}J7oyPNKb^YtV?8mljkJ?d2&1W<}N|-~;Qa(Gp_6x85 zTFW`Cml!#tfjZI|GM^aKpgQ!IL#{G;!>v!t5Xxl<<-|JWEU#TYXw?AjY37#JpZ@EO zvDR0k;fkrdy0GAI!@1SS7;1%BrQ#L^NI6={w;B1w6gh&cUjlC;SI^*$?C{S48{}I5 z_y2gx+k9MAI{^h3g3I$`I-ujigG(D0q40#dJjU^9Qja))%k6|q&A?fCRV=Lk*5Uu+ zwOy}baO507ST+|{C;}IaM;!xCaJB*i!;D5a+`wy*pY{e@1g}ab1S#@Xt@S4kRd26znI8bu`}+It3B!>&a~t`Qqyyx1PrB)1y|pia9)Szw0Z_*&AH8|M~4lX*i3jmh-^ z?8Hj&uBJ#9!9cVrd`zLW4^n?_%VSgX?-Es45jflj)t*ETaQ~4D#bj8OJ15x?);{>p zxDd{qI)9-vgejya_z&5D^vJohb6~IPePL98fd{ABF1|+m)Cx5%MXkgcJ8y`3OlFnc8nQR z5ZRvI?&02%^$ISYZ5OPpLL+QQaQz(^l{GY8ue9!ZzH_M3sAX}zwqv_*HqLuk#mL$> z-v9Bg?XCwKOSlfbF|ziH6K!p-L^R_Yv2bK<_oK<@20pHidzL%d%!j-ChkMsP`q|TM zrH|`i-P+eE3*X8phrj74hrj74hrj74iJ#It*x5b6|1Njqip%8nboCOYw{Pu(f06sx zQ4ZfV%KW!7%As#M%As#M%As#M%AtEkNp#=7-u|9J^AUE4(zy|pLS!3S|BwIS1;79M z4=ldw^Yfa1Uf0hX`gv17CH;)+XF@-d{)Yz^r~H4q@L{|??>&_q9>&tNX{OS=YwRzb z9I7-3(PvUs?GK{(DD-;gIQDr;H*0M#t;deP>OZ=zuD}~n0mJj9^`8F~59+7t3Xr47 z)!;V!l6fYJ)QUpguN=(H`tE#}zjf_j{miW<65Cj|Jds~5SNZ;lOkTrqd? zb*{M(s&Hcu8x7gk8cnTc|F|kafEZ3ZOJN~uy_&iuCtrx-qS8N;Ur~Fqvm}<+;T%lS zvr2dumQueQw+O4lu^6W#df|HNA}SIhX<mr`FWC=Q<^Q}CV~w8eG3O6wi1ro z=8Yq;%OtTK4g=b5X<}WLNXO;W1DT$#{ao<1?D`MC@Q=Lg;b34BO;8;+ohk zjYV=Sp_HO)zxCWx&1>8LVMAv9%U^4VCCV=^M7mOfnZV<4MwB$)x{4#Plx*VV*e5NN z{U}_dxoIO^lCPw@;kbx{C-YMGkbFO!ccUUo`y1Ubi`6$}w1EOBVNRmgQc%=g*H_9b zW~Ta#gad;FK3)oqM@^=ht*CpvB@m!*W-Gp^T*I~0aaI~dD zVti1Cr77YH9}7L;1Y`paube7rbaHM+o{aW}%-Co^1(d02c@n$Er+|2PMZhn;#2dB* z;0<8Y95SZE_wuFVNJ0_1!IYvq;`%zy74CZ_M6@x}2BAX2hsdG~+B(;$(`=?;e`aq8 zDJ4f7on4_i0)FZ89eTtuUzayQ$FLd{gOif~jKa}Ry9vhcp?0f77w^oidK4cv+BYBI zQRRe(JAqSnW3SyKNU*mcI_iGu!PLIq(`Hl{EkxLbxn(7EbKOC<0dF{QW0eo)ON+!@ zn-)fK8I2oBg>y94tfLMDs9`Gs|U-8c%hcK@69oOV=5q<-sOStXfO+ zE9Ab4zGVs}cd@UTJnj~lY(WGC2%djLIx;i{%c3i3VeA=)x^PhVJ>P&`U3y3L;2Ddm zIh?6QPN&2P&|_vkTro?fiEHGH=U6!!T?(RhEuVbDGa zLVqYdaUP+>_VQ94v*i8gul+5rL7W|+{nuyE5FJA4e&Y93n-Qh4^$1tD)1?gPz$I+gS~xGO-C7DwVv}!tM3w#LZL$t zMe!-is&pNM>h10xioP(-gt&mHb$h@$dv%UgF}u1%&qLAIBy}1HPHiNU{z1)hco-Bwkcj8RX{mNkwPriY6ct^a4v)*q6)K!Kt%LJIl%fDtU`)y zEJ~@uj7>oz5%+-f<$39UTx_p%#6fFEA5>aoB>J3qWoJux&B7s;+TSJaC@6YHLf*5W z!p#}7nX6X#UspE7gxQtFsc24)>4xwwFte;v23bx2%y5|0X{;X{jvre9iv>W7Vpd(k z@JYx6XEn$q5Rs64jLl#M#QJHUERi-# zAOiCgxQZ+eOKGZ3Gp|zMBt!lRU*1XpdVNm+-He23WiQyHx#|hz!B}ECYAPpAVf%; z!Vf|Wv3U@-(xY(k5{X782O1D2GHxvAqPUAFTqh%ltKDj0yw?}Z2uhy4yx#rOzvi_( z=H#1Ik*zCL{TlJ5PVaVbhw&!p3L-|GK6O-D`zZf&&E>I`ansG<$j#nRt%zOe>J1&H z1q2h7MhAa)*4E(|H3LQhCM}>;U85X=Ee;MSHPyK=PrcD_LPdwp^00B!lMAoSF`Z(? zq$G%h6;WwB-m3#nJ)$BqNU}q9XurE%o(n_ts z0Twj79pv%M!Z=6116ED%qtvAh2eP3+%j{*D==}wjrDRyT*3dZFXtZVBC^9m(qbnRdAySM4 ze)%1_-Gd$O9kC~23)qiDh)lF16(7tW@Le*|nDq(3o?`>99<1Jx+}<&9Oo4rXfipNh z1)XE|mI=YWM6f%stoqa-CvrZD@}Q)1RhUlMroC3q8iWF0LR6qLP&C6@LXb=l4{*;~ zDJ&Kpu@#<#6S|1-jql0~M-|r zaB1@xP8i?9Qs2<5Q2m&W^Zy!J5I;u_0ZfpXCr!8PBM=X5PV4aK7j`wlc19 zI7HTPOGK~du*Z-mmR4@T$HEdh%iysaKx#wbBJJ|#x-OJ(=$Zgx-lh4-!(U7 zK~hp9J5M5EH1U)zLiN4&1}-PuLaNWOFNb+it(T>rsm~HLi@+RShIip)_oLW@4e)F6gWwLA_K_PwbBp7+rBLyg=1Qf zP%IdQs*i%CQHuRmH8mSW>C2X3dDZ1g&~Zjoe`RuhLE6poMk69=lj{rz>&(wg%%zG! z!Kq2e8|V-HU4|h-;BBj&p1{XBDG2+9*$a`%oS3|9BpsM*af%{y#qlXp6)Z!oFhQ#s z07gSmRpBS$7c#rT`lH%`T7d`DDdqbV%s;yk!33)na(V9uW$Oh{sak#C1(3)X8RRzc zPB<`3(NO8Sg&o<{=}a;Iu1uI@9c@Nv)ftjWS@c0vo~8%NvV=y}InIJZ($CR*8tUlO z7-9j;sIJ}^J+z{_`x}*&$Q%j0jieea+1cZ{EYMnPSO;Lax$rJL`V33}29O)a#i;=T zSU+E<7oc!R@fg=I7A1F&EBavLY;BkU_8ayv;BSVw#4N8h!FDB_xB_{@TzjNj2pUBtY)ku@y3`MXZ#DHt4ZY1^4^mvNy^CgAg@_re z;Auo(hxOL^7UC-dRUR!POaAJQ1CaKPXBL(ToGqu85-R@v?N_?ab{*ri#qnqswpB(U z5x~xvOjYq%0Yj~dXE4B3>}^JlVVXO-SUd1pcNML+hUgww5ob7h+G|xteUA-oIgT<&2 z6U!qL3Ea~=S;M%rC8t6sn$umUx}KY1(>}SP$m{#tPjz*kWHuINU{$(dSPXA#L?o=B zjEF;CI3fe)R#Q(nTp7`gsFiz&DYCH*s2+Aq+ye~ajq!yA1S)uPfH-#%7PkyJrP?|q zJ&J){p?{G^YUA7hOn6hFRFv66Hj;NO#M+k|KGZBwxH|A!F>Bx{mThE3yMZv@Mab{^ ztol_bN>=8<|ITKV&$6F>s|hargf@O})7+-ip-poVHkU4Z|48M|^Wo0F_IB0t;alJN zFJAeUcmCL44!*se{}h5?g}AEQ`8iR`#x`8WVkwtzfP~l3{$Q=>XxCLt!Hf`hTza3N~iTtScnjn3I&qUv+cW7L8XVd^I8u$>-}j;DY%&A(9S!9G30}g)=jV&pF0c z**%mI@b}VaJM}9k%BlIQD{Njf)x2cpn0N0sSH8z2U$ji5_^in@7;98HW5k%y3C$Sp zB~0CvXF+MuF3a(mQFmSLvQ$6X^hkszAe-M5M~VA*j;I+?-uY>{y4m2XGmSOZe5oF> zPfblulUsvxf^+57DUJ~%uHodw>>B$EQm){~vBY7&>txr3(h?FE=>p+d`sj^~>lu#c ze2g>{+lO{km-U_&5Lh-qolBkTL0ua}!4_8$dQjZ2ep?2|S2%;~02`LC^IWMxqiWud zcW%@ZI%53`{ojzjI1to$_>QqD=_Y4qnH03XNaQszm||=ABoWOygrk$JWBa2oC}?Z8 zIv;1JX0OAMFPGUsrSymxegxTc{i?x445zw;FrYMt;yQ#$)Gx{8p)`n&&FZ-$VrVzy z_!aEtELCPj+5a!ne-x(puxs z72IjM=aZhMJJ)~lyMM@Q{kG22Cy}Zk<*h$YUox3H8lI`pC8=6Q0t|$4Hj87>oRbpZ z%**FIT&wJ#=eo{xo#Z48VPYLB1DdUfXI7N=%Gf%#|X#)%Mq^#FZA$P)_ z3+b-B5+s_Hy*e7N&>OET4{eYwa$Ss)=5W43tTurcYcxieWbARvJ!QyIsX|cf>>%7 zcM=j2Of*HD*z1s^9AXeIfwQZ~3NY}hBain-4e>*LeKoeKZjNqfdu1=LZn?~bZMh=r zIxFA3yISt!W2HHg7ud1SVT!r7KoMbUgen_OCK~4Xn)7R&$ft%XWHTY>y`(r1&1Rov z4vp0yO9qH&t|H5pqApnf+b*ijGFolQY=T^UkRG|@a8O-x7#LecfU^1bQ;(XllI~GnLG_eY_dYJJV zgUI_#aCM`tLCqZkgu!QBf>G1XF5pQ|=xVZbkPAdC2I8#HI~hgj!mNCq_qSgn7wjkm zO;&gUyZFshP&`on_-Y*jqe-7&_Y^nXPN)$RYn_nY6^g9MRdSn5QQ3>=+?JNfho_p{ zv3l);f7{ak$KlBT?QFM!ooQpqbDNUq2HxGYDf)l^Z->_(@b`aPzii1iVuV6HylGS6 zcY|*J5rkG@NB31gx~HPkXT;#p&%(QhNGy# z2Yqjtf}=bpbUN1Fy1L={Bi#e;`lRpm4Y^Cg4G;F)hg6l@9mEE>DO>K2v%WVJRx{l0zad=097^itFu-o^0dX$TS$KCPRxVxe~RmQVt zXxTk$@jYy^DtAVB+7t`=3^0n_KIg@V->a*hm_IN~8&>nKm^VBaUZ*{8Bx-SI%w1Fd z3IVA##(i|pdqaVi0tE;S+7%4HdH=y=v!d4%rz(-?%=Bz;DHnBL$YqkPiMB^mOf_Q|T>CNfpEnBlOrl_ORqF|~)kwgf(W4@>8%es8d z_rZTRh|?Bpb(6(1jeA)$az@BAHC`go$x#YlPbQoNgbNJ)dM1v4^{jFr@bYjbTW1dK zO1zPd+ws!fy_xYjp}Ol*DsIM|?rt2f7EV{_eH36^L5?R<0Ydn&@MN|eh|aoKQ`tbq z(C+4HDsFa@?ru8gQ;EC2M!0?QuN)Nubo&Ws3GZGViYunCP27GGEXZnxG$=NA#UPHt zZ(=nJ0KS`$N z`AZ}$iJ<#-qHac((hPmym?#T_1Z1$>K-osuhvJQ7ISNwFHv z#N<^i@p=7Na*3A89$oKM;-KO~K?;>@UG?Q4j>6Vf3hyhM;@-_Nu+#EBqpOEa!_*m7Z6FFHNMn>|CRZnANcyXrk z;RDZ4VliJ12c;supNb6U!!m(S(0PT9x1O8`lA$qu_&QFW31?FuK1g_ZBvm!r`tWfw z<0E?vZ&E=Z3;Xb{oc0N@k6Pcs`BI9Q!IoB|vg0ApO|v7Lj<9rwKzLz7G)J4>3OtS5 zV*2+437ogxiU%yO`}qxK`(YK?oFyPKnB)@Ka?Nr-Y9yaXvVf;%zi{wxC`%O^=a*jE zv?;Yc-ra-KdF9UQg4NSryr;Ksh^_N=+PdWjef`7iB=#=l2V|M<3-3001Ua@+Z^i-? z52}H=d}XXrn^)Ox&TqbM+urMJ63_Q!TGF)8?87m+W@ompb;p7Mh7sPid0x3E>gTg;Zc(w*>|&Im{oa7& z6Fqp8hMzoajDgj~f|p^0BklI2;00HEs{=paWn?I^Fh|CTW%v2jtmi5FfJ&#^J#T)J zK>NDcw$o3_C<}u&9?en9fr*AGt5O2zoAm5{2O7 z37cnyAh?Q?N_RJtBdYcDVB!ESJWWu zc$w1Eei~;6i%Sv0iEZ8+*ELMq%}nN)mn3*c9iSiblA)KftF(zkEM^wxZd0)&mPg1Q zSQ_fiTV7VM!@!mis9K&adI?-`N@XHY+WoBOE$9+}S4RCjOB634O`UB+`r=V9kX4*3 zzCD)1wQ7|xF(f3@YNmwedwGmh@Y34w-ISNQg&{S<5cVxq^h7MUI=yV*SE7p{C^Z2D zbux1A&v-t94Xy?L&D$+qkzM;4pZMoi$9^w`9SiXRZL(FcJxxG-EKc3~Y&-^!@VZhh zC1MF@$meQouJl?)wAU4xJXzk-f^XhZq;(!IgQ^ z_udKN)sXh!HAv$Te*Tyj$j#g}SJ{(}`B;8(C(u6XC7nlKi09>YKZQLnKKRyi4WvjM zP(ez?d;O%gJQUBa)ptQ;=Pe!`GTMHcI!rP;<)b-L$ zjFV;zFjU^nYFDIfY*y zjOCosINm6>ORBnOV7ag?35y){GT7zMi<^o7+vf#kS*(RU9P#q3XV;$N3N?=B$U8Le zB=jMw4%2TP-K=IoX@Fq)N_k>P@&u`Ll&C3c^6o?J=+B;FU^XSivO#SXm9~8 z=5^33798+=Og6cr9Bj4{8q%4t={>Mt%MpN&_`xc20*b1V^T57(lZd6Fl$5+CdDU?O z3#YO}g|w&4b2Xqs|7qt1rC&oOC;meBC%u5-3CtkGv1HO~LUzRIoK$u&z z##RBl?XL9XC70ySb`5TG9!CLG-4s+xh3!cKX=lkUpzcuZOjhacuw=*YBATax7)(Yf zgiNb)aTts;%D?3@j&)w8q zC^r@xiY*PfwtQ<_V}U^8ndW@9kt{2%xrT;(u{m38ELd)pwtS|w&|KKu*jQ+w&U~&h zU&xaOrs1JXk#c<5kZn>}@`l!IGl>r}4UPGx3_9RwA`dg_#le+Mg#;1Sd&3L)T zpYmkK+_`WSRegvG=3cIcjtxT;jJ_jab|@*AJ1eD~$od;RGR9V#2@cgi`4?O^uaHo7mr*6mMh_$K_s?A-7D zVBqqrpWuTs;SBmOzw!yb;Df%)FMqNRdM{sjzz4Y4Z~(Y>6g`(;dcYSC_@Mjpi%~9bH3*P$0l~??p-D7`VH`R4QN?!P_s*hdmn_t@JpY_&%bJr_= zyEoRp{=IZ|cISXUSNjyxOB6PdUs&zSuL_gb|M9I?{DX2 z_pjH!uP)K4mFpz!lzY^@v)6q&-sjKU=OYZ~ox!IP<+Iv(_erp|;~f(b+Jo~t8!vNiLU2dMq1X-I>*d&WipvS#8$pC;#o(5DdSC+V z=7Q%B^!HJSy2@{n5NfD@gjal$^1T6GSkj<`9n;2mI*v4x+Y4W0W zxTematYhSP-L$79Iy^mPqQkSU4Sh=TMtB-)=@M5DA?1xg)NO}Qs})IW1eYtmCr;ul zg_o2n>ah;1vQPDV*81^0S3}l~^V*bOw=N#{I1z8jB`c3Q0Ptek#($Zs0UN#ng%5!> z(gPb6jS7^5%a-?OuOz3H5qG9m2Vf9Muw?b8)r&V=j<_D?nMrs)r$foEwl?dFMrS!f zla(Gf8dcWSkx~1gKsY9V9*uukLqdwp%xLBUB;*vbu03LGm?D;i>x}gubOW(9D2_?AD6jx3W?hI`fx{x|wCl(&5_pid z%SI&xe#t?UhofB%k9c?sMC?T`L_V*t8mxO7&a2=N2jz=gBADu$4n4o6e!cr z2HpsgeT}@^O@j>>i6|wkZN>*k)zMvsYLB5~2xn_r3lAof{L!@zGMkzx^`=Z87>$Ph z7Hf#!sACKUSgXS4EZJGczE%0hC6rGWn`=nOtV<4JecDy6Vc9V8w55XGVP9)3`&iK+ zuazA$l}Fh~Nr$M|g6DT@2JK0U4J2;GZGjzjvLQj?lAA5An!E`2w)_6T0DZQPA3@L^ zUY<5mDG2ZM{K08NKzyt!$r@QyDE6w6L>`L z4p_5R(V3Vx04VMHtS7yTiq88IURebVV2}H1H>#Vk^@)NOkOtw7ho)u&BKQv1W3q?Z^+_#ugiD17Ca zP(7law|g1l>F96|6H&SITuwrvO-c#8%pCXB_~d)~(s(>HI_cJg!fZ$tGwh^mu5KDvkTo$v_#Dhw|y< zmSgE;Mnx*IY-27-GB;iCYzdH+1?1$^v@rg?WL2Fd%%@voZz{d$>}4Z4M;sC&2awo6 zAb8c%lSq7W%h9mF#OQ|5$n`?CZHVD#{opEE^Ki}&b8^?A`3%*(pap3^a|m~orBi*rRu(S5;!6i9%z11@SidWu zZ+UEMxAcfdAMWT$8QS+6N!YwAR;1?6=XP|ER+Ou`&bkMBbufD>alY=E3T=HOM#`Jm z&E_rk&C4h3&v{Tx*}o43$mP+dhtqZ`2rzD8!o@_*xa5Sa6zEQRODaes!9vD`R-Jj! zlwBZ&B?ke@KTBN?RgwvB1>`UwnK(DJcW~2|43aa7K&IBT-pZZv6vuaq+74W(A!s_7 z5A{;I-JWewB2MW@tjb2uThuk*lKvgbUIL+nYxN8$F-fmiT3 zu3$&trzR}>wP|Iwrk=={!bF!te!}G?am$=!)`}X*BpX#k(GiiltwP|V0@I7nsp+n4 z+8}9pc~`B$bHemz{e zq@^R49mgD)bxV+*@Yz{%1q)}z!MzP;Avu%UKqz@@E7?{Jp#`|t44d|;dt{Sc7W&zi z&}54FErQkzN$IIp%j-#uG9VUb$nh7eke-!4H+I?|?#Rj*JCHpS-8ON%yJ2hYm889S z(_m(sPLT(P<$?a*!Gdh=e_@sB=_J*FGy~ zxgVA-ez%s|+2E7#uyn8_PfILuaq^i!I(Z1YQN&}=IOnVruJaRq!Wmn!d?d zqJfpgRI<4SVdNmX% zYMJPoP8V}+nIhR$^O@cIFJ#(Dv)Wi_+t!@j($LmiY}s9GX!~qKzM;98YbrMLU9nI+ z*j{XEZQR`OBFUl~`gY};ckXIv$+YB(Tef7MZ!Z+{TMLD)4G%T8x3xBHYiuesHWVA= zrn4UWn(rTSQUDLTrEN$7{!_Ah+^oIA4T*H$3*_L|j#|kSY{r{yu?j?}Nfao+*gef# zUi0RDg1F^&aNF%E1FFr>#W*#Qn$V>P7QrdUNRtcrMSBK=B-SYCPM96dZO$bdw?$kK zb5z-GT?l`DB*(3tGw^E?nz<^6<aa4^J8G32Nd|;(p%HDNZ}}PJZ;3bGq5j( zB~!j}4QG^tx}osOmY6P%#<#y@7Y$`SQUdJ5nda>eyJyj(!j4KBri+&c4{vQgW>=Zr zS9ZE$+jhNt*dCp0YIvwM9yrye`u&17-4|1dCXxKOw&%)bm~a8El1%xz`s5Z!0Zbs{ zw_}jtoIe32-))8}S(>yE8K299tdTIYU;7J#7omUNPvHFmnXmpwpG!tr<38DYfN8;ZW628gF3lM|N=d2G&|G!>B|| zVWUP{gH+`I3hCp)l8`7{gi$l`VMw)$wt&LlxIarIKhRNtIoRuGYEGEcL3j4_jHiM) zyg^B0pwdp%T`bXX#hvieL=`|cJ*y=rJnBpZ_@i;7{E9C_JkZ|Q85%~{f~PnRACN^R zPi2AgO>~WzC71$Ml*DCK6gdHwLO21gDK1vs_MVeAis%>+U!$LQMe1-T*bf(qo2Y030ElxsgvRi_L~%x zUoN#)mf~^3%W8`kFgFKrqVEWvqHIer#hNP>DAd1;yv++>tXR=Q_JhOB9sGq`m z1|taVOU7^XU=pkpDAl%YJDaa(0=N3Lj{US&fL3Gk*~1TMs^ZKG!92nS=K>VU zXl4wzHBqkz2^YwLujoN*D&cTdmF>kGjri;~aT?EpSB{$tdALj)u@iIVL3+D`O-{g* zh%T|qj}x|CNNS@$n@Yj*g}kFU&jTH(#+`S#Yq+wfkg`RhUR3%J@GtSPt)BBb=SuT_ z#<*Z7D6js?-ldMCML5neJ~U9%l<-EQaGda!HY+NTz$4iM{X-Ird8fW4r(0* zP8qBlTf0aBj~g`!f0KbUrQx#fus7jvS_e;C?FIGeQ^tTep0I!sp-hV~uhK?AzjwSU zPTbPKF?Nc_{RFy1(vrA-V&#fHZE+UU7-POEF&IxMV@5=82Gq#*w78$=fcL?4CJxew zE(poHA#fZZD_TV!w_Mpx`ZMn29Nne*dwENMV|G9xME z?hL1Xd?gv5>V5)C1*TGFa6&g^8+d&=(Cxg)S(sB3*kr3db-ZFnQ%XZZ)PsWOhr5K@-)vwGfA#tm{mf{sUlht6K5-=OLpR)XA9~&@d&oX& zi(@;w#N-=$-DtWl`=rvU`8o8IDmi7wAsWlhI6r7+5F;*3+f>m0Me!xC?Nfc#U#&13 zVUiQm{P@b!G%SsPGY1)v2S>O7U-sg#jlv~i-;$S;2AQL~cJmMlpA7=6djPgNut;^z zr`tiSchFB0>`<}IqV?A9WjENoJtLbp022MMx*E5y_3VBBsj`n1yg^%4-warZ4{hl> zA%<_EsikR9P;8K?|K9CG4?ns^EA>i8b6b#bUUzN?kFXlBXapGABl`UKG#Xqme`FqReVq-2}%;g(4?|rnXE!UK7%uXHLTr6VmlWoqlHWf1Y&D#rYg+fz4 z*HGA&-OM?@b!S5{pB-w=Zo^b)ccIX*txzs*&S6H>(2^xhH~G4AnZ{gGOP(V((trk8 z6!HDGrbeub8n8gx-`rFr;d)~s+t#pc+xF&SLsJXg;Dlc+aHel)*!JkweGR+yX=}dN zG%;Arx3oO8zp0p``bNx}wl+5vnwlEhT3QPhVCyf%|ADt>y<_oTd%1Gq53=33^M<*C zL%QFZjaztXcbr~?BNkd_aQUfhjp@%a60h1_2h3^h?s(4b-h~9Yhh8@3W#J)bM8w51 zd7Q_AuE)=M#}AHsO=VV|*S=@>SvwCJN!n$bn&zop#Oc#EqegKa-Q^`D}V z<*M8HBV{b#*Z{TZG~pyftzt1gv;7fw=A(y|lLikXt)p67TLqAjgCf4sZ{QOd$aSv* zZ=$1(z8o;Jk2$0w7rEijXA|%$08#rOTv|DnDta(e@G0vjTJTHU^-YWLZuq}zRdDhhJpdWI3C1o#>>Ca?4;|7b>Fy4L6= z*zEA?W;6h{;o=2nA8frE_2T8J8RPpj0c}DI`7}J^CGZb|Fo~t&#Z^ukA`y~ebW{!+ z=Pqn{&W{s-L)?f;d2o$5D7wjPz<4@zFs5bH7|HhS4`o}M4@Hc+WK6!FD7%OYHW#oJ z9{k@tT%qmUlqmV>YQ%`JOfE>!iXAfzrLK5!^Jk|S2A*Z$FfSm3y0q*6ZSPHE>&mwL zKHYQ9o#%m*C{aiAM5#zo5;c@mqUNg7RFbOd)$mGnNnKGaQKX6#B~kU>yL~+bNF&eg zMt56wH{8kxxAQ&(X#{~0CxJU{#0iqXaPoj4Kwu|!jMzcC1H^&hAjp^G_h0**doNY> zx;ruA`qJ;IF3+&fp7+{ouk~MRxhbW_RT(>;ir#N|t`Rrz|5d};7Ld!tGxQ_hXLdxx zcGRixZbULH{poB9d_0@D<>CiP^K-;b7WavBS*n zq;^rGU6Vnf-%E^3e<9~-R;r%2f&{I!LWaa1%Zmx~l{Ympr1QeQ-ll^(^-PfKg=BZF z=xl1#8h&1ilCIpUZGD@=o(OYpH$6HYbC($gR+8phwFXcu&Qo7aq_^R1dLDqN7X7fR zT8hq}s^s<(QX*388e*>HL6zPG z@7u9N6N5VA5=NdE7%J81a?4AvOEL)cmn-%YR^gTD0YOkNei5(20v%a#qxCL_Y1o@sL5I5U0$5ar^==%ev zG#8D%Bjxr-yD~5xWZvUwS`#}v{+Qm_gAH%;rwU(a$vMrU zDLW6IKIvzhYx8us;WpY_m{T01N2TPCk{$sm>-%(~u5at$F@w70x(^w0CN66Qw(pvK>`(f+{C!WkfE zG;1QwjT2elc1rC8SMw}E=a|FImOUl0_!zP)fDRpMOXqwNSp-AC5rI(|W5xz)`(GxV z&1JJ~Pb7GTZTg!m`lVX>Qb&Nx_7F`idvlli7i&&ZBNk|o)A0Q@L-<>} zuV6MPP6l_CZepJno?dQ1+|rr6z9*S(ca;`4-*=n#`YNNDs&4+lZVlcY{rpHjzDC>s z;l!x+{Qkebr@3e>$4(t3JB6GbE=&pJnHu~kR=G4(>*0u!ywlcEZQrAj2hDtJj18T6cROP&2N z5j=u-X6U$?)F6dkz{W`pL|2xz4;E^^D1ynawy+aJki-Lb!ac^9(Z}$gSQ0(vm}XSO z$d!+11}@2XnZ4GGqh1E{A6%qMW~&~=dY(FKp4#-lFhbi8B~Irz{>t;kQ*5~C7Lx4q zgC|dPqb>81j*2blk3=my^;z*#m3GQ?U0tfN=He_K5nUU1A;wsG`chxhhSTX4KS@{s z+kola+;pj!QYJ`5`F-GEVpo*m;f#Ji<=8;ew_uX>y!jIMmaZ1Np}$b!3wx}gXwOL# zZ1Dnon$tq{ZB{Gsrm5&JL0O~m@baWAeQ?W5;$}@^043ccAq`GSU7BYjISANbCY9cs z$sk2D59gFhb`sw>ap`quXOwdrmc1Jls7%4iBd(s4tw%bCeO{I*umXbaNN5pWCV_ww> zW8f@i+xT-=?e*XQmYNcq$~~aVm3>3174E#Cg3YhJba&;A9C(#6UADEj&`mOa&asW_Og zppD;AMElKY`f#CwrBJRqQpIKnJEBr?n1gtovv|Hh#H2=Hs937y3zbr7yip(K^j|5L z^QiC3m7xK|2m_q;%cWYqKESEGUZ_+Gxl*lCseQt?#YU+zTd(JbYJ=6vaII8nY%T1r zU}03P9;?@?*9R~pqJSDI{c5ecr&=7VR;G87aC4Nlb*Jp?=Jm60?An!_DUmSX;3ANXc0jR~;nNy=|TXYZ;UJXr6O0_hGKw z6!txTT}ETd=$Lr@+4Xp#3{Z~adA%%ePijeEONy$@VN{)R17R>G7DAzbSiR!A&%P5I^Pz$4pJ#a1k)i<&A+4OyC0Z~=6n;k zOJrfI6@bw^6Wi6WolK=UO*;j-GUD_=Xdsu%vT|`h^5B3;wsTOSbV&B;MlI%jHM;b0hU2YZ=rRobZMW4{~9w;XViCasPJ zXkNA2jr6>QjH0XKTT#EbpCJ2mfdFvM7*ZKj3Xx7-H+AP>p$Uc3ae7;jgI$XpY)1Xx z=x_7@=A3Jh_Y!?SXm~CS{1eG8k96v4Xzx#uGFOgK7Y+5zhhaY*`JbX_aTf#rVc%(e zG}~(MxQYVsgwRUS*CQs-F=hgt-W(1a6qnA`aEdciA55I*U=khsDC<^u(lsdhk{<_JO0jiN1L; zDP)I56Ldq{P8><*0Us{078Rb!wPY$t%r>C{zk@2A?PjqWkO= zer387@pM1^d%J%^o#|`j*=QRVb-D;c)LQv_e~U`$5Pu;Eko872ekbX*r4o~V0A}8J z)6NbKU*M;tX;ZDwL8>-5MbX0GMG@dc@VRzWVdP`ATcK|>#fTO^0a`o zB5np*f|xw(qd~Vbu_8eAzk@Uhs{Naz$Iefy&>FMXjzOFJ3?cLSy7D8Ia^H^mv7d=UAh;d&*|rp2apfhau{mko z$h8LYs(%CgfuC7;DZx=&pih#{>BrhTWLR=TMO zCA4$z^Lwex%jN!#_!3odZ!1LtRp9*a#?+jZ(pu%h0vHtB)T}=Bn1+~EQ-=y-0doTiEgAwB* zYJo+bVTQ%st*WZ-$M1<}Hv1*Km7-UA7)5Y(ee{*oOTG2_C_so1jm4s0fd1KT+eb_u z=lU6oL9{BLq>>ih$JONP4V%`AZQC*Z zSw)}GqkT{P(lVRhecK8ax?90oHlswn#yk_uTANqYpy!!XKQVcc%;HvLwr`l$gS>oU z^eCg|-%Av~xC!cQci-qF+;{(@e)9KYI2We_V3Z#wi*{bsfpI18X9-{2KPzzeh0;$1 zU^>W>e?LKPYqNWZlS}x~s730`O+oe%y&adXM+pE1^X68Re$)fc&pqOh(ygMN`B_|K zII67M04G+2VY8h*YM34;&3T0?bQc*vn4~rY%1#Bx(|SK`GzVxf74W=>s+|hbk*{?(aqd@xbeoOB2>`{(cZz## z0e1hekv$>e=R(Yjs*YIXtub9i|FolnhSRA>O!7&`uphzdozD@iYVOVv6}{}IcKOV z?E@X>m`{8su_)}vaFExu{}goZeu9C4>PWFx22Woohm8ih_K{k#GFZ!%bNMnF^zxQ+ z5sw{(p&EesVr5&o(7<^Iiul1wacH2x;d*DiSj^YTXy*$YxJg@WRO;kdsSXr{`!5$8 z=uS{|s7riSN{kt2EP zl`l313q$3?K&jlQ;HIRAcM)m+t2ijZPM|heuQtjPfM1qgG4E1&?-`DkJFU#P%K;==#S1|nI zl;1a4Rj&fy=oCp>O}&xB&K0LUmjT~!zDlHu1MNd+@Qs4_k#lr9U)-7<$|NyuDCDx` zD%uuKg{g2NeP$q^O(ll89V(wsrG~a{ueuDpKBpMRdwH0@gF;h zaxiElt^3E%!c#4+_s!I;?Vboi#g8RpA&>61F|&KTvz~-L`ZNkQV!Sy+&y4L{OtC&- zB@N7YTwG2k`UL_{z{T$IKyS8#2y;Y96DE^xdvZ->I+?S!ck4*9eRtZEG+jx)$R?P2 zBIpG_AZ8y^O*eZXov%+cvD?E7lM-lLkK<-ZlDqWA^^GvSzi3p6q8Kf4B4U7*4d^d%g?x>HH7Zys3>>$8 zQJno;N*P}PV_{J_+@|!D?nDn_-|tWJ9+Og>h79Y_J74vR_(5Br17D2yI+I(eoCB$V z0g31R!E|x~saAYDp6WlGEBT=mS~&LpZuQv&I)~Hghd8F`?ci_u*+;NI{aH<*F2x5J z&aBsU;IcYSW?-J>U@$K4NKkAovjs8exK*`NvhDnVJDk-9S=Krh2Ct6@Mz3bG}LCgF9-(X>)}e-@Tp8E#kPWdp6To zXHra?n7P%1v&kGPr=D~}&)V-K^X$>$yZTykE{We)=^J|UdnQPrSP={ULafejT$2(cJN09oSRWK(Vl}q{z=K9jjwZAq=c|l{JD^@oA!_G@8vD-_Q#15 z@6co8WP}Tharw<}m#QGkKVTJeYj#SL+~O)$QCUa3bS$|Nq@*dX!DhZF!cHT1D04t55x`Vjl8nfyQY4yv!N#RA&wP0Agq53q3Zo z=KY+X?+Xs)hMNf`Gc?J=NYOULqtTcP0Bi|tuB??|h4qiro0*~VB_}P`VnY+Z7y*sm$F{77qZ@3F>BRN(Gz}Nq&;Vgg}8@BG&9!8Z*f` zV)AhS(;)!azPUV9``5JF%%KCbYkuzA6|V4H90pglPm)%9b7=4Yw<*rQx3& zLZZU-0Yu?wXagbL0)k?zf|S7Td^U`*1EJ1c)A5-*ipkChQj1lrSoz9m`Dvr&(XaV; zR7tn-J=uE59tB?mZ+RITR5J~-4mE@BPCiJ>(WvbT>ZT9<)bgxjwWYc}jw?Q7ADEi1 z&9$Q{PDm{$;x3y1BRkk!*$kx0dwXAbY$#Vs0xEw-gP2^(@mh>;;Ce5VzqNLMxha%F z+#dt!!nf5qU|kt(^S)|AmOS*={0~NByfvMSrmMD?AFJm}u}4CcT0$UVQg2NWX^oS( zB%Fiau{a2B+!6h_pw--J1^`V!BfumR$+nqv5H5zE*UMWNjF?CN=>7*0WJc@fec`=m zuAOs-5yDA(s&P4C!ov91G4nir%hzzlznHl%+?Phm*pnG2+S2f0S)saUZD9 zw+XiyMXiPLatmWlV|JU>!Z<#Y;J^}X(o;!{P)=KQsZR$9J-dYr_S7x!ngW*#|U^^Ll=^r_m12UmspbX@tP zq==@~35m3cP&9@YP!lu-q}6Qx3`?L^8~bjXS)$4cO+Cdc>*_-Y`C*^f2q;C<7@x+}$$Hg}?4O%pbC-`|C|evIZ0Een z#Keh-qsNY)Ae6!65p&zD>aF3v$DqWzdFExCbK)WFC}r(B>HPehB2#%6k zf;-Y%RX8}O7Ku79S1RhwJ#YfOs9&5v?6f>eDuN3Dcp)=Bdkhpf+YP%Bjm*bE7H#Hg zG&Cae=+i}TuEU0>ieFazqL+?h%(&^e7I>njS{^ePmdzqJS(E99IveREfm`Iu9Nzi; zF&04jQjpCjlR++(<@`nfaZO-JjXOa}2*#Jbm08!))+S)Exu>|p$KKuaW814)gUw8h;Urvm*gMnhbwz)G|sunob zgO;x~Zr8UIarL>mbQD|pT4SV9!e~ENtPa+SwR#mR`O)&0p^^^c^+px^f2m#_sN@HR zD~(d4+8C&V$^ObsiORie0AS`Hb`rU%@<}QrSJG{17^nhRfB_`arcbQpB%774ZT>hixOpdZSSutYRHd$yc`^ z8z>cPa?sZ>2Yo3{`V*Vd{`(uv&mo>{=byF{s1lJ}rFr6R>c) z8+d9k6ZbX=nhsBC1gnU5c?>U2JEGY(fLz;lUdqzI)Er}`xihP!+d=6+yZoNfGuv|w zDAb95&G`iDNJQwG>f(N6bu?#Nozg z>O{X-4nwUZ9<7zfB}?Fs4Ih0K-I3u_?eY`m!1BBk)?!M;>s=pj6LzuKshcCP#|C`c zHy|0y4mkn~z}ix*O`1tf(RhO)UQQALn(g1@)0rx2FisC^7~|iRZ);V9mUU*t>R3Y? zPI}_139Z24Ar;7!(skTYkA)`?2kc=)O~?E^9=JHF!63){<3s9W>&N)ChOdLU@r<_( zT8^5>Z6~;dS=UjSez(_W4cyrlll?S8S`PYYFgFf#tN!1gv`s;iVic8cItujW>Ua@8 z#P}cM5cUZY0!30Qe~A4IK4j-r5esHE|{%=(5 z5$r;M_BvIN7S_I5vxSxc|Jb!mL7DA3C9<~@tt4JtSaF)fmyMMW+G5L*awO`}mb_PX z(*(JqI=s7w!|%e{tTg%9q2eK%fz{WglD20Xu$D_gI2|1+n2J1y`A$Qdp{@ z7k%#`lts(z>wum0XePA_t71~E;mrZn!m34zVd9Wtj%}Jv)gpj73UP_G)dup(%S&GN zc@rGSW8O#O^9dN?r_LTi<8{6u*6D>3-}1b5NTmFJ6!z|#x+a`${%CE_un5cap#u{# zeQbbB6e_?MyqDO>byQPkPvko?C z6yu=1h<=3ug{z*Eyi>WeuASJ%7-m`o9ww4>7+orQzWF@YYRHvFMPo+x<3Ea1Vh2lf za%lAbI*BU-ax1rQEO7w-uDC0it06K^R#WLrHdW3RfkC$u#q7K3g9E@66IVojH2fHnx@}Qvr5yNxK2yrE;561wKK9{dnmKCJJtTFWM9>t1e$|y{+%-ra-*HLMv|DRX2BS=BVwXE2GNb ztO3+EAHM?fy`8wYEniG-+n&|;dPai1CKPuG64g2m$O`A{+Kg@weOA=^Eqt2Z{En^d z9iyA~;0*_&TOXgTVZINuB5PGq)<_;D}@yP=lXaw z?hzAqdA;{@9D&*qtn>_f21K{XBoNJjM*t+(HU2;rFW4sau*G>E6uW{?(>RU-*-R?4 zkWGm~J@CBeXeLz?2N<1F!-!B*j+2x1!!VXJqT{{^C?!iXl=ofKrL;o#vk6X+ zDoV}8t&cHQH|g-R2eQKx_$F}2Usc*C`iMD8XJVKv1gE$Q&s^W(J&z4iXHOCqP@S)? z84lM$`|fF8MnAR-QQrk!VXTT3=eau1MCCKT`mfSiT6BpzE)t_2)5eT$ajWwfc@2Sew>Tax0yRCUkmC> zJ$64S*rF~UbQ~fQG2=LRK^x@;g-C?LdTVXJg%R*d3pWs&T-+CceX>xId&4@oM_Dkb z#^LMz_GAE1h^eicWB{UcE|!LB%1*h!Q@T9Ev}4}I{1M1v1;SPpRPICUieaKV~ z5R>ZSsA=`dN~AXh2nM{8T^n=jX}wJ%h03$Q#m zRv8;XZ-2ORv68Ez-7n?x$4bLninZ-8N|ihg`SQx9Ou&%x$j*8-U#xP1FKo__gr(AO ze%oLfhkzXaiyZ#TLsc*ZI0GCUDv;CuLSbZcVTh7VpI=(qR9gCvtN-kr7iRzc@Z5iQ zG1>mJIXmj7gH8Y1@TMSvv9?X05ixRi>m}0xALs-%-S_`ZPhjYYF=9kprZt@+XqH`N zu(-s}h*&F4AlwAY+>)59ZfEFx#%w{R-`2!_&rYA>n)BCY!S2UGw^P~#B>C4gz6w1C zY0DbYCtpB+7tu4h;aW~(>4PDQqui%qQln;kB*t{_zFe9=l&neiL=z@k@tE9@RA)Bm zynw3VJ8f&n{szdfOaHN#dnp+mFkiJ+S^R{vl3RMmggrqZ!A=ov3`bC!%p1^2^!Nsr zr}B5=^eg7I3Ps#7G#KPUJ%@FO2Fu&@k2j_NqfP(#RW;22 zx6?np+xgiKYxAAzwh#VNe!5dEUN4T$6MGZY!p2A}vbJq@Ba^)T`7iDCCx*L$TJFWK z??K|0AHSaYpKkcWuTLKN(BGW8i=HA}e0_wQ9lNnTw0L7gO8gglPuIF1cInXTds83!L%Hcw$0iS- zIDYK-(bqr!-JAa4XWf*C+}!@Im_rl4a<22U&uep?;{^*dK)G z)y)2{_rCi5_qSyS;@~*(9Om<6i^3idX$$$<>QxBkV+A<{t{MXQCPF1-mQRjM@ri83pjxYIs=O^#!)FrOOtvkeRo!D<($)7h;&qBL6s4a|#N1EY0!vvs* zZqs1xqcyEV4;bLZR=CWr1NYt9AA%VYK@V}T_3Bst@aVv)3x`Ac1IHCjD#lI}@_;6Q z&076-X;C@`X<};s>zVgcOryA_=T-3XVtC^Sy+&B8)?$d?7bel_<8U9l(ur@?ULfeD z7M1^hU-wpskQQv_did%$|L|zO{YSOp;=;;uG-~0(W7J^_3<%2BKWB)YUxnqcps{offDdL3nXN9b&jREPWuO^KwFIQjR?KAkWc*2QCPn)L zQxHNtZuKPNYs<}Wahdx!*UNX#>q)-24toF!ejd0N><+CT51Fu9=SwWY<)??>n%e#K z+1Nogbtf47{(Lwh3NrANyjBVHz9FwaK~^_fICofHfqpReF&$WI(>rfAs7tLxg^unI zZ!$QtNSbSg=-=@=tMPgBqi^@ZEn82~$fBo^nn+)|8ID(UyjZl_D8U`^QcG_`LAC41 z^K~fH;oQPA#^A+xC@ByeK{R(*rQK0v={2} zyVIUOY;P>)V~G-0jA@z0X%@@xDXaXC@9XZ4z4)*G?h)Je%5Q9YZV%3~2TvS6dSdFttDpbhXNLy+cHq9<^VR?UyGwN(gAQ#< z4J8x)tC@duVW|E3?mvj*xsBt={htMZ6OfIc=E&IDJp>SYk{eEU9l{YM^n#Pox~I58 zy84lqnEn^_#J{&s=k8sSp%Ka8gq}=reSoMrvPF{8GdwdWEE^I`AOpda^$T%=5|2G0b#*nF@QnlD)OfS}F)7maXqOkgf|yf`k85 z>QHWSOQWJ&;*O>VQiE@0YQ&A8f+K~-$acLb7PE)4L)rT9h&d_WhYEp_3MwW#FWm7m zrj0YPn!?y$K;XmKRhPIqfiBSq32@&t4e%xt@+3XEm0-035}Bo&&h!3J8a=F2Zd~H_ ziySZ=SPA!XJeSAsxB#5J6!)^pMGRm`q4Zzod}z75Zf24YfcVX9Cfi=b?=lS!R3=^OOfCoz2sALC|hTqe` z?UBbL?O7=4B(F0J1D0>zBCx2lncorcB85rE{uLgvAgeW{%mTY78YTNb{FeHIYIE z6@8XS+GgoW#rLk5ZwYx-^J6$7!Zykk#{J1e+OR3ol&cY_dt+M110v|*n4z0-H&(H7 z3KB_evFWv?VB;C&(a z_vqKJEDGK|rsP4$Hze#HMC$m~$t;nYCn1b_^L5SQL+bMM4i*bfwOQa2FE}xE1k$LC zZYGk1eVu?f>TW4vkr{RQW5mYOQE6C(v4r&$TZGvNZEu;?0xx|Z=fURHN(t(~tBoN*5 zl(H{Y2|gzOaG(H`ze+sq`A_EnEa>LO_C$_l`3P16xoMODKawjeidm}6F8L+ST;k8b zH?A1=LLctQ`0ZdFJ|g;tU85D1i4|cQpcbxh^pY%Ay~1MiQ41+7EONIRXM!?o3dzv@ z1+~l&zv{F1K`8_)lZvsbkB@og%}$p%g}_HpT;kq#!k^Q2s8{z9h+^WT^O<{aTS^wr zwQ-$%FJ<+IGAjM%Os20?+T;1`6n!21Hp-F}nESX-hVT;J>!D$6U>DkK2jr$Meap)& zKk6GHJ==`em#4&5cLlBkNkQqp8rNqs$l$U*vVOHZ4&q`|$9mZ&tBUghMh8ptY-fE1 zZ%G9Ao5He_f@rEBh#wjWw;YNd3mmTsD| zCtg+_{+L2i1KHcHUdkOcqx)@MiCL`O6A~)91N2u3AEX1!r8rJ=j&gnP`F=r1q&ZM_ zme7h=39_7bbYPN?F%^0)QACn1o4jtvtKUKoWH8vBcsk}PAXyQD@=*?QpR6Ukd0TfV z@S0wUh4ED9>~0?9e8EeaY{`}5ObhOb!^08G!Xi3N3_RlOF-pqnB-uCims7rBW>m@d zybM6>C(HL`u%idl7`HiFeF1o^tE4nuUVGx+R}%h1sdJQ;tynl@CCUzaIjl;SWqlz7 zB)y)&jR)%vM<;#N*=NxLm*=sxi)R;0K+05o@(lpuB`Gt=6SExfSrYJY%ffkx_fm}K zS?bOt#p-q_;Yod#7vyll$<`{!x7R(uQ%D$Tn}c%QYxA__H4v=;&0%87AY7wp{#{huDW@6K zB{rSW_?)H7z!p;qI|AWlgCLdGXO8}80#+iH%=(XTzIwM#{(Pd>#}flf7+EzJ+lvVA z=%M)ypMR7pNe!ez@5xiVA=~Uj{5l~Q5j$zO*q27MAxz|!g$olS8o$jzPgO~kh%-VA zQtyEQ1uKVT2a+lkY0<<~&TJz6gv065LQER#3aBHQU2m43z`uvUN0#A9QzFYpgfx-L z;u#1~6Pj=fu;4)EbT(bb_$ZnyTfHnQFfwrTRompw0JBWYvgB7kUOTER-a_fH_=!@! z9iaV`qDlo_72g@Z<^E#~cqZe0^e!$9r4ooI9N}(Oa2bQSfoe`_a8M`{@U*X4(bkix z1ePw?J7HDboywzTHK3}iLIYmu;lfKH2Os0_!);)E_-?{mJ?e7(0xRqYYfYALZ+W~G znYf>lT@sw%p*)MWaT!7o$CPNE=5tlm7-6UZh(@W)Znjn6y)jowp6endm2}k412gL* zdORaw2V);~b~=G|V^ed3>SqXyAreBO7Y>r7%N>H*K!3TcCbEc4HPT(uJ(BPdPPp$o zyBIn~P8>iy{QDE~mWwW1-=`A(x)8m(-kr!oux%bjb;$?CJP301grLYV60g=!6aqGH z6o*UgLS+zzGumVT-1wL);|5O1@bchDzK$Qbff`ET{7@<1s1>T1su$`5^?a#ZM_XK} zmr7)sAIR1RwvutRSlgB>mkHrks8{R7+CZ)`h?6-S)Kwd$p?tYf#rr(^Ni@`e+v~-G zG?f`|)3!~S)0?*a>P-FUuME+ITC%WdBVNlZe3yyh+c?O9(-h71M%&2Q<*@Wt0L_!+YK7Aynb+)yI z`??*y-$aa3{GrsdNfffdtUZx34q;0xY&Rng65$g%I+wi(r9@f7ILpJ~9sH~@BN63` zQ@h_4NGb1Fu!UfWm?2I%it2z1w0=P_BONas?-oceEn_PHh zBmY6~^+*RT7a#2;)kgEeClP%+1PxyZZ*L?_$dh42U_CUw&KrzD99z48*3HC(1C>a; zL54GTFI)(xbZ80p^}dTgb7Ee4=R(XPOO+8H8NyrFpugY!9o4weT9%9JH?}%e@D{Rr z*C=(@r6b`!(tbN>w})qXXBg|?J4cmy?}Hci^vYy-Gv44>Im)_yVRA+VUhm)k_2AM* zh7@_O|l)FOpiflm&0*=Xh*#_KYz;v^k{gP41H{EI2#>u-c0{``@bmr zgRjs1@`ps+z54D)u}%(vz`maxpV%$ov6Eqhnzbm1OpSEIm;=;%c5ES2F?s?pY-|VP zc(cnagtJYZ!NQxDZiiEcScMnSa&aK&e$tLthWbx@kA@6ZN8KmgcHc8NJ$p3c4zOfl zEJYaKcmbLt4zO*4*J2rJUYk#K_~(5pAPX|_28*n zw68jU<2UNBt}niu!#5^6RE8dP5U~=v8z;!2%hG^>V0y#>oq4*JLLarfxQ=`RRWHH;mWFhvkuvHkT13!X;d3;Jt+_`FsEAxjsdW(n z*a!HAi@ul=37bZPDSrs79FwNXoH zbwb~(rQ-57O7mc$jbm^{K>e-{CaBFD9}u~Zl7JVmuHLze2oe1i;i&emhDd!{^rIvC;{dNT zhYy3<=*tO}IqGSuNa9{*F0XHYh&I`j-2hK!TNvnaT5p9H&ff_qC)-D+reWMxndJRj zoOZMRqWf}~Uw?uZfXC7ICr+GX2vE2R#7E^Hps}_JFa$GwU$I@qMNS<(LEh0P?Ki(s zxUhLiLcwY<^%z>N#2ZZ>KQVnoNRRsjcVucVhR8crl;9gPeV=i_orQ%&%()uAd-u}y z@R&7*n%(bisjiRsuHFCPV$)8bVFXaQar^c)m@4*nHKs4&1MpG6J;*;wIWvhh^_wij zpXkf>%!4E9K~vstte%iPeT6=1K8FDZxcKhno8i%^i4)`MY@r^lL)NV;SdsnTEG-Do z&xRk>^YWED7s8pNv34EW*Ny-rH1dt|mgE&O{?M3HkTS=@eHU+D3g26X?Fz3r>=)CQ znYbqO%f_<%zSm?sHaT_p1hw8Ug8SS&XZ`el%f|hZ`4ZLo_PghgPP}TCZ@v8|-1jEB zJJT=T_jLI5Q~$xH(jOEbr(Vtc(%<=0RrH^#qW@GCjjZkeXI1nPCR0*NKka%7l`8vD zI!Q?57qKRLF%vjXp?deYUk$&6MVvg)IhFcyG6~6+&`nwX2xqIEpPfTqd2I6-7PK%)}TxgRe{a7HUMrWt4cgcBE1^Yg@(Ej$fgJk5~;gZI0Q__1* z-)ew9mn#4%7&PENq+2yM2BA2P;sLvhX)1NJ6Dap*DSnc=I-x79c<2b2EIwAQ*;GM8 z4ffAQ3RSEXhJQ#M7)%sv4^S(v(HpK&`p_q+5qz!_q+61J*k#Ris%SO2gbPv_N!P{t zfN$FJ&&>;{(>3005=WSN#*qR8s5%mj$vDLKco=srXbhdPofy(y8gl`vQ?KY zse9&IQ79n2TJSuDthL&Qew*O1kI@1}g$~|x!zJTaCH}}Gk`&-zQn*jb3kfEk%y{&g zC^0s&x_;zkSJq+V*Nrmh3E^1;H?op~L@r{)f#^lgMsaK1woh2H-7dI`a%7QF6dtMj z@CNz~XS3o8##^Q{cX78FbR%eLZ4|Bl>se489NbOoqPk#`=_Z%e1|88dY89?g1=eJ= zq@d0AYR4N`5496)O&Xs8h<~DPxrI(TikfR5ZSyiO083$ci1NUmjDZN@2pFY*54T3Z znxl6Fr^5J!8|u|=Q5Ai}NbSlOs5SK1RCkumR?p{{>XJTA5OPQmOm|x~zi&<4wI$Mn z^<*{)f&$%@#nRBXKal&b$9RnFn?Ua;0vY#^0SSs(v`cN7EUO|&$bu*-rAjc$k|9Ut7?hbVYue&lYtFry|)#e}~vSIC@f zqj)7+L*J};#qi89{ZP{M}^=`6;CSNdDrv`8=*;R+hN9E$noxoeVia# zfz#Tl8H@C~)e2Skr)IjUr-UrjurL%`FYR^UrY6oY5`n6^6Sp zD>Kz(18PaLQs+j4OaFh^12w5Uw1@_XX`*G`n=hmv^eGUV6%>d`jfN>$HCb!*>y0PE6XF5fmU(P#+^ z)iRpCTA?A&P&kDylm-YARVtb9rz&c{0-lsHBgJo3y@Xflaz0n6)e8Aav4)8&2CkJx zp;W=F6{pb^JX)gz1oJi2K!5lPafsmP+TSM*5g20o`@|ulGlc&Tn(+IK_!$7 zlYQfM=fKTu-rSgK4-e(B8HY!QGFuVv^fA2pc*M)$(!)5x7g2tbzfKq~3B?Sr?uYvr+_t5tCXy%#x~)8>%^6lf^%;u1B{qKQ7%SNF9Z>#JNdKcNFS$Qln7b!?}QD1mcdjsXsqJ)cg=!6$pPtItc0 zO;N90HWpZZbyUKZH(6jF8oV5LO-le1<5Kqd98lr;ZNIbe!sln~29y`B7+^%{7lhfd zqum_aZ3hFBK-Ocfw2yFx-xLf7zaBbwsRqv+Q>@gF_iyo>+Z`)mtj7c^VcnSEIr-B_ z57P((6KdoSlm~P5v04#?81`Kodj~jJ)b6hw%uqR(vtGMw`o%}GbQ4D!w=)xC1(oi? z*N#!P+D!UMgRZ!ietjb&8xhqjbX`mO!!PVa#c|gqI{ia87kSk>Ztm19r=5x9qqbv} zbzl52hUCv>#4Bro3G<6<1!aFpLHamR+o#)@AZw5M#$|7UxbO&|U0U21f^vdI(T7df zU+_&w$98N}$TIBvn(~)OR-A?QFstRvL1`c2`V?b(d!@j3_-fH9P_Hn~(J4ZgcN0E_ zOYVBR@y~jSSqzx=pUq(qkqGt|Qn_L}m)~Bl5Qo<|W~JHXrX34-RJX|kEE^0vwc zt<0gjPY$VnqxILB=wp26D6xG;%x@3WPo>4~8mp`NH|hwaWI5-Wdmd_RUZzy`JQ?d` zsO#rF9$2>puYisUXHB?6GXCBA0^c=}8$8`E?gy>e239Sb=%}~0C$c!ilt9InGC6(f zfzZ`FW}pV1obHm@+}_&u9ALK{4rgcizhzM&?DC-FwY7_Q$H(f2joH?l(gdi)S#aAN z&B#?}p{I!?=6X6RD8Zq#0RdNuZ~}LX1JzotQZ0+E#j8sV52%fya;`W~2QLS*tw`9E zMy@bYDiG48Likl;u@KL-SSt`6wU8Sw4CX4udYw2dMVzz17T0U}Qn64TEZ1s;Y0a1O z?do5+|6fPD-(S7P?)L{K>OsCUOU*8L36QzE!o@Y!orTJHnIJz?zLYP=(w?&Qe`Cl{_U`@EdQEs6%z);dsz z;|(M;$Tt_+)t#W%irJUP!pn%g-Lf$OUvbADdw};BB$`Y@yW8yL6@*%fX`6K_{QV%q z9E{GPdT=K#;jyk(k^$|PBtfk|GrBE-Omhw-jeEV*EB0?_aUqlRuEs+Bc>2w4i)=yE z=kG7C3X$Swwxt}zr@D4&xs31D?FQcRb#!!cX;tZ@mwJIUzt*d6i9#vEGI#TyuXCm? zb-jC%$UH#9OFS?Zr5*aR{YOH!;3DTxKdyx1L%$T^NH*D)lx zLfzYA0z*Y&qP7Vdm0*Egb4_6XUiVyg+n&lRCo5ySaJR&f*>ae6Gm~KpJ|0Fsgs{L! zhH^U3zUHV7+)p<@bP^!TU^H(VSKC^1%u5Q3#h#+u z;RkLfn;l~(OQ-Xx;0A9zJsrmU_bCPf$q%{J15v#Nrh z!$*T=jeAT@raZiYvjy}|_iG-D+4kL8ww}uVL;0W`iI-;OAg^(D+re5|UNxg;`nC_v zde|rlZ-HkK*UUlsOIxD5`!bP4STrAfv)*;ouMXLUU?*-d)&pxMxwb}*n@{_;b82r- z;7!cKkU5Oh$4&fvw=8yRl*Q?ad;!7)>FqPP6Q&0@>dph40o?QZJ%BpNm|Mi`;lvB^ z)DCWmcV@-A>$2Uc_sN=OwfVl~8chjX!Kuq%Y4p`e-+vh|%Wq)7K>f_dgyJ!L%G&*i zz8=LGulH&Ru^CK@TOO+Ffal3Uow_`UEGSjmztwG`s?g;R-Oi~NF50fCtFOJ}b0~O} zKO7sr3CV#s`2>+EI9|l>8o7T75V#aykLtJK(A z2}7Q%GzJNa-lzgHAHr+-02?rZDmF~E)zUyI$Cg^gTUm)fY6zx?iB6QX@(_R6T??h5 z%{WW17cvA#=ME4&uF}elJh>sC;=X``bV;g8P8N`Qy{ULL_4;pBM-so5I{MRH2+JHw z?l<1;qU65Ag_gmd95Ve|C^>t#!Fkqy+K-a^J)z`wc2RN;K!wQM{E2)U9CykcKL5YC z&U*Fp;(u7Le%O;D{!63cSozKaR=c*iJyk**qT2~`r z_%1!Vti7~*ccrJ-=sugl&@Iw+xMvt2;Qj{{TdZNzW5e#s0-;aC)c5>)SMkvI@KU7u z={*9%-S7V@%JocmyH89Ws{HPoyBmedmX)gum4O;)-*!r{4X?Y)qry4*r7I_*nDF9JATU4Co{Pw^_XK&Epe9$`?#9z;?z!p;c$< z@o-`OVHjx~KqP82kt%q+=Y8(gU;Mqrq4weMZrA5q*JLDKs^Af^)#&AHRw1qpk(0WO z?PE5_vU+FNA(IYj+cY zEJxbN5G|I|7=`=ZLrn&3FN5im^uDx8TJfCk>}TL`YF&Gz?-;F?yb z-R}{>wfqEg0*-=0NPQm&t_8(I`5qBm{q6rg5M0cEgGzm02rix5{ul(8+=jR<0$1=H z5@$G#ceaiK7!Wk1)xIxEK?ccRKXk1O7*Kv+`_OC^ zKZ~6MAS4TbY8ioApfR@oGD&Kb;s1$K=5_sSf+pTOd_;dbTSgPSCHfpm{8V!mrX<2N zcIrV2izoZ(xLAeu`%WI zr~lCaVs`8?95`~{R{{nGIAW1otX&*^^X0)*wtPE*B%+ZYwopb@b7XyR^X03F9V8eo zr1Op8(R?G9F67E`oV6#MN*~h~$J)bR)D_>0m{~i6g+RSZcniNHo!po`od_lbLt_N~{xLBzHA3ha9_gwrS@y@=xQMQ0du z_DE%UidKc-7~}Za_I@N6BUY7qv!BH*2t^J-J);apgX|i?&-#nl;%CufAin7V5w`|; zct<2YQRrFAdo0K)ka9Z?cxw;03BV}vm4KVGiebwNM85Xa98EfhLy4!&&6ng4}sn#ybg#yn;|F#^9>#U5Iv2S@dw6 zyFn+(*hx$5oKm3Vm4wT@5S-D2vniaAnC3|}JQ}1qJIE0b_0sF@EEg8E3lgDO+U}gA zBbHw<43tduZ9gVBGUB4x@t8i`140pN4(v0em$n-3B_L|NSofvVGDURoVWr=nNj{_?7_r*e8O?4qOx(Oba6;h< za!<`s+-S9+hoi$={8Sf_th7gjpXPMZSLl?yVIa&?pbs})KC^I1LIE?A75Pm4)gAw% zf%Mr?P+)7wu{064rCvO*BHl9jr(KR_z3vJ)o`zl^vy|{X>aFR#1*)|?PNchT-;~M8 zAaJpO#dP};J+}>hoL;!5hK&z~>IMtnaipjx>4#_48FSP6oj#{Wrv@MC&qrh9diKG1 zz|A|s7Q$%@UfiYrhk}fwxLPe%ms4>Bal1R6v9%pznBPWb2{rBOz%xM_0CL}hv+1Nr zW8BPl{2ZP&fK2wyIz=9(BTUaC-1&Qt@FxQlO{lc)hcn6SG67@VZqRmhJMU@})$~Fh z>1bTeMHJ1VwdS#Li>R*!{TTO?&ADbb(@PfXMf34fkAfj>DWYAQ^70HFbZu}tsmBM? ziaN%G5S93b2uSV6(u#-$0@=4VkENKKEXh7>g?UaSD#&wu?@I_gqnxrRvQYio60=zW zw!!%YXUio!jum(c#FeV%g|_2G`PWi#GR?p%@*LLd7@>rDjqyx}S zy{HNCNIPUjSKHC!pbm9)B&dx^xJA1M?;Ren* zkc`$8qM}eB9z~g`l7(EMgyvGPN^4*kHZhNtUa%a;aM4dZ2-@wlY|2G!X5Us6jXau!e$nkvS0ZsQdb>e* zn?UL?5}P>xU&tB5!x)V_EI7hP7y2Oj@cT7###Q_;GIB@J zWNA@DR$u-6pT25by3j=iVWQl_L79E>#eVH*QxO=X!!ny`6UezN$^O;M=f6ALmeXD5 zxd#D~+?a%OO<8uDB-t8IU$6?*>zIMmQsSn7>p1*z88vPoQex>70NzVr1n0QyGwg! zTd)4zAN|gNoCv$NbD?&w3NwLwm_-DPhBUw`Tj3(GNM1#2qd*II8pD}Hgw#46M(*FE z%0`k$%gdbdJLK7TcsE8e*mzv-!!#iohsMPHg~NF3>d4~Qg=>gmVCqWM{zCV`8{HYt z2+GI)x;yjLGMTn4Vh#@8C3LQ~0oE|m24xEOt@eXJkU(DT!lJCg7kVJFKVtUCXR`uu z^mkRO5Auba6qbHzbyVm$H(2q^vG4*|06%{HOaJiKyyGUU zt@MPojwCv9Z3cns$-@)JCSU*lXLtPJJ6+m%D4GY~A+P;uh`z7-Nyp!I;Wr*lw?%tD z`A*tvZgL(wg;}+mv!umhQ6iTT{{#|Se>CG%KbpnSGIEwET9$Yq&=(65*oR_i^{_|# z9w>Yz!xrm!G`1#Zk2IA^9ZzbF&#SMmr|P?0j*<4LPppp_-SZIB2}OT@)%?Ai4WIA- zl0Q1~`fvU_|9zs2WE&q&5u62o@~)QX8Tyq2Zh>RM7QWv88~eP$l+EV#S5N-!zdX=p zZX%a&nOZ?e5I$v7!6AVr40GEm-&F#BM_Gr%8KYM3ITVEXsF|i~$c2`=c_t?(&}Nm? zpEKh9HUJY;0X^KzINpMKs(VnZ?9?+3ArE8v4u@KYL{d}{-0fNDW49>?e#)kRC$ zo>?d$H;Cy-x%c|#2mecNxP9Zo`FGuDMKOM;E+;os8tb;eZyAI@D?zHRKKVgF~G-Kenr3O>uM2LQI$n5W!a;fW&-(Xc-@xb=b0TN1Cvc#Zr7nhCLEb$k;wGS+wgCz#G7Z>C}h@N#8|Oq(?g31iH1Mmh8*j%(QPf zo$vOG>3u6Di%GPW$cfA13xXjhRQZ_5--z|6lVH zvn_XgXmYlZEp6vWV8|04ChiFA%hAT98doBVOPy=36ZC98I&0M(%*l>b+wj0k&=<*o zWO7?f;r$n0$sLAfkuA*;fs1fKD(oG^V^_)tHjjaSwsV^fE~&gHc%Ta3A7tlS%Vw=6 z!3s~t0|Yuzd^D30p45qGIpaRpsrtQ9JLl^V z3=$wobtXJklK3+pLF?K&x?aIT4OO~32d)SKF94Bx|6O1|NEpF|mPZImEHtY6VtbO# zYTPLgr{79@Evlu5bBc0@!aAx~67-df((gN{mV}C(YSK4EvQEe&CV*~V@*J#JVuaND zfkKJKfe$Xp*0f2uQQ9D{^)G;fEee0E6Y)CU{K0^qQQt0I9s=!Y z$NdsLo~vvg@pxF%nSQmThJDuFwy#w4xgXmL9JIMOXU;v-fDRBa!4Z$L~%M3`YhP>iS!GzF!zN`^fWLc04*C zva)2(joimiENp|O#v+hGVWHkG1!yeG!J)$mt`dd8$s>u)T=-ja>GaOpP9B1k)RScX za&C~Y3QdI&fs5@t%noBvv|H)8!LlkeY>{ z&FZ}}z4rqbXtp64loveEAODD@{*Yk2=5Jixgu(%zJBAlm15V?+Vbz2cT3I+JfVP-u zjk{<p0V6@S3%_x;P0v%19~>hx>9m3@ z)o41~XKpF6-q(eUjxBSoCMD>>avD8Ee6On4bDr>@dUqv~bm{uzOiFakvgWpxdn2E@ z45&w}{-VhTLO-WaIQVB;TO~rIsxwwa00(c>?deY)&e^=HJ_?LXH^3sa&dr>O=8&B7wF9QJKKU+q5H0 z_k14|u50Ouq!yk=pHSmqen6STYwjX6L<>f1Ed#V)HFPBLy2vA$iTZqu+zN%k0#<*H zdZF-epjwUU0O8r?LtV3Io;`!r>qyY2$rMV9?iP~tQ;!*GN!pd^fuy-#x76yNdw{&b z|MX;psU$Q7&(2ym*F{do+sOc+cvRiDwOBf1$?Qt&p;oReOO$WX&m;6-;@IknR@0t~ zXl>1={3n8+sgU=|y^{wxTRC zvaiIW0Y7^(w#JRF0;8v9!)6kq6*xp47x0EC!9%nV##7$1h>8;K4e(HbhS1)s1s|l6 zcvw_lOQ^btlY;xq;U`*uMz0_;5Oa+u?m{exsuepO1UhLr;{Mi7FNt$&4TZAI`>EKi zft5Ms7iIhvIro+>L!(ESU>7UXZP{xgv1?i{dO7L^ZT!xYp$6oz58*nR%zR)I_iQp{ zc|}Q=8EM2HviPzJPqDp5o3y_DG^vOcs}y=x8^dTN=V=`n9Y2}OtUdxwW|}5@QgdCU zr0vde0>;xqBPPD*Hx*h|bf|LxkvO%(CaJe@%7D$O!U^7QD<+d1zqPwG%-#LZqCEvS}e zw*}zY5~QE55C>hxQ`WghaQ=@Ht49hn;n)4_GwC1QYSJvd?v)nsG=tYX7=D+x=H^X& zfw;LQ<{;~rBnXmMT$Ho6yKCstP~a-@SqrZtQRko9X7FblhZ?ec>jA4y(xT;XPIW73 zI6$3dK$~c3T~*DP-Y$Z-I{RXPD{q_bx_ir%1qq)4I92+Ru)4%uq|Vl9ZH+WGGN{s3 ztuNR=PXe%*c7`DIj;U262#qD9iSwDOG#`Q|wP)lmz`7ia zIRO(}rWT(d{dr9H%oIdZ>AIIO2SY|5Z5j`I1F!zke|BvE{gb9WovQZ1Ctb+RdH^+!XZ-+x>hSWX#fr4i^M;lJmt%PmEeGw~6 zcP|T@#H)|OzkZ1>RRCr+x|&QYf`!xYa(^Y6k*JsRb~ISWH#VIl72>Z$NJKr(G_ZFX zO{Pm>2CpVg3}{)Y6Rzd`9!oOmV`8HNgV@scJ&qUrJz67j^*oVl4XB}h`g|YJ+_Ab{ zih&$xpd~kK%|>KxE{Td+D2RBn+(6k1TR?3!k)Ipu8ZCn*W%Mj#7Hjd4pyvj$rR#7p{f8|ZCvb7h-YeB{`i z#8=1CyxnFX%$Q5FUE3Tx>n9@rO)^84wkgYW5L1<{ z738u{Qjsbk6hWe>6j4M(MO=_gL|hOTKt%<7h2Q6U?wus?`~QE>`@H%-@AEzneR?Km zU%%&^?|SaB-dlzr>%D&XiQ(2tk7riQah_{Vj-Sm|-n;L%X~tu|-5!sp_RjnK)mJh5 z>vJ{?w_o|?c_sG7%QgQsZ_HBfdvSWB*Dk&*SaRR)`FC|{clv{`2a)^C!QhStl=SG0 zrV=w1Pj;0I6=lD3z9*fO1Hp>*AcA3-2erF#%yqGB^O!08R zA_@z8JlA~h>^R>`?U(-Dn|ZX{ks$Vx&GgtB@# zYfIF56&7Jy_4H~*Q!qx2%RdV5wiGsuiR#u=TW6x9$W&MXLM@55f`GzCz?*D~w%p+tLUiR_J1 z-InMoa^qWL&9TM;IZUPcKrG@$Hz%8#TS9K7`%~@lfT6GuW+mZwBjc&I4%4YGQ{9m2 zGNK9_iwv>$?pQ-}tTTx}T9LvgQ(PRQO3NW*x;qrvoT&c6gH^ItQQbAljp}T!aA&q7 z)sk#XmbqhXPjnyD-;Ei?0BJl1cZ+jvZf`2{v+Zq!A_!pDErPB}ZO!77!N=O(` zxjUJM+f$<)ueZ80)mTA2K7PXuy#Iz9MDyPiV=tT6ubxnLGj^Z7_oT8$(-rM)?KS)M zlgf|#Fa4y_q72isy%!2kftn3*c#lf2kG$RehOO*i+~cwLU9W6av~2I@{2`Y>eNcxzuj11KlO%QdCgO+M&&XEPjPSV zZ1gD}JU(iU0q2D?;e2rZ{!w$RQ77#5_*N*OWJhHS?d(_Itg=tM$qhU7k7#j! z?%P)4xLC%1eq65$^y_uOcV5?mY0oxZXzNQtpEKAu*hkrJHrf8tlF)zHxlN&%efOr& zrvAodA-|f+~H>#a)v-~He9_xTU`>--b_itl^APx}d8vXi9MpA!R@70g#TlCS|TiRE&PiWh;O7)NGSJaQG=c-dxru*eU#g;+x0Dc z+G6{>>+653j1!xAu43M1F-qNfqE@upWjEGWdG7heo5dKu^(uSi z4fPw9=_0{%e|r1Re6s!f8|s_wr8m`2>c9WS`Vg~Uzo~wI|CyWX3z+@$TkA*nzi?}P z6;mdN?L7C=$8BE4w;E@!M9(hg51a|HB|dMVhx3O#{2}jS)bFGGc+a0h{XKsUzuSJ@ z*Htw-vu5h7+8J}E&zMwQJ+HbtTb5mIhffZ#vMUZm%v}12VA1}cB_ek`SLtC-uv2Ue z3wfURd=?8uZ8mpyraR_Mo0e#sdN^rMuQx{Zzx0=AC(E6w`vR}ZEttDoMEX0IMX&mN z#^agm>GLQDlv>3vz95c@l_J7l4t_UyL-1g5K`%FgdPkFa{3yhx_IpaKInEpfk3Vo&au6C1FqyAOBPTi(j ztV;PTdySo8ZJuY)Q~GC@RQM`Bb$0V8f>m$s;gULG^5|!B?1ytP%SSr=W!!VMT^SrP zDR=7~=ZcX$+HSLpOGn!$Ru+5hyH^(%+4s&hP?~}h*Ayr0OMVp@ed}L#iWzp_e?+I) zi~k-ixBK4EN7}zYp?HK_KekTpb066(3j6=K zq4-{0!Ia*+saUs%Z7Tkalj)^R#r|AirzOHRUr{`#{}X?WeuCM5T2?&CUfg}Uh^xEo zrRynh-~39u>aFNzyHbppWLJw@tL&TKjyBm}Us*gUXWz6B511dHaG<+;!kyf=7Wa9H5`fr|qZtrx8ptH%E) z|0(}Le}(UP-?hHw=AX>F&9qtLecPM!t~7pUTyAX8-_sw}Gx}PcY2Vi_)+VcO;P#EH z!<1*0>y*vnSE5(!!8HGZe~z!?I{OLx2pi}50UC4uZBw!nxP9Gs9w^IIm+TUzee3tt zvGxXaM7^E+%A=$0GtYX>+|^jTX*SbFY{*r-wM8iXHTRaTWBrx)mCj_jFZ^+e7;QiN z?OLy0euQbc*Zy87!u{XJ|YM5#URtEC^eQD9=O_s=^;lt*p*^$nP- ztN*l9)b!7LsPtRTJm)Ij-YJUuZ~S8E>s$iO2K(XbUKyS1&2APIxp$9k7J>fDR}_Dg z_0$#j)RjC?SIThKtDZ%kn?2$&aiwjfOUK&P>Cz3FR<8b9J>7pm>Q=Q-c|kd;tQ7Bvdqg7^=BNAyzLQ(*>ny|OdfxTiA`W>Lii_PX zZ+~U3QKD@~?o+Z$?al8*$Ju+Y)@SzrbWQmLJ@@tJc8amNV>K^v)jqSTJR+z2*eAD% zK&}G6zW&>d5xe!Chf8}N9`?Y)!wJqF^vv`e^8kl>hFueUAeahH4g4-}dmtI8vVLRT zY{jif{-5|8{pG%weK-5|ns1qpnCF?A_X+Q1o@3tm#@~$xjI>dyzlZ}pu9s?G#8K`6 zye-C{x|JE?IdO}a&40;1%hvJzd;*$#-#`0{b(r!cp9`9~ebGAM*P@?C`WE}%wXaOK z7cPEcq_g+sk@&svW)b4i9(yTUH`?B(f6}shQ-8H`neKDxM7i7U+ii@d)6<(<^3R>3 z*zR6YzSWr$`$S{JYo9q|`uiJep18#8##X;2lw9Wdxqv-ccHgSvaz|5_}%UxLoYsg4n{xqd$~V;AK7we@q171swaC{yXyZWi*ftx>n)3o z>5E@krDQD`T4I}G)K8Quu^x!d)z9;?+!_?xk$dJ_y=+si@1}CG>}>1J<)WG87HoTl zMb7@@kzO{OVeQ`exjh&v)c1l zkMcd`l+uafzZ0JkhwQT6(T7Ua+tf~V1zW26aJBq|+q|9+XFp>(kA2f!p$W=Zv5Dty z#ywQ2Z@qB6k}c-BeG}@$N^R@WNur+T=C7&~W3{c_X!woXxyUz}Z@tLA;EvFIyX}t9 zNBYk@HF_ntcP|a?CQLeL`|b(N%{{yM8CETSryTG5%xJhOxG`{J;l{y@hnoO55pELP zWH`z@6>b__HQaQ#n*P4e%!vQ4Y8kuH6MPh4v^U6r1l$lfFHmYd&wj{mw0f;ZYpnmL z{u}J-6EiQjD=K`i*k>vxkG79RH~Ef#`{YcxTDVzov*G5z&4rr>Hy>^R+(NiTaEsxV zz%A|n_Q_@QUSu9yq?a$Wm!+3qzk;s6n%Q#(SguZUf13K`jO>9o!4#dIkvp#*op^^tyEr8&h@*HczCWTvC~g28f93oS--O03cj3M^2l5Y7Y|dv>3o@EmYQR*>)50{G@h-+cJ0r4I)# zA1i%x;Ts`+R3ajMv*9zOZ#RB5$RLm>y|#6(WBBwGn$n?n$fGJk7l%2&Mj#7+RLO5BlcWjzr1nv zii~HKGa$q)$PdUTDY!=ZXbP^C zzS%SfpORjhgIlGK=HS!PM|1EQ>7yyQOZsRE?mqs)rqyt3;MT&egInMK!ln&l(u6(iCpvEp@89vrh97Clm0Mq2e0<8|8{p1?+X%M_t`2T<|CGnK{Pa5ZD_h;S z^#FU$Zriu@c5WQ%FNkfunf2e_uyu^edi$Si+Iq91_MQC4p3kb6sf~f1 z>RjbF$~Tl=Wusz>m&HB4-JlBB0rh-?e}i9#yKDguvX|Kx*~i!pR^|C~us4_pj1SHW zh62w8KH>A5PvBCj_P*pj;oS?Oe%v38eybwY-aRFrYD{!Ysj04+Rb5+MJEeMSv(f9R z0E3AxW{-XT-uOg?VseY0+a*f%nyo4k-1a^7YbN!7WM>?7$1m&S)%Kj-@!J0PcE@Kk zJGUpkS(|qak?QvInXWOscD;SkdGRUs^XJ9K*k9Tk|BC{;p4)GKdqcJT)|U8Qd)~?V zUHxA@S#L4L_pGNlckkJ2c{F!-?{GFN_qE%Gvx&LkpBc`&&(@tD&Mso=IZAdox5IyZ zd^Mkzwr|}XA7}ed)=#yc+={+hH?Yf1{_MG;l5Z`s*Pa)j zp>9&L<=nQCr`Os~ZHv#b7j2JEv>)0YpQOwahq?Wf@k*^-u`@msTh22zcXo#bKFC(B zr?D~K4@A*80-MGqD&z%3Neey5*sNQM1a?)kla!S28)3aH03RWZ1R{!CT;(n-b2SkD^I z{Y<(Vg>3k=#>@qTc4Y-e#{}KHTnpX2Y|Kl}X3%lIF_edrs`%5%GMQ4hPd?lP_(SNFx?8vE6K ziGMD}W?$*~l*gXjn^;lhn`XXaei<~}a?|ww*n1;DeG)rjylH&JxQNX%Rv8ifCw96w z(O^%>)~fa!6W z>=V~^8TRW_-gGB<-#hR5cx1dC+u1hOKCkoLAdd{UpQ``#Xghr>q31TOohtPH^`{aT zsiarYaKyfQ{F_Vry`M>3Cvr=M6@aR_CHHY&WN)1EX1gpaW7XUX-BrTdKV|BhKLXF} zsg5yr^*cpH-1BGqjTwPa$FI6G0kT+ z3B>6u;Gdih-V(ef_=)}zXD+{v_uv18%a{7u-|W9VbosT4_SdNBzv}GehfWw=UFGps zsjE&d9dUeo-4$?G!d(S-HQWiflW?Dey9VxBxKF`d2WP`w4|fCHjc_-?-3)gN+^ujq zxL&wExKnVShPw^!GjO-Vore1?+~?r#fV&g!F1XLb-3@mS+!?rg;l2QOAKd+LUxa%A zt{?78a9@Ud5bi5*UxoV`+(Z52>&`y=I<7tNA|Ld4`}u=(N8QcOKKO-S@PBH`6)Up6 zXTS30U+}fsai#8IxUa)K0{0ELZ=P1_9$k{L)TJJEY4F#e*P#I&2rE8w=s$WN*)$t1;HZSsOB-)V>9RH9FpnW4NA9Lpspb zi3p8-+gjXm&Uq2ce-^_pS0E|r zB#+*jXivstZRBV4D_EwH{)o0@0)G|J6>Gs?ows!357*l}lkt{B2l>s8j#NAe5lc!I z)H~Z#ZK+n7jZx*o+nVY~H&X+YT{#?Ur>Zrckbf9e!dQb$i$PdI9xa*5w4|D-62*{$ zu()iW8<4gfJPbmZaxqG08v5Plv@IZPp#&q(sGxwJYH3L{$-W8$a-T%Lr@pq%_GCjB z1!W)f##nbV1UOVkO=Ozd6HaBRcxS3T)=2@TCt~ew$+jlhN=x!+tRd0aOaWh8ygS~K zN+%#aLs)p5AaBE%ovhv?ar8OS7N<&tnMOh@mQRj}srxZ(Ieu@VF@cukOlB}u$wbTG z90`6%_J^n1sX@`6YQ%cWG>Q(bAwB${J#h&(CRNQ<|00cAmo z5RHi=_{-%oaJgViIndRb&QLkCB@siHI+~MI4HrNFC|YSnEIdMMZvq@roT7HOKuATA zDv1VV<=###1jZAm5LXh7vYUzmP^1280&_$qwANI6Qbuu+l1*?u)78?M#A+d(`5_`~ zPj$qT?hJA*MM6uNrln#BTM`bq$)%I<%bA=cv#S&0&9+8o8JL=mVd|Z}ppWF?&9cur zWUT;VnjPJN$c(o=6+d_=iDjcMIP;?obir^U6i8Mnog3H#fGjzwx&%zFq#+rkG_@1Z zBPWC>Xw8Jy)!6NJ$?QzTo7++@u%kOvLhxh<%|B-;{4x#uxl?WoMVI@!(*gX$u_i1% z<>Sqik*mqhX1T&#NwvzsC|p8<;Oz&gCbb*zOFdD%n%A#shN1g|el6hDHO=d@EX`+F zek@b2hVCG_-vz~%@=Su4!zs*`;S^gLO_xO*Ar~Q-lFX|>q+SZZi z({TGFV(e#cuD{5JWNbq22R|Y<+}2W~M_p{My`g@ceOIo2+YljH$yUSYQ91_jXB-mP z0aMyjxfgOT@hW@5{Kq%jcmLwiDRy7&RCNY3m}pXW`>-Ie6hO&Nhv-f3)cFf8>td z@)G}}0O^sdgut#iH~&FM7;+=vpCiD8lCja8f8M#Ggm3w){r$y{*NFC(M)FLvpPBji z#kuF^-oQulX}bO0+Q*OOPTT~66n`$wj3RkGu_{m+S0&f(L>z`?VV&3C9`{?|~7ugpsczld~WWnQ4^t|zC&l}(BdE>DM-uO0{ z^Ss70g;^ecJO2pZWd0sx*Hz|bbG-Ly?+xBP-ZJAQ%rUM-%Y{DjviS1S8G{{i_>pLhr`u?npAZ}T3$f`jPyOcm!3&_ed} zFF#uC@bK=P^YNnGA2OT3e%_j~+2=y@M9s2y$M8d``A#rrx4dG%@tM$eF>C6}j;D6&FQljc$y1?jVSoPi(4L+p zkKexJJ8xW9@lh=^6=TvOT7=)@0prKx$*p_A#T%5`|L^#-&|?Tf4FuTEX%6%xivxtQ zBb?36p7z1lDR}jCcqwVR;L~f74big&pOG(7EBLJ0GCIT72|jnGlVy&=W@S&C$h=db z+Q_$u@F-bXOC=Z85F5+rxWdqeNo`C*8^}Uk*}qs}Gu-IevNGAh@q*V-(@+q~dZrtw zb&V|U*VuVXRj2`(Zx%IJBCGHr@3eg?LqwCpsDISd9NA#00z~e#pCZO^F}=49eff>4AG zw2Ca1lsTl}XS{|sLor+tjZTx6@E&YS9d1c9HYKvBX<$CVTG24_&7UcZ&g7wFXEKvO zO;kS2eT}WjHr(Wi_5`ZXk*#i-S99rV=UzAenKp>r&m!h#XizU|YQ{Wb zMc6K(wWJQqn!QxBE_g?ZCiB8CC}Qq@p`-V0xK*72Z}U1`GAL`A0E*d-(Wi}wt zW}p=|B0CHkRKS{We>+`lpx|QqX``QYG=VE6+MUV$$5#|FZ>-Q_EkF;DpJ2S2GR##( zTQ^2UUEL%R^Gxo}M-*Xagx;3w!pza)P;a~vb#~^liIz^EPDnKRO{oj1$vr~tY)-Wy zj;gB^3_j}nOq#L-)aGLDOG9BPE>T1DgJ5Wy0qBfmYZbK}+Ei$cz+}&GD!7Mh?Et7` z$^}qeumsIr_YX053l%`+X`0mS<5ijjTF13O!4hr2e_R;%3k9PNxyU zMU2Y;T|@wBOQ?JEsiPx^wwb8VfMx+W(FVoFDZGTbww~r~l~B@&IM$c~2ZeWlazJeu z&hYiR@PU2+aU)xF`WY(&Uh2$Xf@-<|tuj_dHP55)bZ&G(Dj92`M&%ZrZ8D5R&Tx>6 zL&-zV)Q)qA4;se#-_^xJooEmWy@}8ijD!Z2%Y9E5cV+a3SUdi^YdlR+n}ATEQd**k zLV!+jx5`rL$2x(*Z!xJiOB5h)?(tK}G4XQOO{I15(@&*P;|Ecf1NOTF5Hz>f6*QL} zR8w|RMmP{HVW?K9ZHfI!%z>9GP?WYrr@K$~0R=yp0RHP#H(KGeYShWu3U7BoYN}AW zQxs22eSmv`Mq{m82B1(CdJFavX3$xfN?~MDafgO->K#dgG<>o~6ALvxTcYT|SqY6n z4#Z@uBZ>;`!+5iEDxJrXjuVMGDi>lVa8giym|;{^Pr$oP4+AfC7i!Ef!8=iwMi^v9 z1~rZanHg(~HA$$XCZ-FOQ~fkg1v;k_jb`+Ksx&5O&S}`qLP^99A|Q_qQvfA~Zlg1< zIH0=iC{~2l=@OxL9U-F3Ex3~FU5y|Q=y39D%K^~nT)W%(8A8J`m*_xVIhbjJAd)6! zG}X18el}5XApthvwVNPm$qpuVU?g#;YgOC}7=`*GCf}LXQP_6r26V#75EcZsG^B}i zQu`DUYeY_pNGV!lvQZv*w1~@v(%z6lW;(sIOB4Z8(+$*ca2*o9kwrzpu%f0~GU&Hc z{Z>V3PZHcxA8|o<%yoLP5T|MWgp+sMI9*`-A(1Nga1GZ`7r_$U1;eRl8vu0)aDm;p zR<1V3+UWM7u8viV_B4tlsY|AY@vjgX6bB@z(3wyyJ6)?Oq)LD+SlSIu5deIPTSJ;4 zyn}j89S952)zIKBs0E@JG?{a_lya@5yP=Cfh?agg$F=7i00!vDW<+BI8Jx1hz&gj8 zx@fIw`o?OUdP{{4f+ql_258zMI~^WN3so=ZE$6I7cIv{UfIKL1e-s$mB7=9L+cXa| z6mJ?tpX4B5!I5=FD?!0<6STS$kzHA-YT!8}Xtz<@M|F0@9n3maNy&qRrmbA{wI`Yr zZ5<%qDK8-gepTthzC=woO}I@|WSpB<9+e|;RO+~A+S_PFse%G(xdaClv{Nxoc@Pd$ z^o}G5czIeOd6i;x;sU1I+}WmSc@NSlud7C$8{!=M%Pkr-L3TNfHN=dYymz1zioo^i zu8oF0f{B!X0!`C{PIQZoqaY!VW18X#ik6lP6c<9VDZ9XWK^=6~ol`)X+oMb9ceV7_ z77~CK35H{vaLI#;;*5Z@7*pUbL5NeRTBQ~0 zQspru4;$y^mM8WGdGOQVR|s!BDY;*SGs%gH3RhduOVw0qksyh_E z3xocEg%VcS7l~TF5nq1mGiNsU&`~~A!rkS6V)?tOBG^oPMt-x|cSHbYa6+^=uwT7vU@$L>F6jb?Q;GZ3FG62apx5Y~o57ja`G@gM6-j%<6srZyx z@8hk@O1K!pUw2v=xg7Xg`)DxWV>l|QV8t4)ABhpepJoOTMJt)IKbFjGy37)V84f-= z;xW15g4#mnu+a(Yp-y_a3VRh<5TO;4f9|AgWZm;iP+&cOgm_c{GgW+-yCUZq@*ScuDO$MHUpv|5j$$Ea?QYuuN6F#FFT6? zpK(XLl=}d-xKx`{kR&;kba16PNmK{5yaXI{5XQL43vpjpS-}ZjMUpL)7-9O+M2w^$ zPUa(uAJ=3cV1~?)FA$7cg=R1i@ka}y;czHp20{VcQWj!;{-EU#_$+@kYDJ21-}xgZ zZY?v2lmaW_>lt^ydxTuE1sB(!wCWfM?y{!~(5eL{3Rol3zmWJA(&r_n#OVS|NSRi} zC6Y#&rwx$u8JW$`4ItrCUgwlMhwFzNS)LPK%T(!-jc*t%8#VR z*<}SG>@rbRrD>8yLj7K(GGAK)n*-Y*NeDXCG##giyAIWgLLwHmsZgyjn_`(Z2oLE@a0*P8$Tp?UVp=+p!l~sX%;Y48!kH-XQ_3*<{X3PSw&FAg zZRoB>h?yM-wX|SZv~b8Ud~mN8U|TL{9OoZTxNR%|h^G#_S;snZE0m*6s6slV#@l22 z-BAt`2Bf8s*3llInkR7(j}8GO!y~!Yl?J-+<}YVM1YA@n4hk(elZy1JH^%`v$nW=GcJPe5X+FLin`X(trir507SA}lh61!Hu;H7q$0;~UZX)tIn}~dc0}^j1 zkAGlWM2nEDn?+%Oissy}Q~N)a1^0!73RkiOx}B8y6#N}2o}7d2^00s}Nr6k{J5 ze&01nbu9V7Er>W6usYj;(nHR6An!z>)4e2@h{92KKad~S0CkGUVk64T11V6?U`ll0 zWTl1+Ml*$^R0u_A2NV|@5WUGFC|r$Ohe$uFsEUa;0)6t2$%8%xT+oje5a@dg3sud_ zeGn55!aL=v%ovieBLA>Kh^OF$_ro_uEfaK1CF2srDPkPcU1>1&l;AWl8CQ=3(v)E; z_ofE{m0~KG(kWq%0+U3BfG!H)D%M?~qj)Z1j(p>pei-Ji&Lm=H=Bfa}plODRe3n@f zj1>5NA-}I6YWn?Fq`()9f?|q*>@a)Iy~~BWE1@te$_L;sf?9(E{O}9~Ax?Wq_wgB&BBgPpu{BoLFYnt*tS?u3)IU;u)tt{LGE z9_T2E16_q2KaH7}?XPy>mnw}&g$AdpB`mMhfG~_%nF?Fq<``HivQr}*P^VHmUC<`K zAFN|36mStOid!zhojPQW9dgnmDZ>^zM}5RkfIfMGgmTKc9)_6U&$_cZTC(G*u8I$w z{}i{tIseH!Kfehm5MnwGZNNNDHNrqWfQdySv?s;{hp7h75IRQ9RT*?04DJrfKHJ$G zV?uI?-2@2AF?qbgq3NLf{7;JS_o&}k*AEd3GP42zxI9mgkomB z|HO_2fE^lRTJ`0k7uU+zi&@`3cPls63Sxx?da_1s~HD}1-ACl|ru z`RuZ$bHyPeH)`(79N>DqHTi3}-}JX8U$Mt3HKaBfIPpqCeUp8eebjD0@ycP&FSnPz z{o9JO$6!C-#O-Velu3{6|Gt?!@$4oMK7P+NufY8l?p3(o!TlcY4{(2kdkyY&xHsVb z1o!9ud#?G*<}3V?W1%#9jGrrwx$sLFUXs}^Wwc!Joc$kRSb$CO-z=8>e={tk$nHb2 ztdtNFU-Lt;?Ek-5Hk0{RG$Eye*uSO-nfX^VA^#1EkQu2T_g~b6BxW^fmqEqtzp4nC z`ByX{{|$WMMcOAG#>xU znvnknMaT?kLS9w+RhKfj876XC4vI`OvZslDyoibEq|^lLn_aMki@CMn3sZv6(Tk$^ z3L!O)ib6oZgOMuS5T)h z5vp-RBZU_s>I>+h>}=sk;;H?^k}pj@Jgo#=mf9%o@QoT&SfUPOON4hoVF{U#JwYl+ z(zlwcEe+WJz#V1Ya);2NO#VEf115+}D|R^EMFAkLBeR}y68DxVt3e)+E|l!yFre(@ zN7I2rLzPHmg9BV|$~(^(Pih?*6a*bHLS>?%0X$w==R|0E$H6&85S#t zp9an(36?3zfIf|@MnJ)hssL%}Rx(|ZMMaRA=yC8arJS5H9f96?Yg$TgQ3sHvO|IG$ zC9V|aApPW4bPm%R6Li!%;q8;SvcG}kaa3S4_k$`2G1>)X2IBKjH$JET!H?b3o8~l_zAg&c!o@e)OA1PB&`{@V538G77-IaJDGV~V{s^KC*)XA6O`nd zVn?OI2333zQfcBmlfTV!kvLAO%{v*}2gCt1oR)C^oF;n;pI_>DeCNG&yL8v2dU=RkSd>K@6)l-~6m92HqH zC2SZZRH;xW_cf(MU;{qQa7_A5#YP zZYOI2Uc@8Y0EEzmxk!>y4hqyNkW7$x9ij|KEKDmDF@wHv&<9Rz&~K5b-!dSjF9=x> z%0~(;+?NqE4Eo*lg~C?E9}4?sK)!)^3k8B;qe0?N)ddT~1(67fLhug(e-ss3wE_1}7`|K3ymR!{ZYJ=O2@RR5!=`agQA|JhUhZcp`l4^}h0v*+FG z@$Nmjv^10ZpQVY3r}jTd6EFEtRry0z{^s$WFp?`bZvN%nQ$PrtXK*%sia@Zjf$l_ zpvdrR=Gt0m+3VE1*fmk0oGTsU1oAcvk$F-$IMmV?B?%ApP7!)$K!JeT9bf44N_`e8 z(lx~P*Xh=zf~umtR#Gu2(Pdik<^rjPFGmq0V(oNsh-41_qHGYoaQe85D~`GWRSPSC zq_miny~waBn_lWfK*6C9DMDoiERCIZ$_x0Qxv>+K9XHhG*o~`l4UgU6SUzZd>_(M47RYXBgtIo7 zzfsWDCt)1*x(=EIL@yPS%-$P}jw+7MaYcD@Iv27*SsvwwXp7`Pounv~`W!Q7H|t#2*4Yhambn(s2&2subaV4o&rXiYXr6YH zBV&rRe?}VZAZ>=Uf<_3NXWHgb(Y!IVQ`>HrvXdnvP;qmNqMgLK(l8pDTm!Oj>cEV= zb+nTy%v=j;1ZiUDNl|366h+pp(N*`9K+=9lDQP9)oilGJ!_bLabB=32?bO?ZK}mID zIsZGMfdx{6+P^^Ljj5e-Sqm1`PSQ*^$V+q+mr6oS_6%&6JegKJf~3AhTDV{iYx?wJcB>l&+iTamB(KOql}~^rnzX`pI&vY*ZopljN{@m^ zB{wTp5K1u-KXeodqh?{)7c{MKB;pHN;c&Px3>BGhK{Q$rj6(1lu|hsjTcFHL(<-n6 zpCsvmx?pG^)Ahzgb2n+lA~QHLWI>v82PB$eP901(rD#xa z>r7#bP*wq6r1WSQ9T|QgQq|HiQt5I0RF&&jj>7nXVxh4BB{S(sH#>8$peJ(nH6<2z z$LE8FCvjf!B)e=)_L2jv% z(VIbUboaeh*)j+FmWBil9KFebw(1$TT4Jz$+Mj2@Q4~+f$%YPhJdt*wL4#r@&@b6n zUnA7F@h}HK%~@U8+ffo`!t5F_QqA^eFk>n>N-*l98P)gim)0aQ0EJ~zl|;NShbVoz zQy~`t9fj3TlRFW4n7|6)ilScXM-uJWfX=KN`3F_xv>5x7EitfM!T+URfy)IoXX*nO z({V>tky=vd;S^Z_5GuDFWtQr@l-WT>WS1}kBx$jRB(4zh3lUEolpeDs)er-poy?0U zfkQArldPukehtkrWp1bS#0u$TK}bAvSwGEI0hg*DR=N>RXVl?yHW=~!c1>`<~j z*+_7_i>WFZo1q0-+xCX!p%hq>vSu=VB9=G;1_9MBmQl=B@Lt#U<*b@xN_LKcC@>RIEskoe7^&MW)i$-N2OiXpu=_)yjZ6? zQfWix46*X@S5d$vb&5kGl1MeAFv?vxjPNjv+_E$=)Ger7Q-a%lRmF!DI%JLNkS-`X z*08I^$tqy6b`+Xubi7eRut<~*NhW&+Q84lBNZ{C&>%f&Rx=v+I$PZ*0tQXb*;G}lL z`dnty^}J#(RbVu>ryPz7LWVSpq-eDXn(t0qL9A9f)dHnpSDzQ@j3sgYW5UdMGg!F; zlg?Gr{gmZ^^?{3vJQ{2?@zN1_iCzN$2%`aFAgRBJ$h?sO5*!H<<)Bx4C@cL_yj}5R zLlWA)&ios+(eQqfGe;^t)ijVMAZwtOU{Z!m@csnrv)y0pE-L=n|4B0{y^PE5O*PUcvhd01<$OfC$H#YaEFOV{}*2;dE$VBX`U5 z7^k$_8an`5hz80JLgYgpwWYI}RsuyhbPDAp$m60#&IqQBc0F~NG|QcfSXIgN1{I+Y zEFI{oqGg~{F9oSymwR+7q*d#5rXxlZNpRc+wQo6f8Kz^0c1b`7ppYpD8mE7GFk`ZZ zpz=xmkS36lU6~H~gXv~^xC<{_Lb;qoFVr7kH)JJ<^r3)D$ELH944f4Zr^Q;Z{y0Vb zkmMxObZ*KD2n2w?)4NVIXutz0)aNgf11?O0N{A8Y<%?k3;nt_&CveuvSd{fale!@} zviGTDo&cfYM#h0yiN$da`|{jId{bnS+EJghad3 zGqSUxLlaSuK~Xt@=hn!>b$t2;;N>7AA_a|WidA6`>ek3x0IyWg0T>Mca@a-C?8 zH+OeRKNOf9q=*PQ5&%+0qUPu?DC>jH(g=v0<*aGk%>(-;2<%$BG5xZWx-c`S4yk&;YI^!qhSd>we zrWjs#Asg z;)v6_BF|cyKADn1SD^%eE7zUF{IQK98t#NV4C4rQ2PsXNQKO^jOWks2MS&^@LJ&(f z(&>gl811bo`9Ue!OH6E2*WeN1pr1Q4v>I(q7y*qBi{VU>j>F`j#Ej4o=w=#$3KS~t z>~J4$nT~-?OoM?tT^pPzi;P)Da1s!Cc-*5Q5kayy(GcW8* z@QDl43>%=G@iuLEWuElX`(!Y!CuS6 zw}D`>V(Fm(=xe_bvJ4&KPfPcq6;xrG1}vbxkQs-3UY{O75fJKL({IA^09`S3%ZCzp zaLo(j7#PH$lVq3;K{Gm&fo&NAmS5L{W+4&+5ewSbUN8bI-A|Og*9dw;0V-~JsUmdR z1gRe~(Xa^?fY<9syy->9yj}=<(QCAgXWhK0-|%9bJ_Bk^Fk~~pI?#P#WH5Z_JYJIX zc&^6tw+ufD{iyV#(T`3)2K{*H$7E;48E8tJ0o(12$9S2Y`B1x=-kkbx(QdwK;t%o) zXuBX>xYvtMjNz=22C}6bI#*z}mx7xV9i(YxxNVT%UP@|IOTB{xsm!nqcp9njl!Aw8 zsnIE1bLdj2eNcS~$4G#@!_I5eH~D`F^FC!_FX zKRn9-3PFZ+ho+N$1AI`TSP!S9pG$IWrgpf>|_)aWCn;k8Br?fyNp|6*avAmnP+64%#)$A0ZLB>%O$ZVy%l^Y zy(gnafwkb0d@?*5PzEOt5`i*2Wnj3| z@}!`QuO6TVWpMf+K`6sDLukU&rNkPY;nIaN881_j;u-aB_8@U6!*g8vP=e(=f!j{L zheTNy<;g>tamgTsD8n#L8z2&8#BzsDgdd`z6?s}wCan_x7r7|oR};l3eQV!GGs-CF z`8i~x?Am(8AsuDX;ye;ALz|!=G(b91Oor9DauG1Fhti2M`)1*iinumq#Fjx~QHHle zNQm24`ggb_qYUgCpc-YcUQs0BC5mDQmUL=qkkq71Y2-#no|Kdk`}5SK3^hTEippUA4?u88#H5Tr=+KkW-|CW-GLR;! zQcmv$f=l#XMt2Snmoj+Br7vaRFtJd9szH85Fmhyo$dtiu;OLEQ8G4tCQt>>?Agw85 zE*c~^WjN)~nbJRoX<)?=VJL$;^HiM-bxBeVeT4>J)gbXE(^O_UUk#NU1qc3<99$BY zVAj8`R#RM|EBQGhCA!rafvH}@8cTij)!@H%#;B*P@*X^dj zqmBb|1DQ;(z&YfT48|Pk!RZn@{~DwOLB_{bDYm74CI;mQGN~yqN|2%Cpfo{-TT}=X zz;BmVYLl+E46=bkuK(IhTn7v5hf=oJ;moLcB5x_e=D?pv;#yeh)ltBiMiUC1` z3|}}z)*vG;5>nhC{TB;H{Q{g>cwik|2ogHTluHzWM+R^LQ4<*@FME)Avz`I@gA;~4 z!j(asE`eG?R;Y@ix=09Bp7lH82wB-uAxI+Ol*Ef~WPc>ZCC1VP5Ff1l_;MorBN4`gWAp!~q;Hq>4n8G=l%e4iMB zq6mddv}eFql^G`H5lXq1UT8i@p@2-obPvb{WW-{oHaV|&(Db$E)e@-amX*weR432J zm)XYy0c@eOTGkEoce)a&WSPk1ABdsgSl0l6{CMq-IJl=vaFjBFSJaJk(1r0ClEWzLDw-f)19T;RKI{hvk zWEaW|=Q!6)3B6#U`SfDE^^F%S+>w<^17I4+>LE7}ZGia;Cgiokk(^5FrMO{9QOxlX~ z2AoGOXmKm>90GNs1Wbk~UP;&SL|&K}D>84nLm*Lmqg}3vjK^EO?L*ieGOi7)oIiUa zlKUZ}@ipkf#L^$#dMhpIXc0;OX3&CpPU|pm zT6M_lrFM`^Z2@KEQ0&79?OqFAMS33*93iTwjVbi;AOwKXOe|I^h`TCvePnVKNJHqg zQqE?>;4$n01?$4>3| z9ci*0g`r4^vh)YUpj25#gb_n>W!VB)z(XX^>=#L9r61qM%Sais3<0O7 z)k5nfuIfL{;V@-T+AI^xK=RTPUzD*tFLRcm3b1>@FQbG}((spjz+9#9Sw`dS_Pp3x zhR2JHq>CscCi_gpq5mL*j)nIVb(}j>zOE6fYkgQsI zeS1N<=7rQUW`oEJs%6=_p|a`>@kMAXI~;kn^lyKk$XZ72)Z~j!lyjFWx0dnsFtmq| z+7V96nB7vZn=+m&d3ppy=i$vpXq~w)N>bWBM?if#LxGqSQp?f}j+|Qh-JYbtGSuumz)h7Oz`>Z1GHN*)cs6`cPJMb9@xoI2P+7GspLS)_ zvd9Ja5<*@+EmIFk)o!YMOI}JXGagn!nGKOt%gmK|8MF+6159FQx0_p8M#Fn@^7|%K zU9kezV+fR3&=)Eyg!mLDwgKo|gO?fbmRNy;kQpStq~#C$qoBsX#>5Mu_=QBc077Ft ze-(j#w|oTK?~CFQY@*(LRs<4UJj@*e5eMVjXaLm|pcW8g_bAmC>&+=AUgl#m#dtLe zEX-h)w>oiz1Y2M{oT69Y&(rcBg6Um=;Nt8?{H`Y~wMi#!fExJX6dY}ks_Zl(iKezA zd=VK{_b!BQk*lUQj?%`{sp<$uh=6hcgk1N`o>b!Yr(`m6ScNn@O0oT9hy z=M$v&T}U}sP&iJ5Af=qbVyyPgq6~TqGEAo_sWHjarEfjOE>RUIOtxgN zOtMcd$US{>kJv&0d7uJ`W8(6I2n!Wbjgo3ar(kOXF(1e0NBSD6_$r(cojMekzaz(v3bvPu|bxygTu;ZK&Lwjzm@vL1d*u5Ve4ES1YVTCR3m^ zD?hnWjMe|!YIcV=*Kyq*h*mjR?!C(>gDRAG42JD}H0e6o(f1vY1?A@>z{!Q~$-!(N zHM~P57F%CAya7x%^y=s!ah9mehxYqMQDZ(vFX$Im$UjNEENPg6*1K;s3LY}a;3;?D zhCQNu4e8o;A+ocaS`;C8YscYdk2L65qjG@qDcUc)6o@@e$?pU#3sT-?3jNLncOLpJ zTXL7(xJOK+4?I9_(mNLgE|A(kY53acX~Nzb%5G)r5pfa8+o0{)N7ZQ>IGxa<``Hd> zt<#m#8FZ#HG} zhUs^_gwsW2GSlib-Is*_0#$V$66xE3&?Y(7m6U&zWQz6455i5=i%Gd}A+Tl+P83oGT8UhE=drCT+cy&42B{`D9lk|0b#pqhbO|J{VVSLMl z-qiS{$*!VF&92T;n=4>5hR>H|`(_|cXetNtAZG^FUEonds|;^I(5Z>TW;LD%flX7( zL88U_cU_VqajJFDQODRd)V~F@@UxtjcRvMp(nM6# z{Q2@%1^j`mJSdk6dv``Uq~1f;}tuEv?_C(yAx}SuLd>XTe8_xbUTccn{k2)Z>O_D zbdc^*b;t?i8|bHe)J_$3KjH%KdiamXgHe@0OQ-(=Ls6kZOg9bg$KdRh@2D! zp$8cby)@pt8pRF+3(n2FXOEaNKHImEs>NAM$qCq>&_u+r?DTn^zGm4brai~+-6N_j zLmZ_!*+bD2b6XL&coR&UU|@vl?43i=tGo)n8eHv$ru*@Tl#{R!mX0YhOf3jaMH!5?pIRx>AszpJ8}OWF@3DTse2Op7$Hwu2vqQ`T-LVsRUj4>dGM^%= z_8~l)PBvgjbOO%Ho&O*XgNgX^9SM<~om8oC2wM6i@Z4*_Yk zM*95At>VJ*(JH*M8kk$+D~jOZY<$KwP#XZBA0KLoK;AvhDzCtMt5It##OP)84!v() ztf(jPF8tr^;JJ zm*)6=N2x=r6}&73u%s&>Ymhh^2+&ewt(PBRy7C~qMh;e|Yb2s#3J`^_z0ReYwAUbC2k55_nX*xgkNjZU#~gD6IKsTc8E}4LaFt>A;@Q zfS(RJifa6-N}t}sb@6}Ld+#W_uKMnKPPzBa?e|XanxZo5GwRjqlGP>4mMlxQHKQ3x zW0jFK>Mob-fC(66Bgzm=I5PrCfly2Wfd_&G1{@Lsk0}XG2!=o!q(KTKPZIomzQ1#? zEO?*w{_(DNt#`d^MN50nIp^-P&#u3=e`N{JreU*yff{g63;&=W839uOScJX1gyP00 zadmEptTEW}d;7gM!bP#8ESym$c$z28;M=J|`bz)-@Ye+xP3?H2A!l}!+D(<9mAAGB zAEH>RyxO%*gcEU!>lkCIEeuS7K(Zwp9`TsIAY7yt!4k8m}E-*QIjSNQ^zhWnzpMzh2H@iqKB5P^^zAK_}VCU37HP~IE)&UR;o zu@cL%8XOuZ(GpW2Bf?R)g`=hs%0{ zZMnFF2aJNXCD(C``=f?rd%_K<iU;5RIy6c!_Kp4Cq=N5izC|FPkcT+=y0Y~*ElQX*q#p*_H~TWNunuJ` zyw>bSUU*2J2FItV0SSA$QM((y)aF7!pi4{Om^S6iyNswM(ko_#ul z%YBA+_a82kkGOHjLw`AQvZ`FwI4dN z4E z!G4|^yzc|xCk4)*azi{0L~q4$^_HN&!`9nE@FsrSFx{s6L2B8y9VD-|jR{iR z2c-_|K^pFCbw0A5KUbFC{HO2j_a1kR5=&?;&l?QR|6srOyz6_x)xX{Eb=JB4d}lxJ z?_*C4vdo`taju*WTK;aox7MI~m)ul%kgE)iJy@#kumd3HI-idRpZa?(q!NK=#OLzW z)Hcl!%5ts-Be1$_h_7UU~TckK9h@PinJN7(%b_oHPZ%EY}?7A4M1Bf*U1Qn{(=@( z6LF6L1KU-6Nig##&>WFxo181_g7{#!>7%*(#Ci5AY_~@>ko>2Y;R=Yfk{k`GpEu&6P)^YkVzp{+eK)GCIo27meypxF-t%>glTCa>ST+F zTpP~p(1}Ra&#jx2N5P@CCW(u>hPlZ^O%>64YE$Xz{N_}?ZbCA%EY*lDMO|Ghkw=;! zi#oA!z!`m2)%FFc9m(_){nWfK*-JnMXr$_FbyXc+5)zNh?W$_Ycg?LyJ~x(eqV1#6 z17GfJm;>KC@y+>u+Gj5EN;nUEJd9y&Oy)b?-vH82Zv%2#?&Wc(_Cb;LW^5U+v2Gq|?t*2<`n`q~5mcRFb_R?mf0$jjBHc3&wZ4%{iVt>G zu($|_)>hR&*Yd5-JG-3GPUM|8x1a9!KI|HTSRMTQOux5%yDK(Q5>;aQ;>g%m1x`Hs z`t|t*d?M8xo$f1emC2-Jo^gcflk{k-pP+YTb8ExuUU1>zey@`=7IX`tb45SQuJYVN zpc74PL?{jDBzY|B74ldyT#f3hwq4T-J9pynFk=?sX98j#9y-HO&JalZY7K+|=D;N}G4o&woI0EC0RJ0}{TRf}4w+bX*ctm6h9X+oz*2B!Sx~35*av&y< ztM|7XrM=#doK!!HV~^=~lZ?l;V!&`TK`U@S4Q81)a2byf{L6SX)j(92xLEkdR%;#>`%(NTm>sTqSqV#YNc_rG?ZZjZdA(|TI>(_=9|q-8?6LqOzCumzVGWh2-Faf> zixW8}h9`<}-Q=TLO*}JMfNPr+Yr+c0W(A9%>i0Tg<2DcRVEE~NZ^9yBldy~Je)JeF zP(UZ+f?Ih^bO_uAks`u&Ct|eI>|U)XjG<2S1$}Sn_vTL>+sK2Jk_dihm-D>1kQ#%q z-bNjJKvr>P&8ftAX7s=2jn}(lJ;5ti`n~QMu}T~>AH%y2J5hTVaf4Run3mQ;!=E~$ zS*Vq@DRAG`?@j7}1IAVx$+_A?7+(l&IX}Jyz6-&ZDc4#RLPded*G_QW)Cm_J{NUaF z-k%rzY_g#~k(`2^XquzGDRnYRNTuo~qD~2Ql4~F+Ac~iXbVDNGvL%yg z%g(^76z7eYm?of;ICVrMRE1rt)J0R+S)`iMnb~=TDokanFTa>^F29&109-2p`vY=7f`R~tM|-qnji zh1RQJ{$Zm}lLk&{8(=|#-{LH>en@ymOmx3G`00}aUS}3L{Dnb0kr&6c$p(XWy=lPf z$iBJ)o?hh?FWvmTw+(o^{oqU6d%V`0UB5QqjSyiy(qA%)ruOrZqQ2UO5rV-R`{G(@ z6dOX!5n%flBu@MABR+_pa(Ip~FDSf!z?)odp5Y zb*>C@w^@AAeRX8}gdI*T6S;I!Qw73!t1XnJs%Fm`4e1up0gywNIn2gjw`jiB#0*bz zo0-9*A7*k9X$>6|Q@Ss3J~H6VsEvjkjtMzZV)5>Bp1(IJJUigMrrJ-G-I9w&I!s+| z;QZErx3d;z?IHv?hc8d{!+H>w4^$RB&2ROskW@Gl2x)ASt`FFFnRsJGkpJxguV&_$ z2U)VjzuNXKm2_i2;Q}cQ4X9&DTZOJJo-v#8OQ$k4r0gob^0>ATW|Psz5?!Om*^w zyX#9^dAmNhETWkgp_H zgHA#8z?k@l36Ofng6W?g@Fup|f$l`H4}(U;O;?ld54obTO`T%LDE^f*GF~Kn^i>FE{gry^A<}MdmuJ%b3wrQ{tXEk1(Z#qBXW@>3i>J{9XX}(@pHtw z)5_diI!wE&sEJ+ixk>Skc5ubF;E7d@w(>y{gzKWwvPXzZ-0sjvY+G?t8GQY70LMZs zdKSlR0!LaID{`DdWQ#4Cnd$mex}mEfH$9ttQ?f3d$j@uWATQaR=!6fSIX_*jtgcJ; z;LQL>^F&-s<&w?0bT$WHkIi42GYybjBHsazU)|A^sL3|3Y^qAv6LUA0@2IMmiv$e% zvRNPGS9`g=#<|>HOR6K)lNv~kq$cON_GZU@&9;h)iIrC>vcHktk!{cXIP-F6eze)dY`mN~`>5b`$sh3jkPhCoFPPHWeKKWeospNrVZ?Y=!&BT+5)$yOle>Z+9 zz9{Zg{*THlH}hlj+z-Y^+uM`x_{7p5elc)Ak^Z|c_Pc(!x62K_^NQzmec})P;fo6# zf40}>j(&8}8|s3;D{S{_M*rmdU;O^%XPceN$h0may1D#p8)*Wmozy|jq+Ze-(p=I!(tOea(n8WA(qhsQ(o)hg(sI%rq!px< zq*bKVq&1|qq;;hAqz$AyNgGL>pCf!5YP1-}cm$a93 zA88+HKk0tb1EdE@2S|OSe$qkG0BO*9?%6{Q(A$6UfY}LjXh!xVCK} zP_?5m68d%>+r}%AW7>qR0_gY6O*r#WGpcg*Xl~q~ln9;fv>vS8#pMBHt$a*q7L6$2 z3c&Ts&fxlzL2t4Fr}e>Cxb7}Q(4!GssC~AD6NW*M>qC%}SJvs(c}1uYl!nP>N^n<% zIm3%#zXZ4hn0GZK4LG*#tEQ=wA`#Uu-EFce}<|>yT|*AOwmd zY0>Bc%mo|QELNWK8^***T#ACqVM(!!#y|=}2%F%Q)q~#rU}VjpH)*p;&DLRUdV25} zo~3B8(Rxshp2xr#ZqQqYluJ~>NuICL0USpa;@|I3M`s`b$Q?%bjeuSW`eiMAZ&38ymP7tv}bOkTZ?s}Ze(d%egR zA;FM`-e;$*5AmEs9o!ce$Alxco1m{b5;=QLVi(iq!u|2F5!9KCXPejM#yMwUB}=S% zRTK|0JUmB*hmLcN81H77GVA9nZ1j$a3$5Lv2KJZ)Ujuo-Mb7j9~I^HJP@-?SN?L)k-~KmVc~dd$X0yWYw7q&mIdV>>Tu(=Cd+QBS*y2kRLxsWFr=z5kx%M@4A=Hg-eT*`SalF(TUELdxC4c zyV1_OwnPjoO{*s#R$A0(L^2hNz6%mCh^>DH>&+}(phweLv)Z(0>P=s3rP{Me ztD|FgmZ#GJLe6YVq6yk9|5@sMTk(Fuy7_URAXZ3NOb0Y***)kbmz3HmBBRO=Js_Ik zVP1)5Rh?ZT&gr|j`knG%V#nh*ckTx|I2&jYD|{=zJr*sC#7wwTs@mu>$m26|HP)+u z!tR{S;WiQwx4pcnxIVafV9=|N8eks`mh=sJkK6Qi=&Ng^(St5|kk!Vy>CgU8qy(^kCAT^;h z8F%Ybz4Q$3)v#0W>qiH@o_Qcvsa1^&YMk~>%gESqPN#6gD~fw*al0*nT3p|l8r$UH zrQ?I%%o)CKA+^TVQV7pI1BV&nHa^2qvpyCteOcRWdhoUrgWit2OjqZAlNW0tJjPEs zVK@*Xm)j+YTwo(C?DT+e%TcLanm+2TS$^a&QN1{pyPF>_*g@Kf;2kGvOW>Uv^rp*B zK?*9iPzJiu2OH2af+;7U%4Q4Ll%W@ES3x#ko)LWQ^q}|PZWvUIWPqadv@epfCbX#6 z$vDh0IGxi4+b+{ldMxpaXR~VfR@+Jfg_6~Vpr9mwdL;P$bA#SHv;yV?2hKD1JIzhb zSSY^)-j&%r)IH}8&8qt5 zd@?l+VOULVdMU=u3)0nmaAu;7>gM7T1g_x-!Kw0z;`$`sKXR9Q4m+27j*x~(50Q?N zj**U&PLPI4CrPJBr%5BEGo-VmbENa63#5yrOQeTMkB}ZEJ?1>uQ*iv;sK3%_FMO|L zMrJDc$^TcwLJ~XkOUt0H6c|!4c;NpK9kL)9!T-bPkaLSSL?RYFSGMeusm@w}XuI?j z5sLXve?q`~o#4lDKnUfyTCe8d%f9dB*nQ6D9(A6$Be;2bsn^-)h7Q)BSjF!$Q+LytzI&~<&6gqAx-yJmHE#AebwdzJ$zvDG3#-HBlvg)muR1giOE!p)L4FJyx;Na=J3)2j7bat}MTpVjjU1&G zNpe=mKk@UlI z%2{Bf%5&X)_^uakXPukpMN3|HZ;0FBd|b-tdSyZI>wg&Yrsi!*`e1W-7y`-7UyXV9 zauD3llg~ZoJRuP((C-(#I^sjtdUwLi&Q+haTidwPMEY5? z<_eM%C6m#Y=?#pJLB38n>cdhWxKVqE-yR0IV1l5b4+H8(UyX=hU&rkER$PQ|zm=U4 z>6q45&E`t46e_{qkZ&S&>rqXwFve&9DTb<#Pw1-wJKMG9ZGSZwl)7e`Nh|#52%HX_ z^^In>*4ECtNDNQfg!R=E4osb>kKek3M^2P1v9-4Ddo_mCt%@pS6btcIf?jfpR0ur= zTMJQg89qvvwf_~Mg~1R~AS!b?mP0u3|926EsiJS7yx3b^FrY0^s+nzLu52d3tZ0*_ ze10&x+wnRIifLtr1-2R&dof(@4T;#bk=*0?Cr%6t1lW>U#pIL&N?42T=A3#Y+~fwR zT=VE@Zik;($@-LAPXR9(pfhiGV%rMaEzw&p62-4J zUkb;REq5g1mjgb-B!ud)Hb(2p9n@Q-R0oXiR4W7O+|OQ?b9}z{e=6 z&O0Nx@asPtHqZ9r*7U6%FBFnvNz^zs5oT`VR?zZ$>8M*XBy zNrdLUew`rL>Nt-tx+5qd-5Qjou7B|22wPu}ZAB??nSNcyH}0`xlHFb$7x}{{!%hf3 zHMqYJvRWtLib;c+m5o{xu=MuGA=Z@5SW~k#L>lQ+cg5jRZ)m({8(}2;9RUc1G6~q6}x0r)jKhKxXOYm zoJ+8S9Xpl_H@TG@(3IB)Em`R@3^NzFw?{PzL0Al5cAODyREG@Z#L<2!g>fraUMM>+ zE7#v~yZI57Byc$F031bmW?+1TeP^P!dVMi&ziYhJz{;dfE|0a_K0{+g(%&Mx! z^AKAY>wHpARCWb<`1Yib@6lcfk! z_3&S-Q@NIWbFML8pU=)rA0!-A2F=V&wyG+hotCS~=cxu~RXMy()z2W@R6g61S=3OQ z%QR)G8&Pto&gRidK&zpuskTB{<`F-hJS3~~tj)HS} z$7@JM(&Nr^JATFSzlR;m1029s{C^uYxFE^(epv6~4M}K^b+|BqJ;fV(e9%Wr?uLnA zVd#4)qRBjjqVL?&zoQ0oq&A|(d>)noVgj6VT}LP@b+o=z%eh79b(*h5jT>o>$ZqKALEW#^ z3f`=hx!&`|K!nTm=xxjcwXxfpH^;oBVk?y#uNQCV;H9t4;#6uS651540=|k!TQx7y zeJ_4K6pP}RK5AQZVFGFS4LiZfy56~=bL>}r5g{z9xRW^wnUx!7w%@#6YF8{ zm6-RzLae{&z2Rz4XwZ~t-yPfZP)E`t#a1uMJ=n9 zFdn-he4!Kdg^6yQHHxD62`y9s{!SFjPWDUJ+zRA%$a6!)^E5%~BnAo?pV@<9KRSRV z8s{uGbRNG3@~j^sK7`g7#Y5ecZsxc|;T%l1*41V6*m)g8r=FMe{avzV6XB&co|fZr2lKZXer2#!GwB4G4pW}qF{$N5^Ve}hp|wW1-5k-Rcgjst!DS*BiK9JPv`|Z zgTugYt z60I1EMDtf-z++WyBz_yaV+ZBaGk}I0Y52REN>s+A9B;UEu8;4fkP8y%ptW<4YZWvn zlg2&hh%0tG z7o`VlV4}jUGC_0BIn*=p56}qTJKsn9Y;N!wz-eN*P*8is>6IQI!+R@X7q!Z@?ojkU zi5~^6U7LA4tQ!l)BvN>*S@Lu>NZz!;uIJZkf#QV=u&p-YsVMA$NT-Qw)J@~`S0RgG z@Kj_3Kf4MCp|Q~YO3X<|PTKmDdMxTFr_~zGJ*3UWXI>nUM&H>Zr3M%4P*Kq0(7TU0 zzPP`zbR+76+A*RUCnYf7*B6b3?1^ZG&T^#3dp4aNCc`rdZi@+n)cLhu9Hx#_A>*cO zM^zK^fCzR4-cuD->d;jDP&;1T&Ut7?<8X)=pPWzKu*Js#*a!iw!X-b;YM6*?0RqrL z#fe2zC3w)kjoVbA?VTFYZTDDXC*|GP5Rxd~Dxt`TUvMs!W)XW1^H+~NTYX`f7xQ)S zWdtWfo3DiF2~r@H)I1SxaFUD5T>FcGeV&t})P|N^SF#F!^Z3!_m?*_U1CJshUiEnjc z=PTLEFOH!rKF;1Or2n*{uj0!U>9?h~Wj>jno6flBQeR7rrG`^?xCh)#?mV{*aQ9En zpEy*|Cu2X2eIxd4?9H))y!uyu@sm!*_MDOk1NpG{az^ilr*8QscLHCW>&tE>+mp;Ykl%B$e8`P28=)p{QXT$_R)ue$22h|Qh8cb#8M z2HU>c&-vn8vVQ-S4rqw*i}c&1kC8r3`W@0INS`GA57MVdpC-rxh|T~5!}TCUNfO^ zE2MStTKA~?`(2Bm_<7476V^)acv3vSCRMHCLRqU_TdK?L2D0Y6@YC0p=t0!fuaQu1# z>7Cw!19PcF^{w+%Tn&irr|NkxKNx;zekVUJ6}x|Jj_UIG7+;vJYZSFdUVbR-*U}*g z8?IRw*ZG{|hL>A{XZXy7X6f==a!~-g*3H#a0q5du$u$_^O>ersv|EA=8ZccyG*i{f zL#6RTa?#89+Rz}g2);sn=#bOw#iL8EeGw736C~fV)9dzmeeviUfAfo-w@nukD@xkT z)p6c@YZm6nMx=##q&59ErL(O~$#Cv?df0U}3-)Tg>l}Xh2o2&TFT%MrJ+&FEV!@OP z{!G3!8 z>EL^{?{lYqqWOLQ_#UU#jUb%`rC;mdeSC}(*XLa6Ea=*j(Qm*1A2D`BkDc?2mydSBre|Y9LKUNMcb4^-y^Sw4q zPfc&~TDwLhC&~Z~N@`!A`$qX~=!YJ;)}h;ZUbzw6?TYx(69Xo*xwcl76+GmtBgJcL zsbi^*5m-+V=Y<*k)?REAvtFDBVPu5HH61|c43X`^Rnm=_Ho(w9rabDrFr8vbZ8)4M+gnimv+u1SjF<=ouV%f zg~p5q28MJ*blNmh?Tec<<2A-jq9ID>Lx?%EMcE>m@)|5AOxN_~6X6$|%@xiy z1HW^ko=t@2tw&~;Hdv=@ehrMy^5SQo`RW0u-F>0wng2N8bQZ2@V;9@&Y=1VpaX8`7 z>hx9{rpT$-wGC8Bh^--W#903J!%X$z;OnRpN31?}O>mTO4t9WfL-^GL9$QhOy41x1P=QE#vz0-kqz+f4U zEm_EM#_7Iutb4Xcd9l}HgANmWPP^P1g;$ZG5df5-KfGI%Y>2N3nQi90ZTOkrdlKEM zYcsi@VF0T`dH^^&4VKPNxT z1LbA_T&dJ>T842rc)IVuf5xjF>lm62rH*vJ@3>Kj!xUT8Rxv^tdyz9{1 z8hXDm_ZX0&FH;7iGq#~WKTH(!aGnUnb_iC`28LSqz-yT)!nMU(Rx?efvG2ImGu!j( zhWcop7B$OTy^Cs6x`TsHyw;g?0KW4uRh8+MnCxWB(*W?4XF4!|8af-tbi>SA8D&$o zLZ#ZiyUVmlBMv)6$_AHAOUBkhaR24kIvs^bKQaVBj>w(qN!e@J<#NuT2m1yt+P>kZ z1rx}i1xAKn?$g;9$H*@T=@|cbL4d=@9QBSo$3BE+CC(^pniw_ASGj`O;%T-vw+dgn zwJ7v;k-C$~Nr?j9(I}9wgQ0uvh0K&hJqJcr>6T=!s)q2b`9yst(TKroLq6G^u9~6v zC&`9vHcvR$e7?3CevhyxwQbqz+Jw%Vs;cVY|2X$bXPTO-a%l`|^BdB$(zRF>Ri}wH zR+mliX1b;hd!&|BZ!QjxmrqQ~Bx~RE)AQeQ{>TXq?Rm*rl!v7Lr#aqX7cKHLM__P=ZXWr$HzVa=n_i=w!#aAnW z${jB`-QCfA-+8nD6aVdAr~7>{$*25`lMnV&yrnJK ziXqbn5*HHpBzhCo@o&U$#2=0Cj`zm%-s`-T!4(RftY2A?TjHH}2|j*i=J27J_`_c? z&D-M!`QCfHNfYjR(fL6|;{cQaY zXTIkyPA*vR(~64xr{{ae-5~on_u-6a*Tjm7+J6c9_Fi?`gV*eO$yuFzO+{swx6$Qu z-stS@xjPa)Q(mm7=w7$fyBKu5x7leKz4+4ZW_QU)f^B!d~dncw@8^LdAw-Hu@V znF-$N)colinep^`znFGMZ~o)46|vqGe_c_LIWy|GosCbuZr@7|*`Fx;Q)S;)_Gikz zmi`xQ5*;h?74IhW}Q?V)}OT{E`nn5!#IG<931Q;^8S|7uAQA!IQ<^UQ36$ z#}X`0c4}aHLjxiS7tv;CZe|8EAK&fOcgW-aFfKs02=&aZ4MQ22`=?9hg=kyQ{42~> zJL>!rOectDX5iwka&?qVqkuux3RznvKB0yN?hwD+8gIfyg zcSxJ*2&_){mHOb{p4jd6rQro|3wF1B*u1|GeEs#iy&&-4u-lv1FfJ)=1cpH8XJ%Po zPh!C%{QS^9*)N-^OmUUx9}y1~YUIbzk&F&S;K;qCkuTCTXMO8DVnRq-NEcPF_8mfI&hri`+b)nGpv1SIZ!K(SMz*7B6m5p zW%qFhaf0?gjsnzN&uoQO!X@;DzJVx!2bKQ8lf%qosjIj^#!6&EF#Gau94cHSZ-r`N zYmHFaN7}A}&A}`D&{>HIjw)UgEP86UHzAG?rjL1e{;}ZMr+0f##^tn^g*~<@_?;`e zy(uv2td*eSt-uj4;vEYf+n`FD~)~}j`?gqrdy>>)rX>TZAk5l_5EtKnRnhlF*xv! z-Ck<0NzTpi5SOs*8dH=X#Cjj^libRb^v>qIs>ccRMYE(19va>4O`qtaRmri#*l~WF z<5!x)ZJPjTS@nwIWV}|sli}>}qL(h&t z_ND?Y6Z`}Qj>h#PpD{bm`$K=R1%4gY+%PT&xL$)Ni{og-g<6Vclz6(R#^xjO6Ne}k ze)cR+W<(5O1VvJ)mwYWH~IF zWc*~Hiu;Zd4sPeV)gqCYsa7${;oa~BEfe~#QR?t3hx$(kpS-@?>u8IVf`MMOrNA6h zNMh3#LBa9hi5t7U-a@qGJ7Qdtl!<0^xM>@g4eI1k3lFh|tAtd%lhQ>@_{6D!Jsua5 z1P9*ot}u2?Lr{w6Ic_U`CXNTqD}>}7lcmHsj*h<*$x7Zp=o9~R@UGtkC=?WGv^chf zQq#S}VPevh=!h|ar720HA=JMvRn!)(&vV4XF%j%ba_-XhW_j?zVRNRsc3Flvi>bDj z=GJU#Zfg>+&6!mVN&NTJbF`F67H1?<#AnQ9>QT`nv`9T35|Y{8qXc@a#=Q{H9P`ci zke-yDP^{@`OE)C4U8$O?DamB*+;qMbFq$GZn8os=W22(*s|JeVnJI?8rKYY4x}#kd>2!v?~(qT^nKC~NPj{4OVVGF z{+jeRq#u%gMEYCO-;w^F^be$eB>kB56VgAC{+aYIq<LATldskdeJ0vA|x5tedqeuQoDGOC!Ow z5AF6wwwPV8NJPYnoCMn*zZgObP0eIKf{Xft;53m?U4RP#F2x%d7j+4R9J(|yU=dvU z@NTcI=B)?xOM48M-&t&G)y>M_OZ+rpzvxU}-K%F=`M5&S0Nf+M@-Q$H`e7HBu_OE* zt3^6!C;1^Vsn^yVkk5E|g4a>S>E)#jbhoOT7JTg|!nyxUzOsO*=yadl=~nSuy*Uaz z5Q&CVyKQ7Dnnkm0zWbj$u*5?SAP=0=l^-Pw`^l9ba7bv)HY;HX8vHX{!u9w;QFnEa%YD$ z?GE04Oqe4gj^aGvQ)7S>#Q69{9+pQ~aI(!nng9y=E0P(4 zMa+pp)>f72YS;R)@_G08G)l%1avvJ*gND;$S`dj&Ed%finzPj=ASuJc2c^C+E-*EK z)=BX8|FxTt07k+r3f;AKRt8)D1Bz-RD&i8Ei3ia^Rb7oiv`f6X(w44S%MQs7ctq{3 zlQ4#`zI+kxh;ImaHT${aeZdp|wVRL^-y^TdTO03y9-;eq;QD+f`1POf_EuMdIzo3# zcYbe=H))%ZVM590L_c(NlC3{NwzA|b&McrCx9e*&v}O^WpVV5Q4(JOJP!qLV28ya< zAXxwXJ>DJdrehK!&16v%j{iJZvOy?%(LwVA=LdVd);d96ctOL6c@R)9}X_? zgTp`C z<8?HIMg-ES9Xr9}X@m+BTa*cY%Fpd6AcpSK#ReSSL^jd7pD|a7%hlA$j0!5k=E~Tn zTO|`EA9u8vw2!bD@!!P`3oL2v&*kp8!jYJ7NP}E8sM^X-pjbb?Q?+|$ z^X^)_BDwU~9enQZ_jpZF4QsM7_%m*ryGrXukfM(RBIoEVvf4@;CmQBE&p#Mc{o@|* zo_Gp*q6pgy!FzVxi-%PKB=expZsKacJ_!dbHxcGDeZ8Q@J!B+o^%G^QeKFenFQZ43-zOw?$9mXzStx*w6Cbg1 zv-T?(DExRwJkHwSfca(GeQJ2i3FS2*(ZbTjX|ne8X_xF!Wf)OI zd>g~Z8YvIIO4sasZcuGEC?V7O!)QhqHtAa{0Z5B{O<+HWkKj&GCfwr;jj6+@Q?znS?HU9j4!Q1xT>+NYO$SBvD~mhC2Lc;Z_SRqq-c{_Cz76pPG80c3vAkvAfgNRhLix%(;B>-$?&X z`d_5~ApIxlzeqnPz2dy_qLyJkO(RVw%^=Mr%_7Yv^^kf= zb4YVZ^GNea3rGt|i-2=pu3~{Z>;#oBE_OSrUz^&+dBm5KZ-qnpm^++!G+7m_=5 zHzHSp6I}i3C)(SS-OlJ+=HHk!+Wt^gJXrZ(!2Y`G*CVbzd!JvN?;bgG=H$qd*}5P7 z=%)JVqc3J#DuWk)zQ?PJRKJ$TLGQ93xD!X8{uj4$bnIYVN4DZ06VocU85&|Yi)Y8XXB&E zXd3x^-hVpr0m&pw;*N1rXAvtC)l z3CQZvk1j4%6nrJW)5}GxpWuzzZ~e*I&e88qod-4f?ZxgD*LmmYskyn%cf7FI4<7xq z#cpc!@rHOukU93C(;UsU@ye{Xer<(opFh#zz zQrRkHtCg)$wpQ6XW$Tq~PJo>R;ao_P|!E-AXIA5$tA5MP5o8*4ey`Fr3vY6b9 zZr^tjZ%izV|3&=0@eA?w@kr%Um3t~D#Qr+=k=XgzidZcAKcl13Bhk6ee>z``{4DbE z$RT%LbJu@0=>2dr2-|yoMc1hF!zZg# zE42wr2W7#V`Eh=b*;?mV@DDU*X>|5|b~BsvrmMkc`0liz z`C7BHFZdBZukslPH`sZ0pV#Z|dV8RTP6+;M<00?vV8@n2-eTX5{l5Lm4lwvf=*t?v z)m!ccPuK4A8e+RT80f!sM|a-6wR7}O9^5)5_=g+K&aYqI@mlxtj@OZ%AibXStE4xO z-bi|q^d{1qNta1ak)9^Kg>;4VR?^!@Z+D;D@ebGD(VmDNugLx|`}OR{vhT{C&pwdd zkZsLY@UZmn=ESG}%>A|(%=xJA&0H;V{5ZU6@p@i38dZWJ{C^{Kzn+4I$Q7{;>dS%e}Dc`G~;l&8U80r)2$5upyVj8cD^<3NNSGVZ6<9<;? z*CWB^=Ws=ZytMDw*@K)BT+j0x5o{16TFu+M1kMwNPlnd$*Tt1INc;M_#Ah3gtyu0x zPM*YUmD+eVERCNFcx}KbI>kakSki|OqeihyorELr=SlD8O$b3v~?-lt*zuLa$d&?2P z(yz-Np&(3Z!CR7JlGHeU#nq;YirByTm^}6ruQyQ9F~{$nkLKm|27R&> zP03p~6I^fc;svE&Vp1)%H;%gQqWPt#m5x8Rx2I653%_ae%k^$`y@loLg^thjQla^L zqI^9Mc7vLjcfYs{B{4j5iJJ=BvcyduW*w9?MM@8S)I_+X;kEKr$Eu;-m}C$qwY+Nd zBZnHQhO6~1K`yw=LA@@kzoWLsP2*UY@xL{&)^RL2H12B3lv(I*=p$SgJ8PwFLv+4! ztD4MIP48@Y#F4iK%3+eS$gjhMpFO{kC4!Fo_?P`IG!rswR`|0mlT%L=6 zvHqUUN$t-rr_MHmA2nc4&2-uOgd@_7b`jEkbw`thOMV&B3`z4pe1fY0xD@LMUEk|w zh+N-yP~4%E&`KkcbW<{UDFt*Wy_zk!m5QI-FWnfrgpMVy_an!NEO0^hNU&y2frl*B zF%6Z*vLVRz1_{dV@G&7kI(}M=NZ6VldKjwt@PHx-g*3LSfpB_s&=Ie9BC-PLF|N~jW6y4{UkAdZRz7Fvo#sY|&tuc8MP|I!R)z_$pQS~2pQHHi*Cp|2idENnl><1- zKOv#1Ro%)#pY{#|de%#w1C9>S%n*86^=QeKM#EbsYf1a)odmlnRdC3O$Vk}M3j42b zZJk2^IOH)_@ca~oLbK{0bxk(NV;5lyW>n?%Ud$jKE)~Kl5q0 zt?D+7P2n|LWi$e7-N?|u05)FN3%Z|-5+WLF{6BeeC@j*s-Se5q^7dKB*KbYSHU)|( z&BN+mq`#$(&9p@eN-A|_2J7=g-;uNBuWrE2&TZo~LtC;Cu1DJU5TVIV8vx}7cgDkq zXh{_=CZkjO(%tpAX5!>Zqsh;NvpIgNZ78m5EY&Yo>#gNIQSJe3tyC2oI8y`GkcMrow` zCa?9UHJps{W2nI3CNdnhl@7yZJDy)24xxM#0`^!-WlKIWA<|um377_4!-uDL z&J3mae~6lT{B(L?CpAP^LiX1_LX~27&mBx z@EFk=IpP4~6pF|0IQ9hLDEOp(ybD86;=;%erTx4VL}OD!Bk$So0!|908GMA#+v1~f zvx*UOdZTzyVIMX-k&A%N(x4vqW$$F}`|#kGuT7-0i5#9HIQ>fD-wzwCBx-kX!34Re z&fx~IN+J^?-4T&Xkv>fN29t>mq@=)`UBFJ zNq?S;(J&D>&M1~7I#jcaf5{5jmQW_BkWcTR8k%VL$% zbN0hN7aIw?!ac@3t|W5LMprhY*#PuYkyCE)@gFbustZm?=;=eV_$u}o_Mv6ERwX>2 zqielKEs>QFcSIzT1%y>}%yltRwsOrf$Th5>w-(YMBiLFnE}2}P!OpL95^(b*fsY|X zRAg!~kI!uF05$1hLsTu`xjXz7cYy;Bqi`SobdM7wx@w=Kg4T*+0tBG_p(X+Q@bnZG zJY(dR>aN|g!9f`WnLpi!4wJ*P<_JKND3du(V%3D35s?&Xk zOF+2=in%*lzlfkqE=p(DTL^~bq`K;x7NjN@oEX%^ptKb2D|gBg1sA1ubHMR|v89_6 zK**5BRcrdemT*FlQo7p`(kN=zCSn>LJa)EJlJ56vVXAgo;aBZ#sLvV|qLC@qW(!7# z*i9<#L>?NxGzg+qorgi+I7%NBe$ej=ScNfMybUUHoRxS4s+s80Mk(oyz7m1bA_67q zB*Bnp!^u$hRgfkM%^L^HFl6CC5gWBTUCA6wz=oB4Ct1ztUetgB0 zkUS5x=Q~ySb5+AepNJV?*#yzU(VORB zAe{lBqTT^gtV&m5pq#->2vznRu`f|>2Ti8XA4$n2Zn_FXV@?=qGk9mprt9#^M98Ts zYRD8CILW{S8O4%h=FNvcSi%U;+=UeRwAa%+uXtT515G8Uuj>}apVQL=sJElGC9)?B zFM+djxs=I9HtwVsFI?2KsAtZi1#{;00?DoPGy~*vr5f3=)knX$ps`S`+hjgaDitG) zS|2fO?1zgX6xTc5OH;9)5Mb+-CAP2S74RN^GN6UUqQ?_}4yB5qqKuQaZ+k2mIcN-9 zk_`hs6u6~=V&$|~wWGrVRqVlG_NLxlM)jH+Re#7pyk2VUe8h>Nd)0>kpj0cir`j^j zDM9>r7AhS#3Z-_P0pLT6*%@0{6)J@V8JDr>tcBgEZ*X`Q-py@_#BaG>2+LpcBJgFR zvel4Bz!p&D;mtHQFk~P)gaBBpY?-)WIRyxB7cmsV8yd%WPs^6(5OEYrm_rrfV_k~V zR{5P;-M4Ute#H#}t~>?+YML1B3>--c#Gy=QuiWuV>@qKbQpEqBmSg+yo#{^Hp`kOE zjw?!@o*;0kz8!h!OBiVCM;hAORD%MibAo`4l!jQt(d#CT6o$`)<_GE?^*;pI!@){6Wm?#xN2p7=+E7@+ux` zmIx@1M>InB$+K%%pwo@RUPAd8VzUZxxl%foRv{C3H z?2rk|)WVgwp*8MbMQeI@`ZU98&CnXjo<&vdAP=E6t>uJmI?1i9*K*uWTLuouA zDkDc|XlcCeX9|v&u3=)&oW)tG4bfRx&p|W@?54eh*;MCRPWz#ZOCMMoV!7tv#rG}q zYUOH`cr(an!uL)ag0q%1%AJW-wxW!))X!?eS-PtCBS*}aP1y3qZfvms!bBmNPIjjm%9pS=ONuU&?uTSlnfWTRA@$@w7Ot?+g*ngfcNI-4f?J*KW)}Pngq&rbrS9N&4 zf-c~-%8KLv#k^L9#W$FARTHYJh{d6gadpAL3Q~&mRxE?t_TxBc3h&UHlxI+Ti7%in z94R1T)+*JjaUnd2#_*2zm=w6w@TukvM>o8A--KU4SbDk9_l{Uasu(xj$dvKq9#%E) zmv9y3T@QmysMkWN1FdpRO*|oXosCA^m9>-sBk?t1J?p`5eG+Y#$E@Cqiu)*c;Gz>b zWG=6*JBke$X-Pn1D*Yh2p0LJ>PD3R&Yu~Quu1XH<(CFmDPp&JY|2m5RaAupPp z$dTa8rz^cKVE6?=4QuAakQHi^s!pu-NY#AC&{|abeXh>h|$;L$L z=5Cj@6M7>kz2}6Bhu=2S3SuqVGHW<8J?9h%u6JJk$|RIiAF{=n$jT0v$E4S(lzRWb zu)ReMn_NGX_*#qW#8#a?{OU*(>ce;{{koTII-9GE;p*y8!O%;oB!q*e7=T}_oS2H1rK@TW=Q<{3w=W=? zD~nWhKZ)Rm$mPmS-zTq82Te8Ex{`CC1#gjKs%!+$VI@-oXjrQ1;#O(^w?&7~gdCkJY*V-_PM~y+ zca6c)nkx{)DuExUp+g)nlqVtq?hkvbMLji#7wf|!zV+^-A{@0|!X^|O5z9*2DoLw; zpN^Df*v>z#UvrUzK+)@$m3R#sBt~cXD=R$r;1Ts-A8D;};@Y8u_*yS-hZ&M;+Lqw} zxF-aaHSm42Bbj(^Thy?iKC*VUM!e60Jcpy%fh3jPQQEJwSXV=(aV3;aX%N;pm5g@b ztUekx5CPM0$Tq9FM;(F=g}{NkcEhN8&h{`SP}j>s4p5EQ!SXyJDXX62%F$4%u8)^k zLv?dv&uY2%Mc&H)>Qr4SUC7I(T9(tqTfrn4e3{PHWC#{aq~KH*#D@_nvz*=;_PQUsR-($~~e-p5La@jVF; z<14U-V8+&*XsB#_<^wgJcdBfD|+}}wl8o*I5m%B< z*^7%|3hb=2wNkWIwVPzaoWZ&w1mgPe!e2N@)f1SLljYvd1$`PvsOsX4zaU3c*{WYa zsCv?%(-WelY4cedaL_)&C~dQw%yG$W^~34XByzdumc-J!*%9Jtt-{9cJ@Ih4apSLwZ_t7(T-Umt+pxiahU(ho zfM-vi#f|zPgoBd(6Tk|heqso?)uftyQ6fSWy({!|Z`T`uQDOO=SvPUJ+_Tk1P^>k_8@t`a z;4zM+FL8#4WW}mS`38raC?RY7m=FYC#(L6!-k4qHJ#|y!Jyq(lno#4$-XH)UT)awb z4mr|RG;W+&Qw;CWEAC)uOZ)PKp=Nuf3Y*?A-k!a8cNtBql9Ps}K`Of0i(}qb+ji$I zxvJID4kvV4;Q%yN6rLv`jO6Dc8m+_z5GZ2RTb=6#a-Eg2ft6=@g+kQU67yPldJwZ= zBgqPS|6u!V%qCxWmDy~Cz?eRvxpk`Xn_5N5#^ThF+tizhMmKp2CF}Imngf3T0idQL zMG$kT%PtqW!QnwDh0;GLuuam{6Bnx*9)WYAPL@zo>4B2#?ZQ z9V#=a`a;O0w!&`LcTZ_e;F8S_H1*TuGB2u|NpPEr@Kav>mB!kbP{2CTz=$TEZ8JB6%ekr>RN?UDSEM_}XMsAb1KY=mE2+I7j zLYfj9-j3;wQ$Bn>COKyXGiOZD?3&fyE@|EETt)U!QATkCM4rVZu8PVS?IAyb|Iwk6 z`=7BrJbF;pn`d-&!bB7K(2(>f4_3&IBxe0tXdV?T^7T@X47BU`M)jd*tvZC~yBJa@ z!?za7{5XM0Pmh3?uvvMl`gP(F6|0y1O%&(Fat%fgw{W`~J-Og-U)M))0W+;phaO6( z?W=_WCizO-3MIHQVVW zxHcf_u(bL1`O(8Ca1wR#J9mfg#ZK}R)2=hc+2a}onPrCpJ+m-6h|F5+d(6BRZPXAY zt7Qv3HZ5p)Lm!-=jn|k=r;8DNy(+X5Bd(4aCTpn7 z9J38+e^`vqNA>vyk11b|3^cUD-+8&un_V56du>o3qMn6W-52~ezbxdmr=+ZgD-3@2 zEw1|bY*jK32gLGmtR{z6L@j>o98sMFC9ax5;QyxTO#ti4?)v_D@4iKP`_sPfi!I5r z#gMUilD#GX1rK(0qbU~wNCFC;FXNoLLNKZ_kACL5GHi&FF9zBiL$S}=6>n> zIa!KEN$vpNw|o+9Xma?p)nU30lcH~I;-28c@L_K(GKB?EDPc75%^{jg7Gn2G5NI>O zg#+wE`cfcMsY2ZnEF>X(wgYm0lq=Wdh-ihNE7e0$Dq^9g$J}c_T=2TLfkQB4TG`=O zDDwmppp9soxIPjl9s0_4p342bakhBLIroWw0{ply(r(&KZaFrZZLIA@`qaHV@x&jX zEm)!vl@<0Q1dP$MX8JJ6CMITVnC{1a1VAOqho9Qro*ylEyAMTT;75VXsy6th8#G)0 z-e+x;EpAv)I};PTYn4r_J>{BR z!K+MyYzcj$9Q@lS-F>cf8@Fi*NvjJ&QAznB4;lawJ;rNZ#D8sgoga2tOxEFIv~L9h zq!zf;R0P+=cbpf@R7LSDv&=Dq(}xjlAgyu_J6bwrLyM0{UPIiU?pTb*A@6+ifcr12 z1@8z`0#0dng&!+;laLBFs<3#4-$o0<0Zw~38uUe2hJ>@pMG!2#UY`~|^m~FZEEPem zbEkg1;I;J_4pn5}8+ON5>N15OiG2#^%c{p6hENq0c*d>&$%1zyrdZgO4wwIU!7DF| zz?uRt3dCcv^}_eAyC3AI{d+7YhNY|Mi54l}oK4NjNsZ)$uK;U5FO}GcQirbyrdx{y zi^4l(@%-rmIWR2E`|5svI~9!GzOw!z7ubGma@%sjsuYVT+z^4QCn8V&e=Am-XR9{C z-2zQXB!XuHF=emnfe{(c{q-mKV)xD`fshMI3-i{2 zkgvGqK|?rN~gDC7lVCP=A)y%Q}To10vBIM1(R^SKOs{3SJkG z#&7F&TZ8sPy|&70hFEVGENV#+{bxdFV?n;ARn7U6Ag)&s^LUV^A|>}i%gk{k z61#;h9Cg{Mu;R5yM9MR8^2c@eRi#AOr|$MNxWD+hf>)L-il}6F5aW9FQ{bkSAhktg zkTLW|MSlpqr@MO`9Wf%)@A5xi@P?KmMM@?ydr$9f=GQ@D9O0-}4{P*fzW~?;r~3&X z=Xu?6X>B=$sfN|zC~FU@(`~1tmH;&1Y7Sc3lV@S|be#HDc;IT=w(7j=I(Ki1#B!KE zVDbIcjhy#0J?`~iEO>+NU(#;HfAa1NVt(1TVOQ0Ffv&VPS2iluLb@i~T7lW3ju^jO zIf?LadqXL+zOpirOl0eZvRw&c`l<$!`*Nw0d}(uKX-%G_4Vk{~Oe$AH;=Al79P3i$ z8UCaagM;L%^EWq~tH$0>a)>j#XL9AG8(VJGq>m;W5*>+DzLvz~3uWCftXrDtBAM;Y z)>P*j=rW&9@OGF?bVAtw+wvdz=9j{s`R11~iUjQBxpreGV;J+#`p+tbNMEWGT0a-- zn<*^9*;|gBHc8N{jhZ7W#gd0;ZgSD68+R^-i^rx5WaW`F#!A0i`krC0#S4eWUF}DP zz2+SOzP_M^iFwh&xbhaRYNGE)klI$YFOGK5wBJ?tLq-XV$#Q$&8ul7eMc&Q(V8FB7 zvfF)>OEodsL#cE9hn#d&pe`gpMA|v)>x4L-l?N{SHp94Npt7Dv%aiJTk2t_iL1{}6 zuFRdBT(Y?2Zo9)E()J39Utwhh)^pEmRr+~vC5JJ$@B_Trt>cYU3S+@vozl+@>UCXlB2=(_!edtgQuN+scln2h zy*Bqr+E-k~KN<$Y=&x*~TV8+9YG5F`bSKP&q4tsaV2YTG?ixn(-}F%$81i$d@z1C-oARSJu0U zXTTmo3Ci#ZP=1lqP0bKckw&2}xB#5xA7jLMrqx{+6JznRTX{b0)el&?`!f_}#{S2T zcU7v(zTjRYS|B?Bb0QK#u=ThKO)!!Aj(hHNKQ`=bTr%r~rH3kR;&PqH!O0MV>r1zA zIA*zWgY0h&c(v$9qjRWLgZX`sh?qOZ>Lk7G z&KGMJx!Io@_G0eCw6%DRx?ka-ywTEaO++b&&YW3B1TFcig8n;51(q2$n35tgKi}h45Sc!J6jP7qNCl%l zRMQxq!_dH`RxWhM1LyQ-0#Cmtju+)xkk-lrV7RHeBqe7L%No(5_^y=)6<~{aQDbq* z>6rVaPY!$e9SV?G6&iavkjYmq;~s0p}&QczV*EHB+PAaX2V1vH9!A}yxI$ebt8J?WWh z0W|vV&okqDyvgyK{;KiC5&RoieC^jFbm0Um!NseC{V3*TjpVy^`cec%EkF(z`Dec{ z>~$SinufLCkpHI_?o9d5?E5{0ut`xhquaYe^vsMf67l;7#4No@ZpXRN7d=PZpa0^p zR~ZXZG`Qw}26%ZfGzhmiYFUbrcZ%-hk+pi5hi6r)C*V@*EEPe2Jcf(a{M6W2E(T;| zEEd%T=1A;TKA}J|_`vVi-nfv^@{4&sXY3#Z=zV;3Hio|(^0Emy9VWo7OAP645=M8( z++lbc_*0b2ig4;SEkoQ0UpvB{2{N~VIq%9gQP9=f{G4`w_J2dmurHHVZ!Nz>#y`$4 z6?vNbPk4=+R(>YdqvE`hg)+a>NJ$cwj~oX?w^OWDy+Ck_Z5$(b}l; z3>tSml1bC?V22U=%54oGmXQByG;(u7teS?M2vA&* zv@(T41EZ57L`x=PV*Bj#&m* zG65b}V(#zG{cgA@X+*qF$my^<@vbo5M$wB{p8WV_9K>5Ii(Wy&N!Z;p;evwgtzBg# z87@r`7lFC1d|j%Bf~hrRK(6jcc2-<0N%as!L5M_IX)=SmXEwPX17D^(S5irmE_N?GsA_|4h7V6X+RxJ)nuM#ohhfu-CuGM7Mo$LEQ+7 zkcovkl6M(zn~z9Hd{)jcBui&cl5P^9KEok7$)Hp#J?^{zC42~a7JBSUby z$v2nT*o^4)XvC8xex*ypE2dM9#U*rr2SpJ~c07l}4xWbh?u(L}EVhpfRM_am;jB(_ z`+SR@C#%zfDw3@Zaz+I#>rFGYHDLhefd(0j5$m2v{2qa#vl5oXV4Sk_u9Dl!+>Kv{ zGsPX}0kNIIaIoOY2i*u)cNaGux9n%<$b)1$kyp6XsO6%P`{VmcZ+eImDvM6flSGjb zM2Lj|5kJ!|p2u9c<{rJOXZ9#?X*x)@IA=NiScGS8`8OcaO%bUgO?WMC5%;z^c3q!( zo?S0iw#e=L{IEBCB%pA{m*4W^V2_4GV_&iE+zTofM=t%7&fylMAb6)d^!5>6e$;aJ zXX1X6lQ-QLe{ymIK_k%a zS6ZTC{elBrU0Q3LA{KQ(XD&|zKM`ui%&8A5&7{943uSO zXF|)AC^n24*9Y*>G;T|);~ZavxhLLQaHamPHWb0O6hrp;&!p+*B1vMGZC>49eG$ff zDZV(0a+i&}dQ+Ei9yL?*>i!HsS423!X00Nwt!;@N_v!qqG<2sTg7>`~4Pez&bez;W zuXFx#1V>$Xd5H)b^(6r{%ofAE!x7><`P__0vLa&Fqj+z*kNhrsI3Yh*OHGz?f6j%T zideCte5a8__@Q4zJQ6Ls=azmCsbGmz1en|Sqz(MA^|h#XOY+_c-qB@TNRJed8r1_m zcu>sqz-*YGC&dSjkR34i*m=${8Vf(H;{N-WqJGC?mwo3hO?kmII$u?0^%hz-o!9Z9^39=TbY-rPD zUsmr5e+11vZHAg-ktm$9hGYu1UO35zYkFcV7`R(m9>06~u&gi(U&Ojg)}0~GbU`fo z6%94&HvR`#q>PEo7b2v8IxPj>g|7{JZ`MUkK;Fbdv#+VA%{3f8Aw(9pAoo3AANIDj z;2m#o(mdRNC;)y8W!9M52-OkZJMW_381^Ri3Ku^!%SUyTYQb`ocqYtPyeHT-rrD~I z7M|eF4wYukj3^+1v0Evjl1^47X4|{{%h&`53EXd5<5TvPH-K=p`OTkqo zHtnGVx+T~7C&S+1T^y3m8zcLwbh>!k^M%Y$++}S?|p`9Xb!e~W7zwMOl{UjWo2chrb z!pjg}AXn_lC94(QuW({-Q|RPl}#@77w8CxSA{owMICN+zr~dn z5-4ND_bvbKZ6i3xNPfvGeeAz7hR!u+8lxzFPW26`Sc>FiLG^gcEVhLSulLK`tA9D{ z4HU&Z*^XBZx$^(U9@{My{;DQ(XH<+g=VUo#Pg_dr`#KvEZJohue2tkr7Qu}LMc>L1 zH~m-a+blfw8sg#hsfZigl!=UWnN?=RIbX=YwjMk4; zWRlg1(tAlv$jMffM$A!{9S1Oc$11ia6RDokR3ew^hbbj&D4oD^O;N)w35peFsf>vE zIfviamTXB|g7{n|-Fd0=CH<#=T<)DBuOZtB|JMQkSCZ)?zGK?e{mrm<_2uF@VzDUj zC`+Pt?tSGVfCDpg*8wif3y&W(YsrB?O(x9eTZRH-!fpqlI)M~*2}itJZuoCm>hMn$ zyIf}j{rWFic@E}=Zpj15=9{u=zNSzM9{qDzRE+DrR=R2 z1{T6Ar3UJ9rJ)h;INC%uYNz{$;SsNWn{bqIrF67UL%*j7*KD`1c$r!F9fUHRnlL|$ zvg+kAcQi7h9FC+9xHW6qQIekW@NuZAWJyiRZrkWW^|c^>HoE8lIS26logx)DC)89L zliYfmK4;E>kqxcE!(uvt50SNWC&&9!G*>Obq@{E`API0CXz~saDlF{hYq_$XAQF@k zogB`e69$Y$5A!3+Ax^FgWlY!-<%ocRLGbjxhy8rBtS^OEwP=QMtSJfyOso-;i%4~W z(WT3MwP?h<(id1R#axwZiC?2g6nN_3|M=Mm0D;8Y9eos!Vo$J|nS#OpVCeT(JwEF}j#J`UQ^kMuylD`ZBz znw!R78X`5?>z~1wL5>KUbW>A`!o*cYHPuCz%cFRDh$qyWkC^Ehb`XDvK>sGjYEmDw z5Dty97&`J0?^cXzhTN0fh}TmN)tk`t3aJy-r`SyZ>h=7H*N5af3W_sza+T3MBUESC z8HL^|+!AD5Jn6;JWy1P1^(Hm%rKr|4$}cTnAr6JLqlc<*wm@N%DRKBljCKf#wOc0Z z4IG^@1a5q0MI;)&JLjg$Mvzg=@V{9s$W%Q|tHg!#5LEI1HoWy>$7h0pMe4XEEfQpE z;l79bl-cRUm@7+MD|^zN3K5(;5?OFFk;rn3^WE~ax-}{x$L6T9IC5)_L=sES^y+mH z@gic%2xFLAD49M2>ghf2AQ2y5p7kIe~s|aTWdSXR(bOa#YwQ}TcSaM zSTbF%n1euABO8$v!*m*tzvVES1~|5p^SBoYG$rBnVNF8BduC*L5Y^|c!aQI7h@W;q z%irJbGp3l_>^@fwW+;wCZcgLXu`=lVnh~#}+;Y+mXwqj9o*vHKCFk@8_Z_t(-T*QJ z{q?w$bt4|mQjz=aXE{1q6uk1vgiFlz7DWPrnH9ut2HrK&jXsF};gKhy{~`SKj2XRsMHM2)o~1X&LeEnY7d|Dn2JZ zw3*B&NJ%kiAFp}^b`v#0eN@S6PInrdt}RyLx{om02%|-B^sOj~vH^bTmbSNT+x|KfnpSwo9&A9&+ z_~8-Q{y2c$mCi}Nmoej zeZ9|zn}ZRn%(pTC_^FyqvVu&oXy;(IGPOC(!O8Rvx~ix8S#`R`PoSIoOy5_+k(`Un z|511#-3oV=dMTQ%Jm{|;aK~%l&6nbRqz{m{sR85}+ZX|s-pv$E!pfkH)kbU={aew+ zOR&F40iqQ9;@a@LOsK1my>Qnu&q2R8@Sze|-V+%kIgVgXGWL)?(2u6ml{UazL((8{ za;_70I>7bNl+?o=5-Z1qc^lPS5VYTj05pC!C<$rUtUF5XB6haqW_Us6Es@{ zZ5PDBkWl{N1S)QD!^@nmi-acu=0OfiqO}A)0(8PF2T?1@r1OHAd(FMxjC4K%P>UX& z)jL9>hqgTiI&@wh^~^}6(N^E1L0L$B40-Ztj*1$&)NZa%2iHtz+FJe6=Ij^yhYWk! zjkjX?#Jh>)0D*Ptoa=5I_8RdAU=N??UaPXZ)6a5Ppd!WpVO!edMequS(bTtXHh+-| zg7GVAu1Y9vPtsUw`qeEu3fMPsCZ_^zm)P28QcWF;!b8aM;wC@NyYK24_I^j|^7p@} z$s%QYHC?b0=u%DGJ`nTdnE66)QU_vX##Z)fhPL^K^(XMddSQybVa&iCdKuOz8??Gl zR2c`=l;NzH5lArx{!%PL{&!U{FwNBT823JidkUX61w&n2nf{H8}7pW$6h3QvW_st2f1ZD z8YLat7;^1Fcd~ETyO=QmVJRU(q4%D+R6mBXrEu)_{qco6fV~)Sst%ck;ew0Z8f7i_lB2R7 zKfoLXTcUaeiO@k$_IZD$*X`dj>{az6nBqDgbXB#ce-LdSx}$DM%E2hrTtH1~WXV-- z!)jJ57?iT%kuUmr7lkpLui?*xdu?FY+X})K%>2{^ekKpeGo5xy+ zMLBGB#Y?AMY6n)BGQLXFxj{-d-Y4LxaX-UPwXq0AB~gc8*ok%=AxQC`PS=d>@DOiP;A%)D;=ewz{TzzM3}7Dp88Rm;+4daGmNtX?CV2T*y4L%1ep z>>NiFtGbIQ`#4akj8-1dtG6pg!<@yAYg?TbvNhG=g7G#>vs@fGqB~zQUarJc^LrTu z10LnaJM7tDD?G7XW5}@509hF6BsiNpg*%eg0nPeI&MQ zbqF-QItcXi8Sl2bktH1JEUK}7YNfN!RE52Tdlb=1YWJ4m`;NMtP+Rx;L)Zsy<2%64 z62pT6Yx@2RFnK5j1-!qiHHuTy2eXOgm@y=_I~G-SBb@c*{p6>~Ac_?zSd$UufA+QyK9I#DS%S5`8EfN$dwLA*eE8#& z?$GgJ@6mcydpCL7Q!XkyiiSP*Rj^!MkwAz2ywf$G8upgl=F^xrkz|=%#ozfY2h}E; z)NarmH%Fqg6GXB5<^WlUB=614?rUACTXz`+>ry{~35m*FZu{nBx|(qPTs?(StMivq z>5}q%XCj~UhpUo=AT}p)W~(N}TcSHLd?QN~Aw^a*Wlib2b)>0*ElOR1#Y%KOPL+_K zt1_7=M+rrnP1GfMLq#svR8uOiIfD7CQBswbmSsyyQeDJG5XPADJ(N*?yrV8tL0Q<6 z1eKKha)y9*Z9o2PRb&wO%-OGmqkTb%%#MCosIHgdnQ!4`5cuzvCHn48%onE2LJ-J& z4X%0ps8@AXeEu_=n`5TPFa(~H^nEiRj;r|LggR3PxU$Qvf3I_Nhmv5p-b$J@Z3CtG zaD?FOusho|>Qz=7S~}grt>xO0rZ z6#>XAfeopZ!#yVOw*}*QW-7En8_EfWwxiK~xQE9&@Zje()?($Z&0GBqp4}vjUY3Zi z*{R-i*$ty!V-abdMEG~Q1HGeOd#OB0&2IXd;oge4x8UL%N4?HWG-{De*kb9Y+uiOP z#lPOlV3~W<)fp~lOp3ttzS@(r4quzYJ zm?$Bz$T9lp65BWAKE7?#tM7}>;3-I#5`Grf3~Yv~YogJ+59Y|{7^u*y286*jG`ZIY zM!o*ZHMg5)4Xg!An{DaukGON&N4+k0{X4!KE^_~b?N+%OKrGv+I@59sMj%0eMmGf{_1*e ztn}N%>NRejCRGL+y+u&~Q#4Kc{&F-v^}>BaZ@VVMv7s0@a&FjS&!P&!Qv_-+6PKyN8Sx zuU^*Oo7NmR7P$UeG_F*<#>ZUZJdaK%sO|2rT$DY2VlKo@pOWxV8gKgTc(k zX6~5K7ZHYP20K$q46U)X58e7f)*~?554peMq|vPoje0%FfO8UWamjr*OSdr>JoCOX zxx(E&I7&6+#H{-*4!TPytV3K?;ACngSlZn09Ri#JpMRLQ=EI}j(VZ~@EALK`?uYSf zT*dMvu*2Py=(`&j-$e5s*$y7$XtNmU&V>7sBaDpt@((7&jtO_{GaO)shFyL^b2ng5 znGJcJl*i|yMUxYXt&-q#nG3K@ceR9i`JSybmvKHb&sc5XBXGbIRKz*#zHp2MemUs> zBt74u79Rr@8+1Fw`AO&F2;;ySv(j34N_j7#x+fcr8*6lhm z>NQl7+gx01;DJaOD$)9!opFE2ujD(4Eutis9a+zloaCmvc#^dW$8Wh0anRsCO?#&= zHa<6x+AH{;K`*jMjqQNI9U~ZcbX0t@xVW1#5&EmU-B(YIdKE5qdekF>syF67z)@wZ zG49=W^bK`+ZZ8)1vrf$C4dg-%tiy%Q@O~;4!{P9W0>%d>LrR;JQ#w{~MqsL{LM{c@ zOW$?eE3%MEg%oe?35lQ@*1E3 zpucZSr`z?$Pof@a;`~*!3wF5=T^{wS&jvPXD#t37nMr%)f?EHm zT)1MV%S^!(LZ8O3k`OleBeavcoC{LsKTC1}#yALQaT~7i+T$#Uxt8$LRbQCL->+5P z4Em9SrtyurNO%!|G>WmA#1yC*rg`bX^RZ5DrNS9rP}q_tu8n$Iw`x+X7HWqLZ&wt) z-0!X=r`dvemGg=_0kfzLdr7d+G2=dQ9il9MJn`fql^U06A^_B2v-ui=ZwCRVU`$LUOKPi{CN;t;8m*UyIC=LAQW=qJ$ z`lybI2lO)`>v2F@9%7=<4`UId0?&sz!Jqw+|6KAFdCtP)@RDPi&v1MKJBHBiGt;7O zUURK_dO4I1y)6vXZ9G#uJi&th^dyEZ0E4B7hUBEr@1aQOt-Wsh$FF;*4tr5--vu_y zE81yZxkfZMs&|&GdGSBJ5PI808#1M^ZEei^Y}@ZuMP^|1*=hISr>|4f%+XdXJvaO5 zwg5(+YtvMnY>9f)?3d@_l}NF+;6FG10Pn~}p-8)q#T8ER5qBVc-}9fI=e?XfBDETc zVfpDgXFCuYNnhYUGXb|-pL1G7dKND=45yfdm;C2Dx$p)kiqAj0Hh2<3DgmGWyo>P^ zVtGafQhzQs<}U8MWB&8)`sikr(jbYSl_K|_mvOD)Qj2~;n6td}6Tx76EK%pv+iTs| z$Kz8A0k7fy(>vF_rfU17%|(&NVifI!JPZ&0XAN%k=dODl6DCVPGZqI?6Nk4sz2(G1 z284lHK?u*Z3#+DRj>T#2iD9Lj7LkR|jn`>kvonce-zl@mx<+I^^jS~GS>$NwtzGW3 zzj)pI1C%h3x#vP5-69LXL?l!ldTXEi{4ZVi=9l6{_wR!EXCax-4fSmGqBrj;?PV~_ zEyS+NYl{_0gr1rTwDlk`)mWA(G4G9D(v<}E`R79Lt=jU>#+m4NRfmV~RZ}G9R}^u6 zE?W%|6pQjq6zz#=hn}@@cz>3rG;r+%&xAs6Nj&uTX|5h= zlWrF$^B|qGt`Hd9H-G)QSAW3P_qHx(!;#zM*72X-4}~E&f`DzhPSV^NLwU~*)6Hq# zuLPRU4{(x1n}%=abxH`m9ddnLIj^FGuvBtA)6I*Gcg%hG^Vjh~jc9L42uXU;3H9r3y2Ni?_tu5q zZg4v}*cpBrcmJ4!4Y0_(rVu=N0N#jPJI{n`_u=tNnIc2JH(5Sxa?gx-x9G#4UJOM; zBtZkcgW7kyH-DRLO(j#-oQZhGrVp(NMo&+Lxzr0<|2eKrh)u4s`484FsPKG3KWW2_m&C_g%hpz`-;Rl+DmsLET6EQY@%OKL2h&FTrq|x-e)~(;y-v53|Ko7CyYuDi zUP<_^7FT$>+v|V#&VRh_&4!j#w}2AiRktb1-JMTmQb|fCWU5H=kxJEM@e0E@*^|oE zrb_*p*ClaY#Q)%)-ss^1Jc`v(b3RzgKViG_fO`-rxx2D#U^fEy< zl0+_^tD@2=@TeD$q>KC33Uw^_A6s%i z`Uw;x4KbWUEy8N0M#+Q12%I=Zf6EJfM`h@vBk%soCr7FW&*e{KGo0h`fI7r?Z?cQe@f1DW8 z#;nXBEqCIy9a|&Oo6~c0x)I&lD|?7*<_C>es<02#gq8y{t_bug;kGH6U&f3zyd+-E zX=|aKfzeu)AXic7?B`G6-A{gc)Y}p=-O2JP_o-hV^?s;UV83FP$Zm06zAU4@lY;Yx z`^0BPy|(O%UW9u#+H)pyz%{-*>b;J}dHZKay|E1_X;3>Yi*Y`1i{|<%8a$p9II=9Q z;Kh2sN*#BzJKd}Av96u|a%;$zahpY@#VhS3zJ(_TduadyW_6Fteh$4t6FNx4r#8)g zS3HbyVtGHQQPv3i!Jgfy*_Wz<@ zyZl|7_U1lVo$=%ThLUV0#aL2R$y_aN4B2#3Rf?R0sN$BV(^~rWZ&=DgOKe#{Cw$bp6k{I>jMmiqqDe5ENnW{Mf z1aP8zN^19{3=SeiBrmrNc?KxI=BL75p)l$%i$fr;-5X^P zZkm&djtJ)8U_>$T{jZ}oBD*89pF7P9PI?it*Kxn8A{#** zsAAo#{IXzM5$8N$a>bx{r`VrK_q$I316TgWsMqWHA6szeI6ClZG`wDI*Lr0gtsa8 z|GddNbJS8?AXyXRv0dHcj(vcsbG81cS3?l}x2i&`UG5TRZ){e;&q@o=V&~?59Sx(3 zmO!wKiXQKHlq3_=zH8!_X)(j2Zs&KhIr5Z(G6k<&D~?7AG3%ZgQp))1j1X%b8HS`Y;{tOH4qJhcZvZ6Arc-s;y}>gdW6;oVnJ+Vi>63v<_EvLLXHSd66-6tl<@KZb}Mk7`|eS1 z9VJN~`c7ypZd8Rtpvuqcw4{@`$lX%K?&U#sg_PH~s#2A1UR?IBfh0k;W z9&TCCwgbb;_C&nk*;w%}tMp&Oep;3t$q8@f4R3BRycx-+eHVB4Fmzo{B(ZKTnDNVf zb1O6iB(mhnuyyTm-$C2qewB9pUU!?1KLNxmxfZ}9z4-#6QA*&;sgxKXoxm356qxS! zCzMo88SAz!`X57x4VHUNE^0@4@5gi?F6w!Mn<>r zDx>yJX6->Nj+l;wk4E%dqePkm%{1GD|Hc9n5}d-f_A@8O*f34MHaO~SbRWPdR3Rt$ zDfc&6dm3Fcrk&QKbg%wgulg%O?F2ra5n%IpW5xUccRI@fR%e$d^bt=~)1 zyEQp4z}P2HeSmyc#M(7uz9elZCIxK_EW~tYn7KQ!`oLnWV)fbR(#KJut0*31V_BQ) zu~DP2@u!E}6@G3*G7XZXIU61+t_hZP#=Q5s|IQs78ozDyaqLqZDw5Hu$Hq-bx@>hH z!qT(89SM+e?B>ew3nP%Q=fc`F7#p(F)nM&uFQ+mBuC_p%IreV#B@P~PhfiUMu7oIH z`Y|3EvzTl@!j_NSH~F zno`Wo#I4KK+IP|nHQ~fU@h5;>o$bM#1D~bbcz!%5*mP%j;-OnO2Y~P)4EB)wGAGUM zhtH3C2kWD=1ijDs%OZ9}d1y@~xDJidTy*)D;RpKyrqht!7V(@;e6UmoqT@R_9whvQ zE$S}v-b2xHcNcR@FY>%lm|z`MJ}(w_K0-ACUJ*cJE9Ix=|PU42SvJ|n;j))kp$IX&p6#W8=g$HFiifxxsnWp*h zS#H^;aX4Y+&8DGBN6fd`NfB_yY$MBhK_U`!9al%aA-5Z=$hxM$5l~92113R8OVU3o zpBX1w_KN$%>nxtq$U!1c^5daLZuhI2;|1CQbAei3)CcSm);gD>nZX6a09vy$ZQAt? z>s*_k>c=zw^2>UnKO*CY6S=I^*sh~^1+tCFs*ZcISuRTfm+(b~Y=uo=Jc{iT0=W#e za<2}LdI`64gdK@;ku~$wb1!ug+|O|lb&1SrD}pVGzbI@2*5(Rl#JjOQ#UbGl#mq^7 zA&Z7sli8_Yd2XxTwb^r*2h?j$x>N>S!L39vkYq_jT5@(M95&xIm*c0S6Evt>L~u)u z^{kMxl8W^#SEI)=Rl&jP-3mMuh`E#q~(D8?i92;KU;e}D`yLOcRFq;86Hzq6Ge*+4xmovjVI(i{(0ARx^}v-CkrcPAVFac)n+i(WFh+P>V{4Prr%A)Sjg+pb(H_k z7|ZH7IAmEv+PqfhVp%%nKB8TSMgm5bIGeymb~BK`Ch_h?WHIgc=1B1@9v*@Jku!AG z=UfqAQ42%DbB|*vf#_axNoCwj4hZ1iSq!SeX@_B!z5BTYgfUcU+4$J;nrkwiVJJX8 zT^({?Nih*c0p&x^`*2!Jw4rkK-x1UOCBho#q`o491YWYd(L|Uh#wK?t2G^JzQz_jH z0@j@Et0D8kF>Fv1Bf|rq`zC!|5>-P2z~u+}DMeI){5GohvV5A8S8qg%DD{k}gXFlp zPxn#-j5dKoqe`|c3$w_)BqN|LMPEGN!i<3Bjfc^`e?w%Aa1)`1KGP_Ozh7%Z8uWHUH9)e+TX>8 zBSt$tObS3mY;cTk>`C}Vz==DcZfe|2#i-YkGC%YHrS5duN{sV)OG33G`tU$-^RavG z>s)`(88Ak#>FKcF!_RLJX~}f$)|F_nl4i~OuE!16!bi2o74PVb;2bg+!e#R_>F?vg z^MdCKjMaUi9tXebXpCHgDk&c5cPfxMlx_;{dbnZK+vz?{`}GknCNrwVJ{S+**ZuX6jOrA=Kn=#H6?nMN;k(|1M)nL1$B zzOo}4oeUy%O$Ax+8d`zO%MmcKGl+<<@h0|_l-`^Hd{i{UiPt(4D6mZNwA+`u{Coi7 zu2f^QkhWzBfyaz-fKh6Lp>zL%cDybcS28!lDo44c-&8Hv#cmCx+>>_HYD<>)(b?y= z+1I{Qte4=&{+U{cVnS z&dh{F#m=x%QF$2L>=S=e5B6}M?Ht9WSc%^5y03G*cL|3Su!a~D5|EhU*N$5xJm2gx zOmqnDn4ARC*A> zpJ9mZEyk!1^W#b75s|N_>0OTmUa5Mej4y+0PN^nWopWPdqu##hHAhs}%?;PrmT8t_ z@-V3;VZbDW5o*Y60$7W^x~=S^!CK-|X-lO=z9WnR916i+6GGl-DwQgO25Fv;yZ_S7 z=7$*pP~OmFS^TpLq&oWsX>+z3F&fxqYfj=x9LjM{e1By_s+{e&<|C<~V%(beV+zYV zme_gOHps5PrFHo#T|N+pwZV_mb|vZr=0@U4rlo{!!3iP2M6tQPjWFcBMRIaAe_r>P zhsaPDxUxF&sJGvDWepTdd)?2%tiB00U?0!uyYjwNF1ubhuLkJ&xS0{q8uCU>=ywp(NL(|nrBpw!<^SIYIK91op*RT(ZerHv$$LZeZYPxU17l~|Ut>3#C*p=w)WGFe$& zo~mR_RA~K>VyF%i4>adE&sy8zZ3#zh$~!D2w1dP!ika z+Wu9+tGpO5mNd7fZx>RzN``y#ixe=_I-Oq&$0$cKLENyDoa^Ks?+z&Pqw^C_VGC@eKzd#5bj5=I%yhTPm+XE;zY-h~|btr10@W(KfvM z7Ld@5d~!NqnP?;wfmBR5#}vOHlI6DY^C@{FEYE6y{U)A7g^N2Yj9nUR)O8eTCcdmR z>&$aKzf-{WZ`=KWt`v=`-4XT{?|@*A^EhdyST6|dJ`9fW^4y+~J&AS3UpBp!_na#>|y{!ArQVG+>+tj zM05a9fA^;QJMP?ZIvg#G7VbmFBsSfMc%*gq-8mlG7pTT5(am;*Ym?3(?ZpZ5wbYx- z+CgN*K%0;Wy{{E@zyBW!-plb=k!nvoaDV!>g4c1BqIk2CttDJuiN)~zLO~Y@3Ahfml^4C^uKjVr>m;d}dxwJ#_gAz- zEto3iW@NoFJ_d)9o3c>o8KTh8x-B1ez5idqtDOnBqmSJSS>Cbw&AMfiHtY)e1NkP4 zK@PK;DSjxKeRCieV%AM}Re_8OlNHQihmZ_xtU4i;y9}n!* zlJ6Cpf2Mkkxf9d0*$`Ei8Tb3uSqDD~q3C0Fwr=K@Gov&Q-B0~h0nH@~!VVU9wZTLX zZTBm;=JllVQM&VgUGUmk%+8hIrb)fE$`ZY^+a(fTkl46<*LnY=;GLj?vxOtu_6Y1P zq$U*6JMR7$H&9qMJngRkPtf3zNYN~*4Fk4NiacRo@oQ4ynE7N`D0*FshO+M%hlg#^ zsW(aNzHDu7h>QL1)BisR!hMalqmewQibS%NI8&@A%Oh%mZtgF43x8AadQf4r`r1#O zCAMYib;}DSuom%k&CprwoA)FMz4EsOuibr=w%+|E?Gg9YZwZf^pewuEr0^iiEX{5y z%r1oiZTE>TTOo;fQJ_p4ocrT<%VRwGn+nF zI#8ca)soLCS6;ITSD>EyBVyUg^U1PQX{zd@UktBnF!ren_Guk<@smZcPeF}j5KB|2 z*<~oWvd;Ym?Lf*3O$dR!6l!pdR9abdpQr6JMTA@LioOTl#BHMOUy8-=zK}!?Fh|?% zSr^u%k>J|+dC59YV2D+dYQ-?*OGRcrUgU?HX{Na(zYYew0KHh$gE_-2#?Y**glb=2 z*RWOad`(!T%s4cZlj^NWYCs&hD6!`0!oN2JiWum@Ey4=Kh)zw&JaLwR<`aD?r=v_cCPTO{P#{GyK%)kL=HWVO!kBlNp zWVgo0fk;VwYMh(AdP9RfX~}gP)lJSs$YG9l?~g=BanFQKiT$A%3*TW_gXDE8B4-v^ z5IvjqxTbigZ(=0*MU_(sW48N;A7zU2LG2!)f>+H_SK@{#T2ij0NVAhtV7=1nr)7O{a?&O6tWt(^HaqOePp@Mt^D0|CLCLQ@}m z_uXd&Z#CpD{a*!~zdk|RRBz(x`;_~P0O{zO!}~`cyP2OTc%OD(`$-TwiNJ*bHK%*+ zJ1@FL>V?!Dm6Oc-^s4RKB|}70g{Ue-k1SF7d7aH9a=1(Xbiq4a z32neKv~1o}%rN%~xgBwT#ILn!BPAQTur-pNbRYPcf>#!&pxF$Z=(|79+2&Ajkr~X@ z;qOrYu2N0{Cj!aa6!lxDb-9?mj+Ugh$ZetG zM>A`>z?)p+pTaG+yr}Nsv}Q9rD;<@H`o*AT$KPCa52?^`yC$g6v9>eYEm>l~WbJgn zL&1*DS~e3($k}_g4s`Iy7d0%2!E3osQK_SO$;gcKEvEZ^2gmc3t|BhbEe`=Fxw7VRm ztV6#cHX=|YHu1>?sJ@`gSn~i58cg5e_KU)yfVn>{j&@BvNYruhO|$fz)c^>km{YPG zBl4Zh0;*hpnGL`qyPx_rwAMon)wFw@{hd-ezO}GKdS!G2ygK{~X?~g|Ug_oA_WuST7G-wYv8_@pUCKP^3px?aC z{rG3WZ9o;s_o_SfD?qq`7y`+=oUE^1TWqa|Z*#d1T}LSOAQql=Uw#jkV=1z|snU=3 zwO3W6UZ7enNpT3?&JENgvKwl<9md%8^(Q3MuW1#(|WZ%55i&&{#ewD9SUIn=QR`9eK5>e9&q_&PUV3I{+~R)ubiu2tQcMKB z3RWMI@*UVT$+*lNJ5%sl>f`fs)OFL)O!-9)YQ#<7=zglsefTV0tfBl}^w8{!1)Xu9 z-Ne7V@s*WvFGX4CEmF2gNU#-sFbf5s>n_tfrJ(mYt) z?XN&&GVurnsS&?U6~$3LxX*KuApR?G21{#HyGb1%YgX%-{kEQW5JbrAly{m3I=C_M>o*&ys zo0+$_B;d751Z|13-g>i$If2g@ zc6DtDf$cO}2Z)C6gt2DjGy%EZQz&?s$nrw$swqqsO+7nq>d*)u&9hP^ZBa;pYtfSK zj7j@?MBhRp%NIVISA6s^NY*7>E)FMW$@n@qHa9j#zvj2M)&1cZfQN79xGNhkc&8l6 z(Yz}6A=Hqgq97Qur)*}U%1>_|u_E9%iIansmKJR2bS#iwMJZ2-wLkR3Kx0qD;!iU6~`X0Nwh73#YW@)j|C0{8YMXxjfKCfU;E%Dp^t%^ za<8$egZ@_TdP6nfmPLf`dx^WVbCc+6QQ8J%uTxb~i~s_2WGc1o!mVjQ*d1Ibc)2d? z*6bdWHtRy$H?S_D9h@kjDSMUkOKrwZ<$bE$F3SnYnvAZr1>Fw2zDQD+4(wq+hgV>!E^)nO zqxD8QN|2DS?BOeVmI7zCDJ0Hy2zt$2QW+__g<=U8$2Fzt-AK_i<`f+ESrs#SHP-P2 zmdzPuxeb)s2Q?dJm+gau(YZue6=BvVqFEUltWaaAf+P9%6$zOtMe#^eR6#iR991z}9t^2)vW zj?7^)$|P%5%D5_BQ&yI(Xv^2P5T~8KUWtEff{5|6RmuFuR7+!`Jd>k%vWg$0GpWRe zMdC)kwx%L^G)*FF$||F7NvB{IQ^|G;;t|GFvA&6(C}5JV&Eb;MSz47%)HacHs5X%) z&7(}g!iD83)8wbJLnMX#wqVkAnA zH3r}w*LT>KhDwIEO6I$QHn1>(LQ`b_9@_Z#<@*x^BHdEDP;Y`Pz>J7wWSlv3#)zM`N6WqElwOU{itaf$9z;wMpSHjycIo%$u*@s@zCc8#t zrmIdO|6DTpQTk5*CAn@|Cr04QS$H|i>jnG7Q21pvZP^_dRJkZ-wpR_EB9bGDDOp64D!Vq1AY}M)$!CQUT};}- zVJD;olS-+rfO{JdSAhQNqa*I0=L+5`<&uTlhIAXo=fKi1pzaU)LIgFj7|G?8;>CE* z6IAO9Y;@>!c9g+xb|>JQULd0reuEx8o`S_(F%CN^|1oSW3-pzAU*(CGGE?Fh9J~@= zE5K3g@|CEcdo4kEU@&O+Thvz*jJxQaTBXk0^r2F9>GAboztg}5aK0mE`@Vjz);xX zOuc+l&y)NS3@AMPNL~1)?nW!@98<~)OmTU@{Wcf6U9PR*{d|2mJSObOz_LB9WNE;m zR}#lY&EO7qsU1O3#l+l)II4{~QG!|bbxv9bVQSfXC~UY^C73n$+fiIwkp^vD2E{ZX zqXeGqq#Y+?%`H_u4fvJw?#rE++uZtfbhqS9q8D>-FcN=DqZd=jq}!x#Gp!@3T?n%P z4F~FpE-=h}nCKM)Wu}cey1^*UVaHrpoPI#^c>v0&cypNRYdUw4-7Zjk2&8%=@d=MnCImMbDK`W-I^l*T1U{Ol%Hb}z{S(4!a+n=B4OOU(~?(X?>J z7wol}>tzp7jKONK39(Lcy2WkV3cM&7&dqaFxnz8hMKWH;tr6f-?gYQ6wlroHoy;@b z-%s^w2(n0iSf2~h0$NS(<@8a`^qpjALKEG~63-N2orSiX*S-6qy!U~j%>mm3+tA&J zyRwH|*N%dhS_<69BsCG9Y;;Lzc_A8?qDU${cE4EIWBX_pMZp$z)Z54#4m4}t1D*8& zf%i^Qh=F$2)DUT<#*iM*U#a9r@bCSA+rI3@iM^W8-cB?AK}!lIcSoHH=i&{ zcdvEO-0?CKWLf0@{{zkVHHdp|(*f<^QQ8wk9?!eq;;1@{N?YYT1?+R=4s&M)p-59Y2U0On!hW zZn?@-K3kH^;&zj6z=@_oMcq=Vl;4#s&vuk0Q>B^IX6dwQ)7fN6CRyH-!c~XRAxZ_K z+0oJObVSued(+HI0NT9OOsdX_v7WWDMjX+ z3PLwC>0EiLt}2=8glS8Zbc;P>a5?fPR`pV;uC^qRsz@ZNsaiq>IYOGssyoCx1!3Wx z#yb^d4{IIS-tOn#8Sy?e66qsN=9*Ej-*#OC`~+H#$IMKJs!Eve`z&W~2!|e0#SYW^ z?m5BfYkgXro+v5SC#9J+<0_PoeQ}Xr`a9g8eu{+R6}G7jY1D^FMl~zeVR?sp`tu{+ z>o{^*a*Dw6+8dC`W%sMUK=S)4qsh{r_!U8U@Qe`E_;z>h7fE)$WZF%WOAQSL9;#;u zU{@xEz*@4eh-_ByG@?(W$CK^mCWl9~#g0qZu>D=P1(0Rm3$&ZW4vLJ4<9}>4Nk+|! zd;OQRy+UnX@x0Z4o2nB6xUSJ{@lEMZYIw0h5;Eu9$xl<#qA_AH7x4DkZm?3=Z)z3r zp#x&qy7_;>hcqgOAA^(=OttA)oFs!gh)?2)lJ9nWhB7DE>Dj_KE?D%#Hg!_cMRPV5 zy?@U_P2bd5$nP#^kN|~e{6o5SBo-Fri`>i)K`f~y2NpE-*AaL4cScB%XW<(r3JqAG z$}*)``C&_2Ud_p`}zw3DG7ej{zb>{(R!jAVQ8FKE_aF>2g&v6m1hv}Vc<5b!|Y5<9E6 zl}2!`C3}tDaLE1gmqxsIl0x*beJj^OC*7ZYdBppNr-}j{NvUxfSEZ3XD8(XWQEbLm zY;RfCPt%c%Ti)D)`9)chZ}hA8rttmIz)!l5|Ivt7J5W4EPFuzW+ZgZ^-3bE|_dw$! z_LC&kYg`QBqH>XwUZv*UxBlY@85?5yP}C89e=>slY}cQTc&!;cu#}Z0umSIMD_rcc z4B*R0T$w5HsC{?$|njenY0F!%n=V@Bw=riDaVgnWORL$tehl9#9QK5|9Zsh=nA9f(1x;c z;^+bsYfKu_56^=)v`ye=v4;H2{}}NO1GL(>w&2wU78?SlPU^#e#>Zvt8j@&qKNh%< z2j~XHybV^WfuV5p5xkX!3tZ#8u7Wo;l22g~raa)uo7sVDj2LO_fzlhY*XR6Wf{@K6 zfM=*a94WZn-(qdz0ms(jevq^ED6$!&Sc)3Mix+_QYxyL}|0Wgcz4E|4{$C^B)*!r! zh%#>6RiIZN2fbT>Ft!Gr6$Q#zNh>1;fH7&Gn=F#z3P<-zOKd>5{3b6buBtj%idYy@ z_#9mF5M3Ouwf9TiG2xraDDTDYKtOstzj9T$E=q4JG|pW*>nz9Hw#v?Uq(U25VJr z>x1Vjvt=nNr6zZgtED8dK2@oT5xHb@E?<`Ncl-J3G%5{DR_PB`G^or&kKaUSP&!{) zx4zDQLhaO4TWTZO?M_yeXHpgEmNcccN^loR?=8txBv5$d(q&k#L{rPmBBe^IN;~J8 z<0*8v?_MvAc%LT5p>OV{d-mZG?~r@#dq%ut+t-k$pc$Pa6h}v;fQ?kOH5^|&FT&E^ zC%I{(iUyeydC}eY2$g6^&MF;Wf!`KwC#HPu%`x{4e(kEJP7kIh6KihDb8I%)Wkjp| zv+o^ILV{4(ZF_6PyL>i`kcgRtH2w7v+m#h z;0Tcy{Xaw@o;obgY;R$Nqr7I82vNNTl^ThA-50o}xn9$=_eH9SzlVf^;PCJK;Suj& zMq|i_pfFeT6C>Ur_;CUu;oSp2IpR&hcuS+pk5|=cwV@M{m9BQ3H+j*?iRt@%>p0g4 z`bY&&@_`(< zCE>PHLT23vWu)#>j!u4Tfk$Rs8oVw~z#*AnJN71VL9#bJQpsKhy@%t$C%pY=J_rA2 z@fZRx!g~Y)CTI>}reX`sxUE~^YslRVT|tk*`wdIx2y5l|lsmc&l69E4uQ?3eRfl-rFL3iwc#Rv!KSbEImFw9;1(AEegPr7dmjCg+m-4u^2^8C>KVy%D8o!4dfd4{%^wG1I&)}tn<~WI;X?Qr*qEgq|~i$Nv)i7&ZE%X>Lhhbt(MfS zFp_4br-s2`Fjz7{3$pbo*aib8?Q+dx)|$03&NyJOS?}0pShJWk*uZ+t1#^G@w_4+U zo_n9?N;9Q8RbQnqyy5>QdfXjh+lCvg2!nZwOqt-UMK@s4dgiK=ay!=3ukM{}RRP{@ z-EhW#Z*kQ7qYsC$D5-L8NLuN2J2sy22P>k$S3~%yKalle#ajq{t9yA9vS*2R6^TI8 zuhWxKsYb)Ddo%23CG`PVx(FF(N<1Xjs(9z(x^5(NF?e&Bf@yKzGe*A1ajICL@X5cu zh4NSyq)+;QzuJcIK@m~{g-ijHtc)nB0B*Adr>+07>CK#8U`~CfLe@{JwBdyS~P6m**KF z(}8(jba?1lev)=Sdfxmwws`qlIs1H_G@R8;Cg~3$DJ!z^kQz{xKBT*C6{51>s3g5* z_3rC?&-j@$So;acL%cSs+Jb&Qh65j(yVI+zF2IRJlSxeXY7(*BW(7Z5^=Va`^kO?g zeAHs2MoRl&!yQ4gNLBwb#j9P{L6xWr{Z_7V4G!znwdIx|cz6^U?cO5sWw<1iW3><( zWZkOv@<;G}u;*8*@w#W&i`aUwQ_|;ZqU)7mf>mXj@}X${H3Bm18ca1TZ!@XJB?*;D z(>d<097V}HW30{ayiLIYju+u6!7>RkuFVl$TBGeGf)t{e$qlvYg(Gq(ey}&rZXSUU zIQfTJZgS|KmzYuVRL?_7+<)SXKSRpO%fjDL_(=RF#dOl6wy1hkBM(STR9MKUUZkks zc|t?9ey%g6Lg?o@zs9`C*^p1Zm38RR2>Ak<6f`my-G;wIY@4r38F&D!Dq>oFWJ~9^CAWFKVNFRdRk^HYiJ+ z!wZ$a3o(nF?8ww)v)N5?1e3D#!b~<*QBzWrsLJMwv$;%VPJTB*gql>z^aC=ybyOOa zZ-L6IfafCUc461WYtssBTSZmXt|eA*D9m&O;7SM>8B^3x^Dr4hFiq zC^8JvZQ7+lz4SfV3%X^iaak3crw?QR}D} zTE89@BpklcJU-*_76jv=5yTLq7aRP%5oV>Re<z7}*v(6Xe};1DG&OQB0t6d&O-?`&-S@oxjQ@5_0SGv|-C_^9X^F|Y;(|nVV_*tm z<@(m`ab_w=iRCtW&N|4fxd+_e`%H^okSsDTSp@!Gt^1d-BwZq~#r%+VX;3`BV4D04 zf+R!p&{g;QF{-|~e`33sOi>W|G{AtO_br`EMX9UFM^z_YiuEEHuF0ejLXxfyxo>i+ z5`T0p)CcIHJYu3q<1wBOkzoxXW1aDTy2-@J&?SyoeJJoKEvpL@j>$KxJuo8br-uME z%+6sHNzN3zYzhfxJ1Gp5uBnBF1DKeH$ZE^X;MY0m#<`GAJP=+IkVg2{nEY24+AoU? zwb>XY&5=8pMUW_Fg^JFcP>ZO6l{?%qDsU3t?~kcpq+>Lg!vi>Np!xZ{=_Aw9(=cBmie_u~|o4z0~^9D6-t0DW`tkYFJySR(X~cO7c2&2ywPR z|FtEGqZd7Ql;h)7kSt%>kt|STt=mA|%MI=wY};!jW&zQ2_dzRkv%2}%ToFuA`oE;f zyIrbAHAs!eU((w*Nw2d51p%4S2#y0Q15xSbv_G}WL;FZGmq%oW-U~!+nzU$7%bT+ zy;<&umadJGOp@qU@DZiKVz;dIj94#%?J>*D}fVX%;?$N?M36t@-tGI z%DHSrH(aERL9`@MJK1Y=kJ+wp|H!sA8^u|HF}cMHbWBlM(2cd9@mFt-MJ?B~8E7vT zN(>H}!J<5tfLY9Lm~iYu0c=QC|wQOTbgG(mnn!gZ^GB)3E%` z%+pF*79%YMF5FI)!^mtaYFa2FY2XB*o{&BH)rMiI)xh7EE+JJ&$=?#jZpx53+pN1{ zSV!Wp3n^tGY}|#;M;HRpB3%E+2K{23*cDz0AmLB9Lxk5kVLd3IVhhmHEGd_PIKF9KD}JWIz^=;#s=juX*@ zynUyM88T-(>)SoT=(-GJFkAIzR4;LNgUHuP=@?qZ9bN>*<7MH~kvhpKL;E?nV@X~f zvPJdf%Z#Un=P1tWBv+loL|3!i-A6w$=y#S!F?br8A`|5}B4Zdzo#$TqBqag|2^cVY z#!`LdO@m3zrMkm9lEOX)ewuQ>#fwo|eNN4#_0+IFZw15;l4#3;gj!M^MLwQa@p2+C zD?UT*!w?qJ@L$%l>>y$v7AeJj4?la{uFp|&&R6pr>@DxK+-TONR8TNw-$@f_WGRqF z73!%EMisa=>E8JTMq$Fxs8xC$pp0`vtobA@rVJNFO4Iu5SnU^BMhRt^G`Erol2tRH zlHPD?A>$ZuWhnV3g{_XsmQf63%oh!4qWBAH^4#x#nR0w?x3j|(&9ZgBU%iUQyY|BQmOZXH{OUz5UjKgN${7A&2q`0TuA@!1~9eUvPRhv|l$ zW@OQuP>_~M_EtFP2F5CaobRP6nc*mi53!GK*>82s383 zYU;YTe{Ik&N`yMsE4L#LvQIzFk=jTLUVe}!1N}CJwknEkOo)lScZe;cwR zA0&l$3XV7;!Ck#{MYHJz_hWy~XX1S=e-DwAT_G;Bj9q$_!mYSdS~LdLSFS?;NN$Y} z`A@tt=zlWbe>7lxmsl{+oVq=rLtTqLP%>X{TUR- z{>z4gwak9h&8mkfY(}FskYzR5Ky=1c) zY&#Zma+|M{t9{A+CJx^+tta%Axh6)_*~@0pnS8bx-L4yw&4dZ*!7g>g9?{i(qVZvj zb%*=z-wpb!&>}dJRx&iC9xJkUlvgd>}a|j;RYMa4(LO-c@VM>{sUA$pAa?lqBZUx_*GTy z=OL<7+?u7X$3-iRm1=xi+{@o(WJw22^s?zLiv)TV<1Ga-Lt7<~i{Jft5orAjqS$5K zyk2iyL}n@#LN#aOfxP$)3LcZg<(yE$vFDR%KI(Me#T;n5lGWZE6o`!DDTp zxKrr|2M+qJVKUPuK9twCf`H+Ji&x6Bk*KwS;vUgP2D@lqA^f z5SH5_o`&n+N2Uh-GGq>6aD*mPn9p|&mj?ZkCH@Fdw0Xg=(-K*`gw43+KzxC{)z>vm zwv$oVB$-DW+~&)J{yW{0D}#RB$`BovuDAnK`k9HePkJsHM6zEFhky(2`|iOx2^9=_6GGGr7*ps_e+2uUKuK=_}?VvoL0%tPg9|IV%t~ zuaXkkXsgmqLO9X!E`vO4#hyr1ygBT|7|shl;-$8 zM9X6HyDI2ocZD%4%j%iVX;Eg~>o4+swS1nm_C2F4Dv-CI_h{V3Fylq=M3x1$|UqEt}l za&?UF=ik8jWAqy2QusOMYb3LN_Aya)0!bh#X++c&-a%$#aX}0kv!Z=ds&@j(D7sZlx zEM|km$@OdXv1`lueP%A=(fs*#wd#0T0mtieY!LoN#_`EC`^0+p;h!7yTXxzkQjF|7a?phy%7voW-1bTAevI&g`Ein#Sae^clhb|h@y3Pn(u%OH<<^)cu zYq?vx+MS z??W9e$2^B~vkslfw8z=!j^sD>%%9pTsEC^0Qsq_`=J=qTYnq{M(g+hy}i!?F3-dP9{V z@xsD@P2>GsywYSO?XAU+Tdyx6X+b{9ys4g=b|>>=A*L2OPt}<-iZnbrnh%hwRHU^V zB%?l=m+4!Aq&aw86E$aa>a9EEJ*S2xF7LO|5O6+FREoPv%mW#-o;Z_}KHq<@4De`?u_hB(J)r>Y2d(`j|)U79<>|{f<&JQCc%kVaHzx6wV z{%W`B{~Gic%r-74uSpe`WrIqRu#$nbAr&u0u&6_#!KWkMOm?${#Rx9sQw7M$q$_f* z)s00<@8c=lBHl_a&?w+hWK<=ZOf(;S&$|~B*L0WA*h| zAq$6+)Vgfy=g(|v3SB=M5qx@a{isragQK)>7Xn^EqHA(O)q&mTx{+DyBPGo|TRY8peCmNtw8si(w6RzZg>q7k3jyQ^7??jP9J zkkA`9G0X08V5x3f;Qn?EV8bTskR66*R2um*=)WpYZI&(N&fPeWndUEIQXPo74?w4s zA=q*+cDawQgLCZ0age@}34Sji8HCo9KmXfsF8n*f7Yrjw1` z+HMf7Y;*s(ftgRt=vB9OBYW;9+Xe2UY>yCv0Sxg_ns2YYuc=X1!mHf!C!Ke}CO#NX zkU51<_wBZode$D~3br!LRVX)MU-zJ}Fjlv9vdYW5HsU^@2D2hhMLL)z$n_lSNh^;e zDJ*o!Dl@)!0ru=w0i)-N)AgCX#3ACcK@39Z@lp^Naf?MgX+cA}({?iu9EOM=*j)82 z$JBm(vNE=5Fu=tx7FQdsAaqQssNW#w|!-w6Mb`1JI$Mpys+g)xK zynfbui(bU=PMsOz#ZA6w^z(6)xjKH0r(D;|6hPr+t&=Rw?=^Aj9^Dfdo-DEtL8wi!^dhPc_<-TE&eI5@mt2CIUp@62JnnbP{R(+=TlB+U?zFnCSKS)L0Lz zURvB4iEs7BrjoBO1n3xYQ{OT6M_Pc%o->$y{+oNlA%i zWfFu~>t1|r&|k9=P;2rUB8b7ZMWJ7_5pA5eCqspS);l`&v8$Ad4gdaAV)U&=nlJeO zbe&-SQhs;puf*m52ABh2$xH`-TbJReRk@coUcfOa|Tob^YG-51SHL;Yh>>uKzk1C%!N%*TJcU0f@}^ z=~c}oJ!I|wUG87TQ3zbi1fSG3A<1g?=>oyay3%aDWZ6Qzoj0QylvnPEaG;L{scCepdGN*H(+3s5SE z0Bp$2lpP}AqJswMveKe0iOM)q0ws_^Lk7rU(pXQk_*hZ=NID*$za>>%T}Hq}Dwo}i zIM7^A^eLc9a#gN02_mC{#!cyVIoO44zX7%{kI%(WAP_tEH~)LU?_E^bHA$&qQ)1sz z$2Z3OQCX5+qA$*1Wn!ioDVpzI{r-U8yiJ7T!6^tuWm|fe;H;piB*M>h>*~dLJTe1~ zZEgpi<5JBpqEsiSnH#zaEHU15&JF&{fM1s|CShcx%RTozxsm#zpdYN+R)^(LULVJM9H*GCD;?<5mN8K zocLCW7#wP5vp_uZ8Na}_Q-&K;67X4oz&7fYQt$Z*F#NJGz19{kDwWQ2&J>F6E*(L| zsE~a7Kwek}s!c#x2C$0^e%^hP(~E$01S_oNT9^UT^E!K^Xi$>)IUD>YJOFUD;GE>% zBZ~%TaUM~0a%>t3-OaDd*q7aBeB`KwYv}(>P;3JPFVx7;U_@*&NJxTPdy)-BC~)j{ z>!Pqda|(4;?gRWF&y{M%KiKd7fnUvWUlk=p)|R+CF(84Su&)RQ=XQmXtO|s8wwq4$ z9Kye9KD@}0?9)C~q0;%^Dvgm>Xv^ z1GvLHt((Zx>dSH8%1q2hB8eR+N!ra?Sm}G<=@U~Lw z2Zq=bxxb=aOHVX5eifGqlzWR3SuCeo)~Prnb*s5TUHC#Yil-=xRBP(A`>kT0(=tbZ z!L-$F`Isvy^MrGk*cNj9S&5#muVm2wU<>^Ek~*kby}4SZ;+w)4^^lp+{_N(tpDbsh zZe#`WG8;HURgrPLF_ACJ=#X8p5~7%Gl^>EQ(^(3HKo1JJotC7r&ScRCTilb%LH{S- zGM`LU3t;%KY^hj;>$9t^VSeoNFRG{++>p`j(Y95b{vad4gp|s1F)!~KLlVZL_d-ZC z4JHl00~HR0VRX40wS)df4@2!|*ja^hj)>V3PVErcd7xz+RAdDcPLN*y8U#mAx?m+< zY^3*P$?%1n2~t{^k&vhd)Ra+LWwa(wL-%;J$$_mQp>vwe#diM^xVm-gb`t~L=b8rn zpWn*Tk}IkOHQbc)wZe~+H0Z3-U5E_p3-J$|V3C_1xL6fs&dDi23lN!%Rk6Y~v<~_s zRrYvufw__wCexi;9NXQkPDu?PXPfQhVSMUydGSCK0^F4TowS~{_uQ%7?V1}!?zIIh zhBIU)$2yH3Bi-_5zSUB29{W==@#JZ86j@OpTS>dfvt|jf)Gr4$?SozR#lUbpNw5Px zDdXo<-A4pPH5wM7`gz!1-pL; zx8SZxb>3_?=uM{=BuKX&;KW&%28zg3%tzz^uSjOez8-WI5!5-6$aEGbN)p++bQy9+ zx@ciCScko)JNZM2q245hd6`sx*ZFHx7u**~-(>g8_eCf>}c&F`zB(=RQ8*H!TL_Vnq%tZmtmqywtoc66l&9+8nFR zFLyPc81O4PybD$!Vm1wlM^P(YC!vOg&cE#M*9X={7FOzH^jCYNW$G^ zr#p-4U?$44z!ZmF?r%9`lQdZcu^ zvQH1-+&IQ|KC^Oc()}j8)x~pC#d9=o44<&beV;QmuJJPisN{RumM6>|#n^Pdd%un^ zAyF@)i>PcyU1!#IRAp-RT9nN`8S+{xHI0Y}nI3ch_SpfyDyoJth#I;qFdf=5(EIenErDF7>(qNB8Gh~y1O9RfW{qm>jM4b+PdRoD27SSu z|KfnZqQ=C4i4N}ZBD8~2Q6ev4cBWGIZJI3FpcNY$PnQ_4+>8l0jGH$TaKBZ)+M^Fx z69{=Zg;#@y@C^H1A# zNCRuG_J$we)JnoFQDei0w~)R2ELmmEFjPOeMkU!zKnyHF?cfP+(2Y;T*r?FlZSIAy z4)`16SU1o<6d3AG{@H;45(nTD+h{xHe*M1>_!nI3>ntmGMOzA;q8Uw*ly-&&>-^Yd z_eqY|R^#0;MvqH5KW9#H!*rF6c#FIFb^5h0It4fpV%3XKxOs-5Q8}!4VzJWHkeZOL zv>Z+vDkGqDm23P4^80cB>InCj2$-RO!N`o<(=??oE4>Usaztf_&XydH`j0j`9x$i4ARrbbpEp~;BL!1NFiUB{mf;41QyZ=i>`&$3-x zK>lYdAmsk^FIc{1@JcVLHu6Rb_&V<^wXt)TpVz`n60?JkZF7Bn={h z>aM-Y0zrvy9=1=7{AeEbB}_J9co=@?wg5yg@h-b&xITC`6-uHUD$?=7SP=kc#Qn?P zh_w9u-wya?wLq2JQKO5)4@)Z)ozO8flibn2XQeE)LTx4|beM3^tyimB&xV?ZpsVg{8R{{)s`!GiFNBw0|D(KjS|Czo3;> za8stEPr+wW*N-benL;7u_Gwu6Y)3 z1+?rf_!1ORzDyaMD0>RK1U}DD%q)|t$43+IgQC(*P7aw=ONB|J-Al-Y|YK%HzajW>3o%Yy>o=m3-t7f)w0rMrWIIN3lmsb;c5!MfAwqU5#=wbAf3 z(QBr*Cp&|Khd?qah+eb!b8y`uoqTMnM)okqO8N{jr6N7kfB5VNAR4NpJt z{sI3-BNdeYfV?Tdpr`3lv!2u;pMp*9b01`axW8rF2i8h7%YF{~%hY0%Sx>_>HcI?+ z9oJTfBIh%_C9L2DT3t+d9`^iaz{Jr~PbDVABnCkP;9cQ#-->#Sg0I`wOGP~-$+B!C zzc)RPXfZ6g%x(S60YBp|vRyE1raJMZEze67A^z_Yb+|RXYohtczm|X0q>cttYcFsH z24EV`7CojBLdgUj*FL>^;n|z)A*}EwD_+tuaNtF`1}s;jCc#`Qaso2)>)id{f;3}h z5F(=crFs_Y32yCg!%~PzI>Enx?9Tqj0e_48J+}M1C3Fc85c!{^xU__G0Rg*B2wm(K zTpyajoF~!Yik?^X;CBZ6!=87`jj>a|1`Tb_1$)2nx5=>gQ5DnZg#{H=<>Eo)&y}?` z|Lj@#v7TnHUhRIsEgEM-!CRelO?=(WXKx{Sgr-2{pt$Pu3lf$>prqZ;yL1^X9AeO@ z7fSF2R`o_CsIy4C7;O{b5egWlB?S#Z7&*_0i_*5;j4msz;rENGk=hC6erTksoQIr3{pSJyh?`>DK(q|QGG|L^alg*7 zfh;YjdDIDs>Ue#QyMf#ZNQB#w<6pwC;0@=@LyD*d?Yf2d4{A_!WtP{3M zrX|+agWFtm?Xo&%xwy-?`^DGbst5B%&xIZdJ2<#p;l7ryrz*iu9!C}NFa*0JCcBBG zQ_2!rMNS(DNW45gw1%-L@t6|#KmRL}*Fc{OA7$ZL8p>k#74~0o??jtuL1#dR-NPj{ zKf0^DDqf$=RcC&rqOzhfPKBs+G7~589b;*>NEDHbHOq6U;7qb_f2xT3l*vSn$o5=y zE+_Y|L>3pZECjbbnJrDn%Nsyt%d+K}^JqBbJw;SsNS2h6KQNI6zuj9}o2x78q4F54+hv5L>Q(DLo zdJSS^^Jm!{4i7u$h8+aYPzy;u7h$29xaj#&uX5xj*io*VE#T1Rm^Xp1>wn^iiMXDK;DTOIM3 zlTZR`hf;fug=hG4n+U*Z_fF1qx$m=G=sGV-!al)v!6wR)&&VUp%wa*M5*K7Xg9Bj= zF<1ibO<^US-k6^UK{g0w(t60!pt}D#g-q*;E)5Vby@&0xMP`E&O|6w6d^D!MImcTE zZm+IeVrog4-IF02x&j?KBp)!h8|pE>bg?-`)FsUiwvq(5~$sk2rY|lHfi&%{SM?E?qF-%*Z}Oh2re;c@?2Q?D}UI9Pkuw*za~+ zt`9^o)I{IYXyF&L!M?TM2OZs8@0Vomns32+YC5scGTS5$Wk7p?upCx3ekx+7zWGo4jO8|u;l}|Ib z2mE(MNg%Q8>f!UmQ|HhB1Y6>4C-dp61C9p}-S9$y`jAWnw)x80d?u)ll43oogb{DVxe>t2&dZnoL=}Vtgy=aeL{Ax0V(q z;>AQs;TMzniK|6~Rgw9mIj%%xSsY#(8y=kbbFVv$1+Ia-md#6M_CT=eYBF0(@R@x& zogDC2Ghd%B%MSRt$dE|y5E-_C04+(EDb#DtxLg;FUnbcCfq=GPOf$z&0sN;Us&itzsx6M8dpmZSgC&(-EXuH_@`MVEc$UrB+IZ%ozbRHQO;WFr z9L9OsA}K(J4Qld!m=LidOhamV+7)5TtMl?y<9PDsY#2p+9Fc#FH0$B(9-~E1K@5VR zP!>(#+kp4OA(b}`|Bz4Yx-cOd4TKBczK|J3(MpmA($nfLV-U+EwhkqYwS>{VL0Js9 zLz5MTqgDm|!MOX>axEz{ikW2HqND)7o;E6sWKkj__1K5OVvwZ0{wSe5}jR5h+M zoVdqnh3Xy7(e8MDOo9@tOTW$&%EcMOmnO}Lz?hrOzCv5Wor$@u9;14QrI-uR;y($)+g3zI9`1X&jdWeAq58jR$crEYlhfKRSt(PPQ<+uRp8 zQ0~5??E;TF&d=suqhhl)H^q}v`D}*g@ZD&dPJvn*;bdIaPip0LIn7G*LMh@`p&w+g6;-KD_E$q~@V!Wo8AQY-6tJSyV z#hkuuml8S%r8K#*Qt(be*qc*ob^z#Xi1o0}{q?~Ce`y|>lj%G6=n&I{X`rY?;JVN7 za|;0ge2cNe7Gzg(y%Fv!g_;3cXCiIKiDU zj+{=20*9*98Urs3;)tcfgqT}sve;JlM)rCHb_otff)6c~8^P}hN#hQhyc-Jq=ZwG{ z5y2@dS!xc*dTVnOrp1il*%9z(do@d#)Sgnz4Kr0eCyi-$x%wrZkn*a5J0-MZoBQB% z$V#)8^4z3{Dj0wk_*u>#SA>S)n``I90f|$$<8w)64P5Ltd<<0`Nu;8^syvU-1@)6y zocR#0Z2$4oHH06R7MGyQoV(Z^>?tlQt4WaYGo7t0OUFBlGRIMD+Dc17yvkA)MIctm zba7c-yu2)3be-}zHQC}^#oE%AiZs3~)$rBOl8KT|17MHZ%9ZOT#%*FJd@%>PoqzaT%_HLj%FZh~L+f~YTF(h`dry#r`)Rl*6(+A!0${B>)|O^t$I_1t!CkB!VfsyUGEp1J?s7}?R#T_?^n6D zul4)md@_oHAt7r}&Rp#4^v@#F2+3-g<-+YZQTF%(k$K$JuodeDfS>o-y&`Dj3>OJ#&TM?)OWxb7=Q+ zW|TNrv-^#|?)Tr7^nCO4d!CzCx`w~+_v_Y@=i}mB{-3>Ox=X58V}(TumL|8rTxcG( z3S;<+3iv4C>Ye5bvEG%x+3z<1+{2GYWXZ|6Y7tX{9KnGwU}WmPtp_R$Zc^YslSgYFs zr%I19cfg=Z9PP;boPqep_#4P36i~q8yZ_wpuQ=!zOoCE~q?ycV{-%9nOT0Xsx0Lb9 z?N=vcE0yOhHpd+N8n{=PzV0BTn@S0Mvh0>0e!E^5Fzx4YpnY`FliMe4lt6+`$PaN$oG0#48 zIXUKG(iM;vbqD|Ne!mRK9aUKDVwvH%dFEfJY&~Idsd-j2_cH6tj5oCF7vZkabS^PR ziTT%K1@&%sB%1K7Jw!Dap8=#03 z5lLr@(%^^PiF#C2N~I=qT^u2WW(9#6=}b)?iL-NYbBt&M_$hg7cn4u$}G$Pk7?d(8OkIZ>fk;9YTwt zW)F^Y=b62+f-Bc>g#+9dXVTytGT3FOp1UHJe*=+P{+5P>k4F8;tK)#mJKoptx7ORD zS)qoDwVnoKJ?&M}BMUFs?%wtOe!p+8LE+D^!v-VYPCxEJmrH=kByUd!%VuX$M8m1QBtjnGJHX#ZFq1SqpvZ_Y26WqHA{?vGTk z9+M6O3vZzb^g<(>?NZY(Xu;H_*!07yCgmGq&J5VEnL;M2=eb?K-|ruEzs7d+9*DZ~ zi%F=stgk$Rv5X*ku>e!gV#-)~ffHl$)Z}Q6{pF-u!)~VFrE&Ok>`*`=JKJO#P>i_WNIToqy2p zFU2}Yhg!hnaWk)N$QmxmYSN5hr9UDuQa2R6}qJ6U2(w3kkI(n#Afo$fWW zTZkO&1Rnug1`^bIj;(>pNj5&r71!|m!=1;Z;dVFh$$r0_*hEcz8?T)%@u_})mwPAM z(#@A8XN2Xd%VIchQ-soZ2msIJ)?k)$4%gN#{u~3r;!pwbgc^GNaG6{8g?@i5 zCn6{*sVY(r(w>Rr+~0BhQ|_<7$dsCep*+088Pjl9Xx`OkCUWf*I42hPWe0X?9ldm|GwlCiF@&fZ`MEU*zkt;wfcL}Gq)ScO)iLjHmD_`%voMA2$2<-hBU?RRz7FCUxpw>o33AmL~1q%HHmk&_nwBxqC1F@|)Fl zTE$`f>LM>bJUl&iT@ob9Q4wwO?|HxSX4k!azw%~t4`qKQhp-77Pr|bhEyIKdvI`3^ z4iltptLWge9ijX`a&Pw6-ke{K%|&vE5w1lP12e($Jtsc&%@4lWh6AVBk=nWHl%eSh zm$5s5IpPvxhHK`>b^>KC0~x>NoI_v%?>vp**fE~!=AYU)Ma2za*OI&hE;cDF$UMa6 zip*@(jLRSn4~y!Fz*Z9_IW#fLr0wSy)g^%Y;aC!9J48llW-@dsr~y)`p>tz<$hQ!| z!V`u2B9DflS)>TYq$J;tAnNB)gXSXI;xn)e`C!D@z*25JEL%zSuqJ+|2;A15d&wQ& zYnm-2Bv_#zTB99Ol*Kp13O1*7S8D9=^^)VN0wbMmN%qTp3YtrfHb3qaMHb3Arg((X zpgfj$`KpQfu3LBLG11*E=CbloI5y|3BM96)EXvdR?tN$1_s&tAiv9_ehhj01gXD{n z#_*o2_r9_Fd*w^svPq1l>4}2+7cdyJqC-1ETS%^LwXdw<>V5ZK*z>*S3OL6k-NFZ+ z=HQqyiau&p-fP_Zy@rHAX6yBqZTDW-`@P1ze9HdKjNkkG-tUzc#->NjKDhQ?+rIC0 z-+Oc4_iAUQ8W`kg+xNahKzv^Fv^AIo3{tE1`{s(MLk( zd6NK1Bx2996S(`1Pk`Fs9-^CI@}*x^X*Vx5$_?x9edoy!N>(8RGEr9Qc)1_HFm>sM zxm40t(rOp>w`)fFLvf|l&l3i#E5=8b4tIv5>^L43K%nk85t3gQ_HNz#w8U3|^kE)Erh`Bc5O0T<@+*|f5KR9jK zHZ0frP>fupTIZ$!&bPV4${T~I${kN4W<^SRQIOR%=n{#)L9tgWC?48!JHz}fG-7f} z5~{bC&r;rzw>n|ykhzU)knp>%i1~YO$*=#Q)?hOW6R7Lts`K|={q-Mo%A;2EXsaH% zQ$p5EFpuq~d;5Rm2W7j%)s@wqgR)9(w=Cjp9T}dC_DHO3^hhOvoia3YGz4NQtJbM) zel(xeU{mJ7*845Pk@>5_VHcvaQRcnS0}88FgGq!kv`uCjiX%%$7&0v)@rxHD^|Np5B3%>*spLq!q@k>wN>X(dx!P1!cUio6ZCP?`Lq&NVF_Nilbs2FAVAM@z zUVacM?ta5X$~k1ZhDH$y@BhNZNY}wjG9%7;?Gd&+s`y%ya^qfX ztf#N5CvYn?1Z$)|mw08R+Loq%CS!aQ{FMX{v$U!K@xg`8yyT zVP8nMH?n*C{_R&Hbw?HOE%&urUA5T2Fj1s&NDEjV4#GOVOnl_BtR46aAe>7sJ5(I7 zLItv7=G3x3qB0p4UR!s+>D9<<_g{Wnq^Ud)$!-J@)8ciGdmy#)PF#Qg^|wXVcA0Wx z-jNj}vJS`fbwzbdC8L9%p6<27|*1R6#@N zt72mFsB6<>v^Vg8*W~FPx_zru*cbA`QYM;oSc!)n_wRivvXT7d!$T}}12-@Yj!X{`WNBH# zs)MQzfBDOikw`I5v%;#Sa|{AUoBJR8)5vNotZh!N-NHVJyptk;awUNwLE>Z0MM$G$ zLW@~+>Y{{^TbbH&3B7u?VPYNU%yJWL3KUP{Aw-j%d#x&NuJMiwkY8V1Ye z_pK@Qm!b@5Tf`)xh^;9SqRi_Lu{nSL;h#k+NuM}I_*+<6lYn1g3wmyi7SFm8-Ks^h zqWSh$V)Gpv!C-0bwFmD1?0<`l-_Lz5QqmC{xr6~{PHck~a_HkUln(1RwV>ovFEkZVPqd;iO?Mw-_cDb^><>cw`~Q{U1a zt_4{im1nWVR@D-hgICL(n7>VsAnN{?UwM_h{_ersUX7HeqhkUQ9-L#~_UGE&_8)sS zGQR^6F~q9(bHAy;;Np%{T!QnJm|;nwFqC#*pnZKU8nCdzNVfp+b8=|3sz{|C*BxT?I6yVF9Y6VMWN}?sA<^yC-8P!V z-;4o7C?X)OaqaJTH8L_nfhyU%&1L6Sl)GFXU^A&crx?{`gR(?D-pj;qsUmALX37XvHDv&{quq+h{kI==>exK355msd>Gq`h2??5AOPexC8J{LIfp zIxdq;&%OJ%UyanXM7xG2=|EF7=0kp1B2rimn8;)>AesNxefZT#)iEn0Y7R_fzG5cdVC5x+fS@B;dl{7PDy{mZ2OyKuTGo>2I zDfHyhrq?2I9IlF5A0kV}pMer;cCK!BpZ)?LStWj@S^gYNdX!p6KG2d)iCOvLtC3}- z`57LXnHd_D`>SckwJZTZidQ2GI>}i$1I#K33a{uza(j;wDn2{}6et>3qSACFn*||Nhd`{y%;dH4~R+I@JWkvOu!_HO*$`ZQ50Q<<-a*S@;>LQ=AcZgHfJg z_qttmNi&dIYszO42D{E{Q9GY(&G>i?@lN~A*4DkhN{ zdkmc{JIvER`P!?Iz5c8p8=Aa1Bh|wU1h8+u+W43^r>lyt;e^9r3cHMI#BzDwE%9!4 zF~&1I;;q*fS|c^bcsw(7OSzoGj)-2pB-i|$W@UaUo>fySdm_75MUX_3rYu+(HN}N0 zor6`{-L7x*I$BT#{(lWfPd^>Bd+*L$-wGyFMNn;1ZheAOTr1M#-#{MCrOJ!Q6k3w* zd!;b9ht*p|%@RUmv+1`TM?l42k>aT7)KV?YGJ|#UZD|%}_7|)utZG3Fd^-8#?cSHY zhQco6H=0zIhZv(A`kjR$EJ6MmbAR;S*S!jO%?;4fg7>}dVdRWma;Mq5|BX6nLPak5s;kpq$<>z_N$ zu9Ypod@=KZ*S#ff;#Xex?z^&IecfB_#@W7do_LDMF&L=W!RG6vlBM@=X=vt|JhPo! zTxr*DLKT^1ChTsMJZm`iLf9-K2~*!hs0F0`$H0K3w2v0O^VzI432P@F$L`;M?RBp# zlYi-%$~VO6l-vEm*S+2D{cKy@pR(-$&Lja1;Fip|1=#i}4wKRbwR-PrfoMN6rq((dhqu5-n2Z>EJ0(SDr z9!YP%pf6q;OCav61(X2kq>1y33iB_z&;Bt(c|PMSr7`tQn5rrY5`wi9-W{I6+dyg8 zXF0ViMifz~o|`|#Aa-$-ztGq*qfD@&N`^$oa}Bw(OzEZ@h6Tn?xu;*@;{l*$Z80!> z+(rL8U4@Yw1Hl}r+4oE`RyPpDtWlNRG6iCS13Kec4XG=uiIGPB#*Fbv%r|>zB@0*iiCnZtmHDug6bx9 zBQ%-uTj6rwc-?Ex_=eY)$Y&%%ykMi-xakeAcGir`D%^EqYq4af&IUH^5{QK*K$*6(Yf<-SEQ9PN zem2kP<5Etj(uOu}h>Iy1cpM<4g0%t?1n#ols3$KbM+>N$~h-{cP&2WJS)6##kS#029)8ahu%R@e zdf=g!WUqVF@NKWmeUxo?^IY()y8VQhVJ;uNG=#$5a}CqOl1SOpqNZlxZT^Kleo-{2d*8^t+}-MydtYcw6uS4gJ$}j4mp}Z5_qOQ0yfe4! z!g|&P#!m_|=ZUddfI#OiG=JM8B}f;}v8-4FFk4&s{!2C~e4%ScMB;CmO{#g5@u_9h0G#4Z1|jaimUQ*fRmmS+n!owcD26DWt68zuVgrR;1U=jMT^|L6 zM@HvivpSfw$S|FGe$G->pu=RbE5VyD2s3md9;(m{t`6?}XdktF)}QV3YsVj;Ek)Y2 z%rDM)uZALNt0olnf3N~@hZFob>=%Iaq6+Gr_j2I8g%o;vRLr*BDHhP^>CCY11`(TN zHST7A2Mojg{Y0PNf}`NXi2QSoxdrF@{C3GactsHcOZD&H;mEnBSWKBx(8WR2BE2B8 z&=452^u3D)d=$DxQ+cs;_V)V&ytiXia?e2x1{r(R3DYi{ZLyRKK=Dd5iy0HR$WK1=TMNl^) z3lF0q+)hff+_(n8)?M%2k6)YNp~9Sto9RzVBZq*>M(mGc7l&m?I;FeGmVu8M!)N5` z8J{?+b5@GNq}xlFNML-%GMf8!ZhkpWUnD)|#2mwUAYy-5eR;SrBEe>f+9gD1b}rZM z0-JF2O-Gv1fr#OC20e%|hz~HeO*6%F8JZ?dY6NK(=U%(&D8DaKVDN*lYmsmcg2gc z8UAAIjmIf6n8bxE(cN+`J4LK0Van?XD7||iS>txS_htU9fy`D=IH@7o1(-fHGf4o) zl*@f|)bHH?&_;%-4whNZW<`O}^ha8`XDBjsF?fU`LzFt4%);4%M*<-l^7Eg0*gw3% z@5`!sgjjmW-TBz4Uo{jb=2s%bBN3`Zh3=4xo6@fNxKxq#$;0aihm;*ag2S{JT#ykI zn=2r-lB|0V5A$n@9FQK_LY!xE{`v$*54p0Bk5c{hVH}MG}q+R|45nv_TZ75qNOi*=qKa0)U|z{PC8{p*&b_bmPdVgBtJTIZfAMk+$|LdR3o*>->}ygqiSzPZ!n#WXas6>#bc`VypfmDgS-0lPqvTil4%_02 zhv#UpJ1~J`mB+p>rQu<(d;6b^`qiX3;Z~2t+UfuznAo;Il+h=*+I$g1zJWS7q9M=< z+ofC(59hmgeua6n&m(KiL+L=5*LwLk#>Q^R1@WPAg*w<5R^Nvmx>>WqIqFgc2HBxb zz0OfpWI4QPzU8Qy?{59KQUBLlNd;{0vWNy3&Da(^G)A!7JZXOFJY4l%m)()CkNQ{Q z+&x+*`6|zSk^`%)@E1*fW~00F=k)hdJ>K%yVH&h)@>3Tg@6r^#YUY`vt?X{Arq#l% zMaVqtaR2zms6VnQTJV8~=Sji5|a+1FIEb$T2%a})BC#xk@zM=tH`hRVYeBg}x z*>8>dFS`eSNf%+c7@_Mlj8W>v3gLb<&eObFN*G)o4j$gr3oa+VrF*D5Y?tRLu6|(z zsqW$b9QDgcbUrzv>x}4ItoZ@A@2@yh^QedWt}!K)OqF2V53lJ!UIFjrdcQqN#PT59 z>Zq50aoD}aZbPnc3Ta=!GDE+b)`#8q|9aG~T~1V%GUhTsk2Qrm^Yvm~QL5SCb~?(O z=OEGB)I=MZkpJr=(V|NC{lDR+`Qe+_x!J!R^-J9Yww0J%r(Zu7`RGY^(Twg5sjNM*G%tEiZi)}ja-ya{X*V9pK=D#O zjQEz#lW~6b6@*gfBPp|+V{EQVa0!;{CF_*_e#Kbu*g9}i{@ncP;8fKZ6ELW(nFFpL z-O$fSl0{`wFDotNr=lTblKX?@m1_0ds3 z4izLXHAzz2KX-S0sG?7`a!e4%LdfXP^8?!srq6}3Ru3Y%ac9ek>#0O zX;E=Jdmx9LghP8R*@8QkmQg)2hXR_(aw<{Wwx_6ZdHQ6!ELHoFZ@%G0?nLt%BZr^H zF8_tM!*lyTI!1k-@+U|9t*)WC)60MQAE*Dq`@UD)`>EjJOY`O}ZV4W~FmGP^I0WOJ zPp|!j$L4={PoG}5 z%0d(t=Z;41ST>YJ(IpJjDr2*&tJod7xASAo4XZq_XL;~M(D)9IrSL?$XK>7m^aYP? za6ko@b}bJcn8iGbNzO^SZl( zyQ7hJ)o~1XZiT+me%zA2^>`hJ8NddxbOh zL3@$6D94HbsdAeY~4JumavvduyUfK6rO_FL%+>#O!H3VZ83B z@AY&CPt@*(D8l6vlhAhf5#C6$D!Im%akPuwbx{qJ_BQ)!xt_fd-&?UP+-;8Xs&;U` z^<|Im^=Zs(U`YeEWIT8xuL=sNaabe&g5DdiE3a#5@I?ICr^layL)-@Pt01(JrxHKBG%5ZscdNpVba=S>ahWAm-R zZJqblTTK?5K!sY+8$1@nMmSz}`RwT2JD1rg9n?UkagxTZ)cW$gxEz6IOS^(6?&#gG zdkwREwHC}6Am7>PWjyE@znb5g#?6|>cdte6nBBZQXwtiqJEAAJyD!oixqDT=S9o48 zgQLl|m6TjebP26j_1;h9br9er#8eRExXANXu%yB+WFgGrFrwM}M67t1&%t67rh6cDieE#L&iR>A{RxE>h zTRcPUe=KGsxhRa>Sw_Qq58wOo=gCFJSm=B1?AH~wefH8q#J48RbU{jET0kWvW-e~` z*q+IU49qR|R{LnJvfcVp7N)h=iqxGTUJSq{POpPm26u(sl}7Fwg0LQrcW=qBe!Mk& z3DFT=3al5$n|3l)jowNJ<!(D#<4{0E0Z+X$~zTUaF510eY(%TF$9iX|@ndcg&zu}e7>Ny(v z*14%lX>TbXe&0&SgmnU;r@X37$U^I(g?_ZFX9YKsIMZEjvr}WYSEKlh>X-VO=IZrM z32A)G9WCH~96Tb63zL`GA4a=8jB_eDp)C=ZpWPK}m`VP~ku_bZ z@-#Jr8o|=DBruFq&ze+O@pytA{=>bVKj1Eut0p7iD@QvMxj2Xoe)sWoyp#mQiFlC; zL9&w!N}5U%@%(grb-I|V;&H^NWU@Dl{KO4c6cb~fk99U#p2`uc7oVRaJy#iWQA37I zUWvpS*#K5}QJ`^?)3ZX?O|CHhW%O97Ru!IMGl7AUD_ z@OTGT4BNRa3MPq-Ms;#2AzNeM)pxH(D6)fEU^+l)zNB}HhkYVy1Li&hA7XEFXnlG- z>M}n?I0k-q=Om!pLfM5^3;9xl$I|fw{Ai$z21$koRz~9h6-r$|dE(%SB&RmNU>Yw6 zi?@7ii-#C5B};g0WE-}@o1K8u&~}-KSFl>#GArxfI)wA7g~8n+RvJHPG9BLZaExT& zh{%uE>w?D1*oIEwZxQod|6KyOM+vJl+(HDW4||yPdkH^|$;60DL~D&%t&N{wi$+O@ zOIOOMAJh;rs;?c=52ccXU9xzikrX5WJr?pA1?0Zd{`C7l-|zQCc9EeQ$Njk#i?EwAWX_f-U$cG#2ccKYoM-B5j`g-syPS@NS}IBBdd^!egT}D2c@Q zduN?1bwu~$%d2?I;E67pZ%%{t0DGvXkGFAT&r3YHG-KFNod)!Y1cp)BF+wiQA{_zG z*{Toj|A%a297$eCgzvoHo8SKn0h3hiE6zGS>qV*NoE(3| zzH|QT)`Ou8w8_1~{52W{NoY+xJo65swN4ZkSGmto-?@fb?ZlS5J7IfQ=UVxOgyzg9IA5SlO8xA=9Q$dUPgyZ;k>1>(1p zh4}~m?0i(v3>peW`iUJ4id@*-2^b!A^!~;f9Q6Jg$X{G|NkXm)Nzj^4jK)5L%Di6` z_rX0tU6&lm#>PhTp*T%#?@o?$3PiImLNmW3K*jilnx!9|2R7@;)WqbBrj`v>z>CTF zrw~zh*Qi7zQCe9Hs0rZWer^3T=11ApD529C_2ihehq)1@Vjn;Ue`~~? z8~a{VtYmSuu1Pi~bmZS|lPNL?De;RA)RH#eA(EUGr zbYv>x*J?1&TTNGL}XFJ{OZ6!)h+jBJ=8y$PM;YADAD|sd+u%H3^ick>!LxEib~W zD58WQ8Uk+xIeK2|d1WZ_fPx0XD)xw71dNr@>?>rTWDqY~e3h%-Zj!KC87=kgn!mzD zP4wnzcRV#sLJN;40eGQcR^kp5+QQ9uoL#znrO54NQHdvkNFq2_n09~vTktMjV{y)H z14w5#e2fo0h-H-tJe7uZ#9lfOiiL9J3F_4ojnW3&Q{~C>T)L6;+C(#cvvlh9Gc?9} z{e_A08iU!cidST_-M|NCa#NM*9NJ(-tfIWUIhC!d*_caJ>`1RJCkU7(7FeFk=d(5F ztBr;H;T_d=n=*~rWOb&jI+Lg;1Gkgpk4#;vDwEFVNaIBzO_tSmRG?s{D{@J){IV78 zo!M097jAz&7{pI`(}@G;;0$Qy42dIHrk@^DA-DMC$h zBLJ0W#U$>7?|vh2U}KmnVWgq-!vYz8VtG)sZCZ;ve-%g<2J8;n$J3Lpf>dfImY*cG zcuv10i&Apviu)MHY8&Qjxl#EU9Rc|y5a?UM;)drOP+9bN27kPWNl%anpFt&*Pqd1RZ%EEe)mDJiX%%yh#!{ zomD3-ReRCIDu~Od8S`gc@#dGvb2>+Q_6Dq!chCIP8-cKw^JS5RR!#qix^I5|jX=e= zw=_g6<*gp}_3P(@db+KV2p;2h!oCnWQ+LX z;Zn}?{MA5M?uS|S8EDjGgb>x5cB2CPp) zX8>K(hWi`|&DAG8A-#~WyrdM2lbJE*yG&qrBlHXOEygr`r?7C0HPv}w7b4mV&+$YA zR`^NGi_LD9B<7YnQWFS{ifM{ZuJ==xd4s1%-KO7pBk)lRdM?rlfek8aLKAN5S1DuY zH@(=LDfDCTbD9};iNoubsch`M5Du4(5Z?8Jy!tJBrZS21Gq>E+o+$=1wwy_kzvg1*11Dv^k$n_tYP zvrV|{lj#+iLS<_gCU31e_131AEn5~?wtU&L<=)T2EE?QZclrPOh&ylQsIXwVXsdUN zS1l}Fa$mjJ<9%i>vSFBPB!=LDUg1zg%T3ZhU(+n>^R1D^7g*nD;`WG{9lL{(QE*N* zU9U20>X=^hHb3foHxLX0rALS2C@r9*B8hb6v>iTTjz!Qq#s;@*@O8vuAM3zTV~5n@ z&WM0$U{3Ns)Y{MZisMA{Y<5n#o!5H2vxfxK&1{{2Mc1g&b2rhHVzdt?*QQ-jQ)jjz z(x%8h)O*T9d?q}}nRO!mx|sWo@;?c#e|G!$kL_S4Kl|n%+-P;Tz6^TSyT5#+$NN@r zB^gjAzFKv`ZKiJI?Ap{R5@~vFPPtBed~R$2?2Ea=qPh2S1xe;LU zy=U{d+>~O=RWMt0!Y@l(yv!NoJjrTDhts?FHj2+(F33&-p}uTvMD1&&y*+0pVYix| z0Iy6!?185bUHveKac+j?D2T$sY&Yka&L#f*uq46v3V}%xcIm}3ykA+aGgkY_uf}?{ zy|V;r$PT=NG57vR4~X-<_W*@B6%0?h^Rm-E`!Ru&4% za1irCgXX4~V1Cv->M>7!+}*p6=)Ob(07GW;dXGh^;b%{!RNORedv`&fc{D^R#-jAZ z&9G5b(P|#<*5jhJ0W8WJpY=t@sO-vbJOCww{s~g?hdAp()kS{gOS0!iD&&}0$b9jj z`%hy+I-A#%PW#1qYppcg=WU2L=tzE)7uSM^Or6KKSvxBuek<1{PFHAE>a=<1^lXU` zctIxQqJg)nwP#H@iW%gK3<*v@`(kr2QVCnrx4+by6bT{HQ1-gqFTaG3qsq|F&1-i< zT!(|Xz|+m{@nny80PF#!)nM7h0(nGT2&$N$a6dW)agsqU1>m6Tn(pzo5Kolr!^kzg zN>7vVjpN%)=)AtE$ZoB)`vRE)_@1BV;q@!98o;Z>$r z%i;{D(vqI5tYz)mW1YDJg2vv&)IaUM=d~X1#2i7M2L(S$v^yA@kwa^7orZZ!RPvQ+ zXHJ(b_Bc`*=GL&-N4^QU;_zvEq5~lch8NH3DXF%DpI@=COr=k z6!PU}FdT9B-vCDlkN-wYZp#Wjr6iZd!}>X7WP<k{-1= zP{6Ynli9i?u%x(z&n6R9?a_=cO%+96wijtyy`*}3rg}#+tC;ZM~NJWXg<+rR~Eye%80}LEBvP zL8(3P;uHO_rp-Jx=dfRD1M{LVKqL_d;!pk3`i_-yNJJvEqCqG@*^Qj4TUANStunt{%7Mq{K4{&X27$b`{55-_m~;Z^z-NEb}u$QG&-&d1Yfup zC`9(*Gfert%-v$d^*i38DU{x1Obb?1Qa%M-U08VOMfQiO$04{kWvoKl`B{``~st zr8;uKn?6U#oz)kf{p^o_P?v!#O48is#o$4G&yt`0VEGNZ7q07k;OT3;{7zAB=PNAM ziE^9sEUrX6rTIL!;cHv3$6DouOD;H>8?mrR@!$bL2KvE*J@h%4_`&`_bB3?RC0MYXf?N9Uv8ZN=WeJkM9AziJbN=uOR24#54b+W?7Ws|7!M$bQ|(i_#qsax5>4W&r6b_9_r;b8}U`fra@e# zctrq1^OL2yAxI(#c)6Kw>bpTW8o&*@!ul(*4*of0m-9+f@q&)*F6nzl^5@_F$Gd@6 z;;T%5dEk${eQPApcDk@Q#ztMrMA}`5UF})je-t9St-F7bo6+Wz?)<`4M(- zc&(YvBFU)W)|WJW3E(P~EG?er0~}jhy*&}sqim0fsiv)wNe@l=Wah~|C9UQv02`$3 zF$wN7SKpG3b9^~Pad^G?O!{?0I5s#t*7smeMRfkI6Epw@`xKo+p5ZIOFu8C8ytvr$ zVR7n)%21NfX>j!`hG%`1I`C*S|AxzrKX5F@L8-2nyOw!E_48d5%m7rZTYCO#RAC;{EZTj> zKaJiuns%g@1=UHRllu}2n#gx-j=jD6H-Vv90@;{I}N|$`8rk~no!bz6yeA*d2EJAw49nEr4vxc=c2(h z2$OvbutGK)!FVx%h{apnq4~8$oj!e8O!C%JiB{d#LjloTf`?cfcsu*w12uE{dbjyW zV<>Sn#!vPJSzJ+SJ+lx;Uf}XM7Nu!^muoZ;WgSKnAp=?Z?w~OMl-7p8yxwPWn8gdR zAS&Q$Xe!!FK?Q^U(&OOy!J0tsKNKdjy_D1fM z7hAazk8E|mCE1XQwPlknt(nxmuEcU6=F{R;2Uk^78!^aVkNw4|D4h z@l01&4Gq3BsZ4u(Q*5W;dPyNjBsMkW;6XhfC!-tgOj4Q4ps(ibHdC`A3!ZF|$87d{AaYtXF&CsH4r5uy z>1X30ZEO^ z9F@4Zwp^=QfCKems}@(dveq8&GJQP6A|J?R{|R;+T~QLGef%h8(kNW=VVXd}tBByl zsd~wMs!h<8|HyJp@aaZ(ti8uOJZG-V=l1y9{1~T{tve>-kC);;lF|6AMTQD$TnCDj zXLzm?QP@WOINhCoG1C_#I3o>SaPc9VS8(CdnuiG>Irs>_rRukp8Dny=?mp}+@W`g9 z@KghBW)-7t)dt?u5L0@m`)nO-4R(*t`9bdksA{?e{}vc%JhaiaS)vLmA%Pv`^1 z`f2iyDNcE=pi!YwfKVu?NDiCCLE`CsfM^(7nM2~kG~_*~ZV|9zFm&Aykx7yc+ou}P zRdBli0J~_K+;%bF{b3l%oe(sFX@`jMHTkeusfE%wWhWo4U+MFfm2zp4UFfaC&wVZ; zBMo)RLr%Em8+*JTa9?NHVUD!LPPb(fJq<2~EX=T0_otx)ow7yhudunL%8Q5sUnEo-l`irsa7LM3yvc;X zHGb7hh6UF0gr0yVrTEm%7kNTN_z*S20DycMY+%5PGRbEO@`j%43VX_DpT7>>grJ{EyuLkDDSYELyundebGMCvtWgfJEWJ!L21?XeYRYuQLVT6>@<4^jw?P8Z(vxg)h zbZV)&W3HdA-8mVn&u?+sRLqpYlkN}Mzsc3_710v@!Ll2G7wFNKn@jI#;ea-3jASIS zj++;;tSsyq9ZT0uw`mObYku9-(egrdVFmvdGQL@@sklwkb#te#g}OfefIHc=nI+UU zJ0S_T!HpjP*4%xJWy9QCQd%CEo^ut~=39EV6H+q3$Rf&9`n)fMV*R7QmPtum+V?ON z8W>kZMd#>#V7!1;iQ;blShA?};7GelM(r&$_`oS$_fiP0s1Ga^j-3j)*AJJ^#R+KGNfT%Egaz zu6u#yy6&)#41pn-lQTf7=e`_^5#P`eH=8l%;VBN6lPBn&9>X`bHWULNX$-JT9+KQM zWvm@346+13!*@CxKf`wyc)HbHJx*d8Au2KB22Sd*DHk=Cz9jq4$sqOfj&cPvS$2iv z;|kyye1%fLY#we+N#!gl3=QOd+?`e5RVD&yIv4fUyTh?@x_wh-!p>`@UxmCmdALn| z>FDJdhC=Zv`BYUn2TNJXU^oCz0S%jvBrZ!QrfF0B(fyu^Tx<3DUo>y>2KmS>`TIOA zH|`9;@l2}G5PA?1YBPOTFnAZM!PfWf4+@MG8BHo~mmc(xX3NYP0Y)<$_HkwM@&ARU z@Q?9eufpnOXSTb4xWGKh$eC)ND;%goHn^W5L<4eZCKJzBWirb%^|#OEQx}uD%XE3B z-anIW%{Di^P6RozJejDhsG?{!pGee#OPnk;b?i)LP+AgIU^_Kra)pXyJew^Xtf;GM zKNR0dSDc1iS7i!pL)zrz(lxU?bFVM!Xw23nme=jTWmc7{tN^T_AyGlsyy|2s+UEPi zI+rc$^!{@GKy9_VXmO<)RF+lCVwqPl2P+ECqwoIyAKmmG2b&WcDA^$>Xb#)wQq&%V zg0k;!23pB?b9evOO>eQ?0s)sr=xvt^3;lzUiF+#>}iV3H+my zSJjsyVg|F=DS?-I5h$USsu;>G<=MW9@RAgnmm{*LTCvbZ73(JEpiV}pQe>UXxU=85 z=~ekTjL&6g?zQ^&=RT>)8v8J6vM$7QQlC#duS3xXW-u96Cf6m?x!`tJ^%pn2KLqg- z^0XA6^5qp=c1&EZX@_an>wVwN4!!8AjatI8v8=}P1SK-H;fi$aW$le1ljO*Ik*S#_ z%fqey>ziIjhna}dh^I~Z!!4r5EyOG2hTaPQ1t@n|-&!0rh?680Tye%S7agq3f}9X5elhdP$k1sZVcLvMHm7 zCSaN+&8_)`vKWcG%S0Qmun3@VPOOaJDzQK$(lLm4*U?B2^SLvcK*$;9Ye5EK6<59^ zidm_*4XJl(VJ&F*0UG_xEz&nPkUexF5<=bNQ;=kM$i|X`VPZGiu(48J*DqSPv8DqB1CAfv1D+ zcOyOC4tF35mV3LE=v*c5=q^9kXKM2E*j^>HX9bIkJKaBXW?M|RU|c%fe5}W-ph}q@ z7H0SrYD2X9!0ToDskp#Z)7nKqN0n2E7KEMAQ$`5oQry3jWGQdRL`Fb~BhVX)<#ykd zeL662?(P-x|4m4B+Dh~X+Phc!s`yN;n6W_4M=;<%`_gX*_pT{J)y2PO9wpjS439ui zW4?r$;^CzaPQ$Os4VypxEVt-2KAZUbugBa+e)gw=ad-Q`r?kBBrC{itANfcyn9q%WN=%r@q$HpQpojVrI5$u{OI66N`1Vknc#9HtLURjUx?Gr9I; z?pPYw&D9Ob`rOrId2NRFsKDQrefQ>EHuHsZe;f?`#N_}{j%97$?^1m?$=@)4L#4k# zw-ovCVQV9qx2GElKa}H*li>YRtM%a z`x>_ErkgD;+KLyJlpAvriQxyHT|WL}x0Lf!{hKR-za0bnQj@XYr<7V;Eo8K!Ac+T| zxbJd5XYgsO{_Xq071#8R%4gRl$z8xdBLnX?z;a4ifH#tUGs?kWnTR@mQ|IlLTGHx8 z@6O`TQLgu1wuy2Ax`YmNMSl7HE(?HKcbQ2n?ArA%1C-iw_cws3krx^r1NzE@rzXTf zH8k}Tx!S34_G8aH*TaDC{`V`R!f{SrBfj6N#RXr4%#a`@wb#PHhe(#}8?{HWY^F6! zmi1XiN!G2$zoCE&0h5*wqRx!4vIW_Y&L`ZC-*`XxZ%z;q#nim38-%>aP>{Le3uL5E zVbSYp4~GC0#G@=WwN~%vXOr&$s)TG@(^1Dz-`u_b`hKt;Ll1bhK28#C+z7?*x)IRO zTIPg+W&x4;K@O~zQP(U5t*|Z}CQ%sE(2l+(V|b4k&y#SBOu3OkK^}6*zSzwb;qb)x zphjJLIBPgecg#L`s}-?W_ed-7=o451G!W!}{pY?1h_n?Ng5Ug|_k*9=mZ<=-Gg(L` z>l<^xady6SAbmAYC;0a4z6~V*CDIMCWcGC+s_`PV#HpgKtEnX2@XhR>1mDd5kKh-w ze@aK|(6ZlIcFu+OF9x1R#_sbHYu%5tu{QA5vv0ofse1R1zuX?2a-TS`7-)Ol&x-3;9(s3y&D+s8pZ;m^&8Pp9zyHPG|K{({`1^DIzQNx&`TGn0 z{*u4H;_t8d`y2lLmcPH_@9+8h2mbz%zkdpT;pw-6k>7Y0dD__Mw_7YjJ>0k~oLSuo zsFRzTI`4g%q@zB*9>^|78N>^oXAm>z^*sRV!OjAIM)@9lXkUX;4K&Ucwhl&RIWDBd zVsId`=e~Hxf>}ejulNxbNg$j|HKp^lk<}}ZJ6pR3N zxy-BQy{fAgaP%?Ig>_4#hsfBs_X#^{O*ug}R7jw(N1@jXqT5$}w&Emu$*moFFaZeU zDK>6MAgyx$>Nn1N&9#0LmjW0Rs3|^lR8Z3LzH9l)d2hYD&9W1rGftqnh|wa1 zHml_^9}~#na1Y`^><0#@E)Wr08fkVjzj@v}my_ZDjxp2jf@nSA{)qi64o4{9q4~># zG1ZkA)@Z2=^EFN(3^*<{NV#|SqWfW_0#V%GH{(Nmws@gog`?g%?0)XI&U-i1@UPS# zR_AVY4ZnTft8oWdb_QL{-DhPjVFN%%$K2Q1SVIBKv>-RFO~T%SilJ|0eKoc^S_*?& zhruf84L+iTw==F@YdZ#UV(D8ASrObi=vmA_D6#W*sDiS zQcg1e6ICrBlC=IlisLc4kA2`3#fZ%Hd57|t}9?{z^G z@%vm8Ee!O2sl9-YQ+6bpa~Jks@P?{QNp?eezs+(fFdcZow5vaG0T@dq<@tE^^hok) zQ6ZswIBL)iyu^?OMEj>fS1IR63n(akXsw1?IIec@fs4TaXzxkB@Z;JQ#JljBu&E2| z!~ad=EqDI#1+P3KSE<}_KJw%h_gzOXcrDw*C?I^sV>HCoXt(pwQnDb5kHBf;_kWPLJ83 zTI@bwTyi(5p1OvE#xL78Z}&@>QgZP=&|F*4Se*|0E!t#r6uKX38A1i?aF-!O zBI6cJ?^q3TCWGUK`#9EY`V;$k3#I4NUz@#GjGG##TaLvA&$OPQ)bE0>_Q&jSFf8#oVr)^ zlPbva846R7!+;#%U7H*C%3tDR@l#kgX}FP`RA0m5%ql%=JQVEXt4Wn?r>>CO`y6W* z4QX^8X;K9WYX`^=!KLl`wH?L3T_!lUll-j5b-xF_NGn%ioeSYcsA;asDSMe$0WK3G zJw?}(ktwmA)4D(~ByXp+5giDHanqAa;bT{}Du&{W%hbyH>?IL}xyua9vjw7nIs*0C zH7s(F5W5)#&#zw7<3yNpxd$L98Ry&_4h#Z!Ry^z8{iO@um!r&BzCx>O{n7=mgK5R@ zc!yKE7`hH$&w|r!`f%@<3o<01(-~FDkiiv--XEIw?`39vR&?>$ZT^)D-g4K^vTGH- z8DK+=Si8xL#$i5vm&=-a>qrP7U*7peF4h}$-~X!`GXwt3=<K`6-Dq-MJZSBM<`big~($PX9|sV$&fB1@|1l; zN^f)oKK;=BXqd8%JSD`633jGxDCnq4X3phSq|^D-V5Tyk z+q|(pou~x9lUy1-Q=imOXgc(&>g&9Y85nnR5B# zz*>)|Zf4TyR9AI6QJnz9GYbq$mhPUJEcZwkF0N*ORjw*sgO`sSwgh#^=|WX9UjK!O z4}y^v7kT=J!S-aEMG8Zi`oh9}_u3!ydbc~h4WpE9XL-w%fqZB!qwKq4Giy6M_-65x zOZ>mRUR_P0DBbI>kxI-+_N0dAq&v#t6?2Q4{HHshx{*Rrq9+8^gUTdAJ|uPI5eS2U z+Dp4Mdv8Rdg87lmGqkysp#K)S^$qtN;rMY~`HB`#%$N#G64GhM)6^-N+eI7}oFHSI z2VacrQGgFpUf9TwUIA!Z)=P0M8+SuN0hQ_DZ&M4{H`=cjyoCiRJDw?V3zvYTqLX<< z`J~0T`x+Y!WeeS$(CmeWUH#X4y?S?u<=TYAVDTlMrvAEf>}j9d6?jwHTbBaqJE!!V zn~bdr9O(VaKK9XiDibh1P=ciOjE6L?S9NOC_oew8dz4AQ*zXq;*+vG&(qjVh!7LZg zyb|`T$(dgJSe;mD^TI*aUx~uBfPKU8DcapP!cX5nFMy_h|0liPfcy3TLG${GFb>uS zQ?_4sr=2)GU3dN|;DU2{K*s6gBR-bbeXyh-sgkWY!fj)yBvz2RU~V>2mPth$Dikfb z;kfcNisGp?eh7C#Kbawxj{sT2>R}S>(K$fdiv-@&v3`lxEk;Ay7ii5z+}i)u>m5EJ z9nx^9+BZqxIUiwBMaHy!P0JCKR>F5TrbNm;Ekp1_E$W@gpR~O7x8i{}``z51^?Dzv zvgG8V%)*HSEbhp|Sv>Au`zEh^-LI?EcN-6t&El^aFdM%p?;p($r}Xw~G)}7x;;Ex7 zLNV$T7R7q)^g?)(e1N~sf~dR^bd{lk@YD9Wg}>_cnq?bOfs2#hWQl1!*E0HeMree|RWy;mcMIlJO*9D%CR zu{kt1AhJnkeTV0Qgw>IP&DO(SgvuV##)5@f*7}~cqUPJ7LYGZQ4bd%2I$AivD!Mw~ z)FxybA`4#|ciG7SwL##4i#7yg_dY5toOZAML$7y;*~3rrZskAqdW{EU&n_I|2c393 zxUpv2RSos1z9Mczma{dc6)tMeBa`Uwn&COG-?_X5b2~i4SG7BqNWfs7L z_PE~(-tyL!imlmP?cD+y0j@;&$bW|l<^)Y+3jo=@{<7|XW1j(N*Xm}uj%?<17fhR^ z0HgE<9TptMsYufuDD9KSxMy`43tuf;rrC5v*3@;$vO zc7wkEWCXseFM5}%R8-yK8slb=<=ilC?xM;6s10g`^yQ9SL1T`c+TTxqX3M_c8HF=Pw$Ayd(=xioQO{ zMBM10sZg)4ur4M8xUe-!3p4{6wVPqdKwWYlwgXZ>1z8qsN?tdr>zd-g1GD+aC4nyG ze^m2Y!Pv=L7Yv*Yyccy}uejxX{}sxcvC@oR=>wg>zE`58*m#BIJfb8oSSizX9JI5l zIyF$usN4b~t3`WrB;`y-NmK3zs~8D^8NiW;xYjEru_+pS;6;Wp1;u6cAu&8!s%+a#AMU znMl&oCr_)`#G4Br1i!HG&v@NRnqg~6GpsBuR=aHX9|!9X$2N?hD#@AYV^D6QL`beC zQQ*0Ph;C&Fq!wilV^%DtHFhw44Z08qe*SWx@Z{ZfKho>{K!8Bb5U4Z@N8Obl>-F09 z&{hXiz9dEI`hrRS64yK6(c)^NZwZN(OiDEyCgmuw98UnSh|k&sZwWqHtJn#NEnwMA#`IgM5gFJTI2J^@J z8bz6G#rslnZm*#3-P8_+z8XUwxc`Ns4xd! z4BUd4bE_g#uc5eN$rUw~47RD? zA#(`m(lxNjWb|Sp7#$edxP9~H9fhJ?o*RSSkZvZ$@`1W{3l+qux55k2B9U>BYIaJN zrmca=GwHta)4g8RTx15MN_vPGCmFHWDRN8`yw_NrqIvaUa{#TAh^VCQm(KL2KeEZd ziO-lSc8nHuT<9#j*GcT3kZx+@i)SG`JZ}6+?|TY$9Q8#!&wcr4dcE{fFEUB_6&Vvo z1{Z_jaRB*w4*A@1Y>0L0k*LX)*Vn#kT?E7fScguzpbR%)X@BYSz1WyI1Yp-ibwS#e zPozQ~XIw){*`zL-wczVEFYy3{cBLpUoZ+0k8te&COiL?^2ganQS;Nf516h2e(?Qt1 z$74!_v>@G}Ra-wQHZg!McDL^skD`aYaZ8Lgj-VB#qwWNbm@)4YVntY0g}&_)mGo|W ztjllrXfZ21>4kmnyS~utt;4^YZ>TVxjYV5YphbWH}M{K-u0rE#HUnb}-0b4AC}f!Cf@qd*Z?7h72j zE}lk?^#&PAHZ@P`x#}fj&N0-bq|b#>cJ7i+R#Ol#c%iyAB;9SZyZ%MK(N&&9Dm;QP z5J|AOD(8;fo!&0A?uN@R>euB#9rWUpBU6K=HmGKe45XwZhzH3-GL5wP`QE_mS@-2% z#E9!aH1Gm8YHKfY&Y1|x;L`j;wd8en%_4x*zhD-(t@Nx&L1C#6ungLw$GX zHRz8pj_3O`g#}5EgJK7BL!hO$|dgaE)yel5&hw)|>y(QtMX-ff%+&1<(?uV=c*1j0-gTEi8q+1e6OGC{Ff^mGHBr01K~25}NPBOyO`@YxT>6OSa5&q#+|nA4Xy z8)E_RI?Ib_OR8}2nablx7;qfT0Zoyt4}r7rs;-&PZRmo*ey(j|C(&9)u+WS{SV@#0z9+m0x)nWVN*{2Lbyz5mW^QE+ zq%kS&-xp#|c%cY6rtZ;y?e&`W%IYm1*BG2gYrcf4!VyCIeX`38goZv2bZHJRL7$l-WnNk%G~&2J?#OTTdR-V$JfOK$hz$%6 zlC7|Cjvo$Vbt~dwKfH`(?Y`sx#%Lys@$QiO2CG%B<+po1)b7zC_X*aj=7KXaGx#lj zHMCI)*TShFBa19EeRnI&&lmJ@)>kz&SxtBb>kb)n4zHZ+gMU zTy_iR9YefKn!p@mi}K*6&GC|T z$#`{rDqfAeOrcJulR(*^L#Fb0IWy-9mlOCNxf}_E>Cb<}TkC#5^mp;C5FMT~o_>n8(O48j^?pO= zre_0EG)%-48ZyJKuuk%FN-ig4{;%FaS?UnWQAFOR?`@z<%!oBPOtH;4MDpG>x8ZKD z_daFilYQ=2?(0LST_Cxlz_~+h!L_A;oNdMSDAQtLtH`horw`pV3Pp3JRH|!=uMux3 zIlE-`A1>L-)=;1_Zb8k3?Hqs|l-OvW96SAC3Qc8sEsSb%9sy(k*XrD&_-MCvxh!th zO;?Dd(dKZq;BQ=%hlWgL9OD8%GiTSvC}8jK zzs|x#-L%!u(LEBABc%9>_~W)*n3QI2ZGwFuoZuS`g8+hT;L}Ov>L)czkJh34j~Rlz zKV@!H5@?+AlbW%s&gu?X!Qn4CCoh@Tr#@j-sl^T*Z{o9qywBy#!?6WuhJG0)%XE-v z#Q1#%&eKL4=vgyX<5D!=az(^#nCkUHbLI!1mCk_&f# zPeOn4Hj6U3&Q6J>?^NpC4)jX`C=8E0(27ze&8Dqv(f&1dz2kb4?frt$k&j{>C!O}e zw2!-AnMQR;gcQ9gN&)S0cV>FM>$idte4VpM@P$tHu7EwEZWyaR4pJ)Pl#_Pr&h6!*vWPUz_AL?Z*+BpAp)4yrU;g^lA;T~F%w-Y9w}W6-un zs^LWzyQO0BzS2-bfeV4p9t*tD9Qat9UioLZNL~Wun4wgRYd+B6T zdjeFlj@6V6Gi(99v=WDCyzCU^?CQmHD_L>LY*sah4Yf2ORUal5THhDL0=R*+&RYL zmP$m5+u;Rk3z!;uQ(w^$yI;|z?P{N37LKxKwjixwuTLoAIk{DwvVFsPR`FVKXMKb7 zc&KQM3@vG%&fSJ7B6Xx8>l%+RQBXWYL4DC~cJxsdKQc&(`jW}IXDxeASboOVOia(v zWK3Y2U*TX=cc;Sm*1qGcG|0*UorZls&NQ&w-isy)I^Z60w|61s+^1RA&4rK>ys&vO z1NHncQYAhZ%T}6qS+q$;ELYZS-w=t?9oH((j8UI2dE^$v3k~UX!h-8H#!(k-^yVzldk&LxF0e`tksT>svz@5laHCEhg7tgpg%&q-4?EUYx!*k((a8Jv=1 z7u8Q`(LF3*~lOn5jADpqt%FTRz&Ic7K-r{Hyb|8|_Xk1Z> zn*aK*dEt9FrFlgS;V$vz)wpbjDCa9yxz}HSV`D}rR%uh|%1%yLnb19Jg=Oe}m^N(- z`NJhnnaK@B0By>!i6WMHxa_bz7ELb3r4gRB?$knP^%H6#x)<1e)By0#iL+1pI3Y|Q z#Y}bm762~?CP%2p_I-W0pWsgZV_hTN%y4kc(@vk7>NCCG`nfNf!M6@uQuf13TsAD) zzE;w%WC^`Ugh7BjjPWP0b1Y{e4Qt&~9`*?A;ofAoIg1uW1!E%Sa&QXha-#t)N*X?- zIO@X=Z}MR6P_)l0ENpZ?cn;SacMD}%t_{P@ zi7iR3HLI_)#p>J4>^o~r*>?hv`|SR&%jocTLpXmqTVK2k;TxbmE4&D$mzp`g?MAk4 z%dXyK=&LiCGC?{OUt#yFR3PYOH8j;a@1*}|izz+NCWar2uP6(CI2;{y=dTjaU9KSkjo>f*#k)jAeCMpzsI#CVBCot0R~7c{KcCz_Fx z$NLKxbhDNA?Z`lf^Xe&AMWU46S^p;gWl~Z23~_ZcTTGeVo2f+J6c6j?bcjN`HQjWt z`wutqMU+R93b2n%keiHu-Opdx*8>NqJW>!ft(Da8~OpMcnE>oc=h?G%MLd1oB#c zueY(qu-O*2axS%AcJDn?36t-m( zHHmzAHeW?2`P@oEN|nORst5Lx6qyo@%Vl=Bl&Jl_XN(fRM5av{n}E1UwRJ^T}jKGM_s{7%h{i zs#Azu)%+LbTk8dQ$EO~PqHi>#%UUH~mRY_^ z^5@lB^a1O9wwYZomCVW0tVd`*4}bH&j=pY|qKrvJ>%=*x*+F=k5Syq(^6X?N22^k0 zab-d$$FQVnEXjZFr$6ZNn%(cRd=`wxKD`sW6QCROl}A4PJ-y!V&sh%CZj((#g*Enu zf`dd5p0G-*+4vHBzUlrbz-+~MSds1*VsD_gH7nxcj|108_WickILe+Yd99RJ= zfh{g$V`H4f{aC5i&O*5bx5w-C%H~XBj*3%XH8C3y^I98UI#o`ie!rmI7*eM>L&PhW zqo&C!fzP+IN%^OQ*bu9yNN+Mnj6M7uHAZHwOA9$EAQP!Zg@waxzI;#0SD{kk;h6lDkE-I+}$iUo=^9SS3GlzDT>gCAGv0wQ0P&K)PERoAO3eb@B{6E zXKl8eqx2ocS5WE)@4NQf-PgKc+%d_7RV= zb`WJfIwW^Pah>}{H-xfEMzXI6uQ1QhezMPbt}gSI_VSz4C8x@I*S!fRdrbt71r;tN zpJ*J)JW399w`1+~a8^ciyGQ(T8XkJX;y28)IFrC377tJJ| zxvzX*zgHcGdOj0!IUE5abJ23Re!MN7Zq4vtRSIu)M{_1sk*7XnWl6SA9p&{nQG2uGF|CJ?Z?V1K+dVi;IgjboI*v{*1|Tpbs}F~6>qMI zH<72nuj>=vhNB2R@iLczYuD{*EOG5x;);n4RCSEdn_VMeB6w55)TI;BB+t$IA8(t6 za=ScrWA65^_IRtY51}sk`a442q=JwK+%}-8~I!>d~z(2i_ah z=`Heb6e0?>E0=4Z`{;i)ybDyzHC*UH3HRP?z$1PRp9FF<$A(m8Y$P^g%wvrnd#|VK zR&8ssHkTSVZZyT^Ot{`G&O6uDA? za5?N0k$o*}r!VYqmA?b{M19bknC4oFT%Btbj)JXDtir|V{(>`(xkFz?h@J}uXYe5$ z+-IOw=jMP+WoPRQjWt@gr|5C>2HI=pj_G*rg3oJ7-}tIK(5C?;H`7+>F@S< zpOA)}lJ9B6wf$a?w{}M)*at5>E*>30cFCMQ&N>xBWXdn4>m3Ia1^2Q}dJTQS5`Eo| z|2|z0D(MOhr{d}4kHH2-FfOcfkN!Id!9e&8xsgi#dJpYG z@c`F?ky(|9!pbz(54{lhLnU(A-^iXL(dbCY=VUZ=u#HRX&1s-tM3V;I$JB^@-duEW zvTsJcS4{rg>EVpCy26%l+4#WSQRX?uuSLMGMLZs-U=i@k5}$K1^PtR15SUG|SKz?V z_JVnJ6v-I&4~kB=Cg^Qzoux(8hp+&3Q@8Vvz|6>%Q7^Zs^zPbjU)QD~3WXtPPY0W-+;{LdcmCw1xV(rbDZpJXd!KvOf92@J@Z0IzbjGgrEt(zPHw0{xisVbzGE04umNO;ya#KHc97z2Yla>B0LDx z5#QsH+y3Y90gm5wwciB7%iUwyzoelr&rMr{D%Fwf#K z&b((ZGg7ywQ@#ahyJI%F7lfWrh;6#e;kf74{54%z5@su(+sJQIZje2P+|RP4MMZ!N zw^MHQ-}HF9&f;d8x14@QR>qY=$sd4}m~Go&hLBltr!-Zm9g(tsWfp}SjY za%aD*5ai&(e)qk9C&U~JXYA$Y-X<1%OkmEC*FH>EP2nfM-siVMM})EZ(Gn0#@f$7C{+7Rl~wNhJJsI_D*`mGs&p zXbm!6JkyknS2X0(1gSImdK3phm$Rv4HK2R?ePy<(Ru#;ty83*1J`b{9O|G({A{*aX zQ(jScsUlgPDbIISWNH#J^8mYvH>TpbR(0nq2X8N%rSZxEh164PDs$OvRUV+{@4x-! z6>A$%BGh89N-g%LB`lbB(h!=dLmFik$!^$hAUkw<{=v6G8;D2tINn3y^XUh4bIAa`yVdL9TH%WC?L%oP~fFRU0<@*T$xAM3hSv@bm3X9OzDtLA#dSaL@s1B$>bqYCQ|~9m%1A#R4h;|WLD{0` z7el0wlnO#RIC#{6oT0}T^*~2W6_6>C5iN~lh}lbxv5^uS2|k4P2Hp4%_joU^EH!0Y z80TQ0=^Y}%3zj-3Mw&qAn4ED}{w-q12br^Z^dO=>nZ7AgTS|(NvG_?e!XAP z(w;Z4HeAJ_Sh@S2AMNq3yMJKWawRxQX^y@aa-S)r1Ure3a^-aS)d|@ewztZ(+#%%yUruH6MQwBb3d<3B>nDf_Sh9}^-sc#LE~`b|LECf7phTiEu=8Pt=7k4QNlOA;5i!z2fio+8E|WUsl{WGj-k|kWtf>~ z>J*JS2F4#EIs6ZOfR}O|KLu9X?QiS*W|~+&1P-6|)iXtu*S)b?y0=->sZf%{vjLjP zDWZWksxRLdjSS9U6F&AoLhVw^H#^wmR{k_VmTrz^O`baH(IF)-``%!$te+fPMy%3u zfAmfF$-J17Hdw@2{vXwC<2K967VKbr6|zal0b+3G8mzeeLte$2mj+bA$nq z@^URyhHf=Egi2S^pHBe(si%L9D;?V|!8#~$+$D*2YY&T4GCD@WA&SbdV3YyKwslwY zQ>8+dqb9fJ7=ER|Kv}bN?E{!KmJfbrC0j=vfHp$DLZewJ;ksJcaU`cR?T z>D!0;B1fc1J*3pcg7oiQav%R;#91(T2{XG-7I^T8*$)y`063g1N`cLACvi{YFYc=fi^d(`9AI zz))-uBA}UUjInoE^Yaj(0keon&Nuhj20 zgaa`g<)We$?t2HN9OBF}1^2Lc#CC;N2MWuyPQAQgW%(sa=lrbx>l_dsw4}Ms65!iL zC9+M`*p2g6Aetx;3V7}(Xg}6BIIa$K;?FXbCiwW`0eYI%Xj*e1g@?WVStf;fUD==! zlmC12zCyF69?4DsJV>ZZme;bcAp2|zQW+F=n5+2tuYZ7IGZv z+R5U+ES&}E94In4KTBpm`uya2i!Ccg(uz z(-XF!l=4nTUH@p0xBr@70V%!$H{pJxtUbD|6A#ELI2d8|=v_SkRh(4+6!qQDN5MWA zoPg~e)S0Ppe8!q-;7{ia(Z~gNX$;;0jGS+;Y99&4(2C-Sj0S7sc5{{xllKRls} zZIe;|vT@K|zO(*pQXe)w`7fsawg|=C3WAW`LtHcMKK&B#dTkak z=)Uo*EOHjb4}+GERkX_WOmfAzY8cG>pK|}qj>Cs!av}`R@q=|z)K2jPd?B&qOOk<8 zDT8@7|J$TrSS;o=vYtgFYCM_4u6{m1&vK>!Fvy}d<>HW@d|_JpS!+bohbbV%lqjvu zC8LQ*R>xPC(FSw+0Zl^+#Sxvdo_uQn>Mb{x{0w~G{MeW$FnscgLkP6#urJcAACP+h zP~!U+JdN-^x*eV7?a*wOyLB)3ct@E0%I16Tq5BjKi(2tN@s!8i*;nyQmC9d>FSzez zbBp@}mb;<`cDQiC9e)i9r1ocKsGsJOKKp78l1HOiXR|xYW1yZ&E4topxmu09?V!RA z@0lGR4)c!N22+jhctPAJVi5x9cpoo8Q*=P_O?*Z}>WsEGOq@Cl}a z<%xE2a+%xnoju;w?IssJ^Gm_1pm=fCm+Xrk(3G%bgJYgIAVQKzMSbF_H@K7EEj2U# zub=|ApJn4&^8|=QQ70#t!o34jy=myg=M(1clhnr{fJ?N*tNK0f-r$V?ks~$^@&UKH z1zN?gf<=$q=|h~08)l97cd*u7j^^c+RVBax=rmKTOAH|%E+aEk9s_vhqF%JHIijld zYDT#XKZI)3C3Q!`v3|i)k+|l+7B&goQCd`N29;z~zQ-b;*TXsCdcT*ZYfXMVNOLGM zK?wrosKqv2e}%6kR=Yptq()+P1}o(!gziE+hLR=oUo7>nHw*Myoqh@E6r6~*bBoKg zNsDkra;)ZIyFOy6#ilQHNDq%mt=zeo^j0#oM0V$#Zx>Pt4o0;`m2Z6GH$XX>aR zLH#%XFe8vUu))emq+xcuiZ`MBp=grg+EOwdMb`GAQuupOjRu#1BB+g$&F3flk#H)W zsYj+7Qi;N1W>>``p2$JES0Caw5X*jXTZXNd+&@2sudEV>5DfuuYpv~zr*)MVEVi_~ zq+iOfb-l`!y+v4Ji$9G0#4QoW_DRGEI*l;pI9eW-k{yqdg67lD8tS6m&+*%)X1~B_ zO$d|$pj=9Z7(nnqx$w-*ZvK-<1NX};`;&4aqWC>MC~rpN_xE^<5fMyboBMe-wu5L! zP_1A!!5hF+AcmafzIQ@VxoU(LV&C{cq9WOlYoXTy&?+gq=jKx>d{B6kvS1dc^2#|# zrjI3BlIik9C%w9=Tg!Jew8X2kjk#PR+qsd_ipIFrR;0>FIY=b0o?O|mXVX-bNTz*5E|u*_C(8Mk;@o5o_`O`7`rHI* z4|um!e}Nk+0l;#mylYFcwJ@4YSOP+wI%{sg3)PU@FpQICa-5JJ<|kUQYuU`_D1+ye z(qE?8zKTW7>x;rKF&frLqpOq=pdE&$P&kMO3!~dIP)9?O<;R7UY#L0p7kt9}ld^w? zq_ln}=QQhUfmi7Fg>fi|_(R+sV|O|A6@e?Q)n4=tkO1T~xTjm;{BukS<6nSX<0%tC zEDyzSnUhN>dt5tKl2Pqj?*boTN28zQ_%Cu>{g0N?ao15ai7CId*%69P&paWg5Z|#b zwu%bY!J$bz3=PJ*5!#4~3of}G^SLG*222tMb?Ht!sZQua(8b&@arnlT*oOg#MLo#F zIKQ>EbqO)nm)O@WhgWxlj`}HyN8OKul7BO5koUz+u6H+1--u;0x4EBWqiuaD9xElf zHp)}YE)TLSq4Z6?ofpOn35PMS{Hi_?_G@TXrZViR+y=r3jCaGO# z$-DeNhVZDl3-56#C2PL`dKXN>Vp+k!7ZWbKPbSoPmaRhzI_)^}g~LIjT<`Vk7x|U! zeL)I_T9=V0gik9FY-^8F5Y0!`Zvc={KwIjePC0;_W~g-}7Kx3|z!oeIM#m1i4F{0# z%R}njvv5>5z&{L0+0&7DNY16T8ns%Wt#0Zdj?$x{FyMF!cbMkl9kB?vBsJ(8A5zER zo8hQ>C6W7TcB-xozVH$R{=zEv`9osbXgIzx(f1dy0p|LbXRiiIFk97jpT0+YMKSqR^Fe*CookUKjJGrauf| zo=C}Ga6WL+)PNdy|CsRhzYPW7B;SDh7W-?!GVn3*i_>n~an!?#xFtTmqUXj{Tbk#; zz@f9Q>jV+VxloC$FY@d<%P$&P|84O03lH@=1o&)}&`A#VMA5`gu@`+Bb<;AWQ6c$2 za?g!u=HIT+#m=^}x<_s^lDY>hhvG1MqR^~eED~^EdI5&L(vPTZ4991|6C}tZ_jS=) za%V|9V5-4eBs~Y*Po2b_v<4p&9=t?#ORMhCq1(Q2fIF7$mfpQ^hJ%-GkQ2=QZuh|{ zI>Khjm-Tgc>`rzE-S?iBCQ{tWMq25^G7V+MoC+q$Bm}VS33d`~Bt^<;k4!#93<9T( z?@B%)%B=zxy3}5UPKx^IbUo_cylrE*PuKX3EVV}$ZIpDrjS3qWLC!5jr>E;rvS*X$ z+f9aqG3}KN^Q#e&ivP}|OTIIUlMaXEM$~ODc~ND?3@BQlsWRZ^&i8m1@eR4Ju~OfM zktzQg%!tp50j=kjuH~1A9x^r8TCF+4=?esu z{qi7F@K7eEhR0FxZ3`U}dMI;GuMpA9EVXj={Rd&!a1|FUI=~Q>{r*r46S7A=J;X!g zrKde|ALE?0?mx5Ke5qtjZkFMelX5d8*31Y&z>ir=t4XueTk~lI|D`>1Q5S5JvE5{) z3?neTfa+}C9CFRqd%UkFV(`I8APBT>@LBqgZ#1|K@BTzEMDAc$Q`g*+k?v?%?uP_&?FUO}7?;vF{pC{IoC?`QN34(S!m&=i` zm_3vo$i^!MT2|C>th@^6&W2Prz9N~y(L?a7zCIgIm9K2;tS(P?=TeE4$*a|sHMy!p zT|SvB&sC-}RZaPH1GScllnFPaA_pK`6$y;Me8jg=?~_iYGnF~uLXwASE6Q_q=`=2) zWQz30it{(mleNmY5&pf8ytv z9*t}ufpwVS-soQV(>`x|rqpM*DDH469&p*$e=k@uC+mP%*~AF5-(pF5-xR*h{z=nS zw_1}-GBTjKwbJ(%q-n;f?!7zoaOys+;D!#-8ACoQ9P&Voy@t9f3weP zX;+g!QanOtAPL;EsOLXc(y6o_bm_n7^O`FSi33Fn&>$87bMX8--4AoDV@@i5QMTW9 zDuXMAb5u5h}FMOvT1sMHy|iD`@HIsltvm^j z`INp+6O-{)MOvd!s4sn`IrjBcwubn@u=%EsXhaDcrao!1wasUyF7}Uo^g^I0fV4mK zKDpN#<V6Nb{mT-cAwNxJA^PLGSgy zk(}*?W4gdg(^ z=*B6gsKPq;^yoIOsppP!|~#cQ@+;pz2l zG(9$IDjX({e`>mqWggno;}Qmty_ihGZmU zX|<%Yzje!fu8ap%`geWD3v#3X|8%_vlwIjn=iB$58>();bt~r_RjN|XIpk7TU~CMwa2wk*fEk-$!`O|%Fg(n_7{8fE zuOalj-+!Mg;kVYCT1!Xgo_xNuzn%Ag7osSQit0V%ei$G1F2}4gKrXeXKr0)?d1)s9 z7WbF>L50_4)d7ex7zuRW(KP~om8P6)O(8kqy4M_`^ire619dK8QL8u&@o+RzsU0U6 zF=Wf5AYl{zkRMxpQBc0kQy?SdiV>fU@=(;HWYJ>OGo10uq7Sor%=3+p zu?hFLm7`u)gR;eBbKPWToI)V3AB3_nwh}64}+9gl~jo`QISA(YI zwCR~hZ&*#A+u1zob+;E8yTyV4lJUFy`nWE93zboS=?PccVuV=&7=m9w>%&y;Fy?Ib zJzjCkkC@;#PvRJ4(wO551n=`qG;{gtIpS+r9?XcdBtYBteZkrhwb;OzR&!oxDlelL z5kZh?GskXkQnl^HBFmBJYw5C`g+|sJ^obZo{k(^`!bf4e?6P6rmgU$B#*NzC ze`05SRgprZ`?Qv^sBP9YHoD<1zWLnCV%-%5<4kKrQ8yl;Y$Q1zG;ipT-HYSLhuEfg+uyQW3cIRvl3U(%)P9`ZWO2#-nUXGHTPQ+W%<%P9m zuxEN(I{MRub!(O;(_Ll6esLsLSNBm;pXkoCR+Y7Y!;&fc!aoMQ$Q2(Y@2O2ir`^uf z;0?)Fvgp97R_(c_^A;~UbLGm6U$LVx4tUWkGjt-+h=?u4gtj10xTF)m*MniheCJo| z&wpzIZIWbiavrrobfUJVc-AX)DSGQ(B8H<~qUon_1Wb&P+NcetWUV4sT@^vL=@FA1 zjbO|ud!3qzFsId%aTylz+qC#w;!>P1WiB z0ZLwAg>gV%|BJX~p$V^<{70obxt-w&@2Gn!GU0V4eW-w)B1bYKKghN=Nk)K=ghngP z!4gJ-#VpxH(IUaqnLNkuV;zpfgDz+?&<6_vNy7Mp=!Dlz{*zQlDmvOqCZJ-0%**aS zudyl>8D~JSvh=P+G1K#m>?~uC?QRy!=0~_2*L6a5P<=Bl$ho0$$MMBr*eVXyQ4Dz= z^yLXVvQUkuo?>H+??R4!a}h$~QpuCx!iCdJ10kbym=Tu!#r z|3}_ZowXnP-ioIKf%khKh);NxQe?N3$*{2TalLFL#hBl~r+t+lgSgP~9FO33Xq`a$a4#JDQsCmM5_a$e?|d z1}K4-cRl=Yb^_;^zHXfn#SZtWvI)=a@y^}w@doy41iDSn&Y79Ft4&)v%vvi|R;wE2 z5!aSZJ;_?X?cbzVS=jBKtC{dlms_wO(G=#UuhKwrN1$-Wh3Y1}3u1szyD3(?0s0fE znL5<7M>jDOQ##5eH`FlUeZDprg<@ege6wLrY!Qg0jrl3Jzh%O!t+#aX8tIZ}EhmPn z+(hfS-_ECWpWu+;a`sV{gfk)-$&V4rLh??#x3*4reSR|lyWSYdS$IB05DfUakSlMW zpw~!v!rf-2-TfNNUXpTr-Q7&Q%Y<~U&B)OyBA5ly-&cmE8qLVrRHez-BG1NR$X)Mb zs$eZJBW>JMs9%=Y?EbGVJ|+koipolvI42GJ2teYLar3Nu_(j75W`(T1e$A3~rhW&j zu4>FmaKqx);Klq0xhZx;$qZxmKoSYP=i0=~tmP={L2m)W=;I4n(shOLmCf#FdM9Xm zYDxq-34vo4PfOTG-;2S>tlOo#Rp@b$+mGX^c^}Zi9H{I%E)}Kb7>l++7Dr-of%>5> zAMl}*t>tFkAr)ah;V?ZIl!1ALUpqGf40c^}h99?miEi0H36qH3x|e9-DSL5~aNC1g zUoHw*Y3|1!_pbg4ZyU`E<;Rq3tigo`CcK?lzp6rGf?JrmyVU)+L1?JEXq#Ttg%AVR zsRhbI+j@q(I3K21-_H64ms&pIHN+qaJV~&n=iFH~G}l5pNJQvh7e__N{~%6cfVa=O zqbneu)Z!U-l%pL=`R{b^W@8IJg>&44d%oa#Vafv(sjT3*XAMoHz9eOnFQ)M>PfOL zw1&w&w+K!FN=(RVqAftM3%8<%U;!!*;W5jAR;H}*icEDS0BFr8v$))-GQ%e}(37*q z2hB7jVKk9uy;NEiN9f8cloeQJhYXSEcfAjXhusil()ccIP z_sgSRI`~?h`x+~oyofjJF8|6XJmj^*?rWdGI4hwo0b>>M+!x>Y60wyRULExgH^=>c z9X5>Vm`A%qcs_@nF0rJDZs$HVN{U6%n7iO^{OYJ2QYpODQ(&0PSj2>}7q20CM--OV zz-PQtP$22ZM$p6GOCZr|VnhOaQDQDn`k6e{{BA)BHD{;={_8@PSSPBX>7d1aSe;RL z<(xcSJ#OIBqh6HA{1uftJdhXbqypMZ<29_8!D8}L7X?WxC9)hNR;dX(l~f7el#z9d zc|C#dBe{EkpXV%zqs%t|tz~_l0u8AKE7|*uq)uN^8GnxTm}~ybs29fOh0NtASQ=JR zistuLmuDAJsN{w_{n=4(We4$3h+M3BR2(SoDTP7YjTe+~7oX^Ksoy|Zt`6bapEgWH z%O1H(N;!|eu+9DU=SID)y}scJ|0YAq-o;q-21PrIMOXk)i_E*+U;WmoccLw7VW9nb zdrKgh^^L2Y+5lz{&(-A)e1WHIF^|7=GNSOjl&LNKUTAEF)E}Rd{oHSldVA)gG>2d^ zAJG+h#iu4E{7OQai%H4$wP1r=h3f@=@BnhC>*X&g)?(l?<_p=of^AjfEO5R0Xx^+> zTBq^C4kQ{iKHTRh8`t~DaDWPrkGq!NVRTo&l3@GjZ9POsssBW>^=>wm`o&s8mNPwq zt}Kru!I$0oFEcCRDq3y}ywn_c_d54ow)~#v#!C0`uQ0@97xB@Lx{Cia>iq{Y1ldD6FWBCe`fV!<8qu8a>I3T z{tj4xK#KUPrA>44Vw-W5X3&On*IZ7aVx@Lk_**Y(2af%0WJj@Tat-1%mn8*>2`D>t#6j=nCrW?c`#cW$fBDZYGIGxA+4!Ni@V5reUQ0U0s?tFW1&p%u zPfz7Hpq#L912l7IezJ^Ch-=l3+^@~CJL}yq41cBE&An&L15ke`;#R+R%)3O+SkXqUg=<@4!>cucmuKBi zzi-TIJjIC@ECbn4eD3z?NuE_GzffAP?Xl<7LyD|9bJ$gY>}#{OkHgl9eVkMbh;ku@ zR?6pTNxC&*@BS|hf2GmQy)x!4g;x?P>U1x>f6S}$a9&vvd`0Q2w1Sd-wC~}@pBnQ9 z1Cm6s+q%CM8n(HsKRxE1m@_8}T6<7tO=aNa8zP<3ActMlu^S8Gi08F^?%IgeaR;Zp1PGexnLv+rO*`(e`8p7%(rsWbk}pAj5_( zSr&OJq^X5|&b|0EV@l{N$&XRbV(1&DDgx(*8C+OYK(z~^V&9lisGg*{pbt13iamzl zncz#jTBrBF#-30i%W{KWsL6oS^g%&n#^-Q(91-_wdEn){x=^|xQF9|DZFIkJ&7j#2 z_q4Mn6uM|UvCmEa+!!8ap^81u_75HB94rq;V5wc5#Z*BQ{fwk9Nhs1?^}YajkW~vi zH^{YT!reohFh}ml2YOiEWUMXF1(ZX&`=BUR}^1cs`dAS<$#H~%Yg|M=rzy)mTSL^9l^ojrV zkulFlquk~G`4`5#w~-Bc$>72zTJX@1PYCAn#kLFU0n({iWVt)gMH|~Uw4Z8E68uK=s4UrUTRiDEl z?-J5-Q4u^v;x@ zzU)f_8ks+G0CM(@Qq9ln^)^cfiU??$=C?vo>fU_qXNw+ulO_Hv54p+DFyzguBlF39 zo7mj*Hb*G8pf(An@!FjGqtA|c+m8B>fzuqZ(UPG-Z?=li7Pbr*HGZj?y@vK@#UVLM zGz}ULSj(=df^Kj#Y=Am$^mAk0)->KdO$nR}uhs@$KIESIO@xSM`B}~*q@y!l&^=}q zX<*=?KIQAxZq@Eqs|Kizs>DMa!%&KDNO7m-nx^%%`^hgLxaLAtRit?~l+!Y$BUP43 zwWD*;To2u%l46|9x9hkGp6b5Sr9R*VrsoHE^Em~Par;ey@lar@pNIjj7H+r{ZKo*bekAbKf1V2s z=2xsJEZpPWW`bzMX1|ltfG#N^xIGxcAr0xyFfJ>)@D<#cmO=5JQFg9U-JP9!jaoY? zr*bq^1Oub~A)K-uA8~$6p3^Jrih*te6ai5{-S0Y#YHoH$P^~-oxz;0HdzR@frE>*U zoD(+%p9cSye!906X&x=~ORWND0Q#3NB7I14*kz{m>yoox^bs8KqJ+=YB511pAc0e! zvNNrj@j_$U=6}6+f7!=>u#6(Xr|#eU_z#-z|F4h#pl8rj6APUU zdjS*|389tkEGUF42IZA&P-w+x3ZLn}|KVTyL2o5Wwt%cOTgsLFxF9{{=>4<5{Dazt z@HL;UPqC?6R|5a!hT>P@z-wpjmwe&}KV1R_i&XrZ_b+aHaWS6fW7L0- zYPc043>E`zihnV^!dLG9!_GIF6MQi|;d;#1?%jW8*Bc%8f4J+7+O1aLB;kFVii8`F zKmLwt>N6N|4ZwjcE^B~CJK}irVyx10SO1N72ZEvdU)=ph>vCDvMi|cnDnjIhan^u6 zNjn=-`cP8*vJK3}F&xC8`k%i)xc7~|jHwP{ZJW)F*LDB*_rB3|zj5Ci-OpMYuL$D> zq%HMmH6o=N%f0PoZ5dH?jbo2^d0)8P%)u;}hmfTB!bN3*+`(BPGBmYehdB_RAUKU4 zvH$+*18>wXlf5QZKg7Xzi{qxRago{uU(eJ>?$KjfCFb_~4-dZ4knsT?gEWPoq5=Hu z#QngbH)yyMp)rt!Z8mcf9o7tX%nX7PM7D+7{XicG{33m;VSS%%zzjeqMn$6-Up}eLOLYSvPRt~jWF5D{_2YhY_Bx%yCyYQJ*qAhjN^VTy z+|)QcDC5`z#gUV3P%oo+Lg)dCK$>F1}g5&s=<`+wIww`6*7VdJ0q3 zt0ieiOvH2voZDDW(sBr&AmKYd>ibpo@ebVI|KQCv_uu~D&E@z1_cznD0-Y!@dX6`3mhI1CL(RWz}vInh!mE!4> zFWm-cP_A=KyQLS))flj+ z)Zoyh&Kr>FlGA7F8w^w1!QA&Rl8T0A@Bih;-)u%-W!ujC1Hbg<_I~Udu}7UB;Q%?E z?I|y9VoR?WJzB1?8=`?PMeoo3@|$=sEmcZt-t`d{aBa>pGyG7Ao}f3UWy~lkXK^K6 zYnNrk;%Bs=kyM6znhRqxKh~Ie>KB6=z~Ih;WWoM~E>y9B<*{m%Zt3I;vvOCaeKn;G z$s+gnVxJgGd*%I4fAOnr^X>US1;xd8IQS07QcO$x7ZN6H61AAy0~{_I%vw>sZiHWI z>M>^2zR_@rJTKIC6p8tGNFr9GaR{iwVkWc|X(Tsrc6}kla@?O!#+u?O^PV>`xZ-Sg z+1+7z8%8DP|2_LJ*Q7Tj<_Kl#`iEPrn9K$sr+LLhvzdBj9rwJ zF$Ps1zek=(u~`X$M;S6=^CdJhAX^JUGP2zCVl+XYJ9?Fn_?k*KWGL@RWn*R4o!Lw- zof*Xa6U!A^&k81gX)@WijP!u6SamFwSrzN(u8dV=a&2gA)KkaH&e1n7nP{q~LZ>visEB7X>KeF0Tqa(e#S z1za}ZRf!=;C~eR;tiQ;jrzp6LeYZt@x2Dg`E9dJc1I-r_-A8VF_!E=3pk2h_At3=q4N0-qJ_&6OVbW)FOckyLIMizq5(GH}GVZzG_zArunZ< z1-esIrQtRcGfM7CT+t1|c2uH{LiWa}| z;L!Z4nLrjYesHDk9vGylQ21V-jd3xU;hk#pxrpkcby=>`DU$ZcZs ztkGfyl`Y!7!u-ir7}&Ut$6IP#TWJO}av$7AOCgPv?_|dM9?U4^nMzZZWCSYvvN=WU zR~v~SShzwOdah*tuU`t>*cC~QPh0^^yBs8cPf|;S(PVyy zr8X!&9?4?!{K!uRdgs6MlYzmcaucxHs!{M>9-kk3YoLD&4qF~-m*%ox(Tc*}9`W3! zKB@hdbycz)kEam`yO&UXZb$+~XPdFf<=UL#>}N#={fAjxvBYn2nFa$Xx;OuOZwsu& zFT?{Q@jydn;a6?p(Po5gJo_!rg$`fmX^N6(sJC-e&d|&C&TVU04DMyoH~(*M57f;M zydzNIr%X@HKl_eA)%*wE5$MXP3oY}=7vX0lhHuXwd}pA3{#)-PHi}DszW!Z-Uj!SR zxqoy%`tHCV%$L6>aCCn9JpsyBg4gC>_A{YJ^H;tRs6K0Uow4}jvwBY5eV@sV)#e#(xAWI)kT(>}1vMZJQK~Eg zv-&i?S@P_KCMO-~X~74<(fL@r=l|>v0|)!q2=X6tQtWBBw2H039nM^n6GNPw;LzB$ zJbAJUH|G!iabSefYteSk{F-kD_OyXTFf)n!t5=WEZVosSyrrUA-7M!HpKtkAAm{f9 zv7=T=;VA4d&w@{3>+LO8bMTh1cR^Rz+#W!y0VYOszi0l#-wJfkfBRdo7DF|qTIAXt zde}*6Gof;jQh&`Xy+l76Afi;Sdq&)3U(whVO&n?wyqb01jMI5jgEb;XIExY`XLcli zUTImys~%Dy$(UZ3bmskd9OeS0ip6k*w6e1rxoTu5wvOBpYp{v!Idt=9w&g8A74k@eGvEtO22}0e4Oo zJn@E1c{UF0OA3b#N=CK>;1z^dov0rq$g1AN_e?<9ye50}a8&zWIaS4Rp5P zcTsMIj@%GdhWjHMWR%$hNo{n$`<9mi4RZ!5vT{P~abuR8j0={SZQTz@2p2Z8xfSb* zO+T5qW+Cx?uYh&;=%V8xD+QK_=<`CC0P*xG=Uh}~j%ka9>X^Rc5iAgu`4}@#5^#A` za@p(t>c?JEnrsk5jI6&;|HMmyW2gL_k3K7|H#(a$8}OLWFwE_Msd`P3HA(TE%zHiX zc5bx3#Ec-(_yn4a-$zI`>y~hMYQjDH)|UbY@B?tBDEyLz^EbG^V{=cNDaU@`XPE>* zpLF8WvejgPC|K3!e&ua1LC>aHAOr$E(|Wm$C$&t6LwE0(m8D;aQ1p%(MNOj?-{Z&u zvaRx@-jffj-N+&38Cu%G3+A1V%T6ItX9kXEyay~c2GR1stU5m1SdaS*`}l3uMXX6>a+ z8)!D4Ld?8CV(wPI+zDU2@mOcv>VEqROpjw$By_udrLsHk@H}Sut`#f3ca23viZC|j zog$Oo2`D4p1^R#aFS1QdD;HL#6j#Ib?*;R2;p;D9wUj(^0_t^XB{x0JM>)d!m=c$u z6>GIyMheBm4X$NLc-una4uld%t#gv)Q)kR}>N7Q?0hrFwNgpq($TPjmk9-`H;mFJ= zFt*SXJi$Hthc5-T1|!q%S6FFpwlv+cYJ+rbN*ix2v`HQzv3RvkH~Pmf1>U!*^l|mO zeWu+eHSONfkX&)5C*b3qgrY56DPfFchrD?HeyEs|crpOvo zTO~rGvUv`Nb!gB$(3{cg3B^M@UH9w)0C+x5ofw)k%NtzVcV8k_if<(Fa80Hwcq%a0xIVe3W=SHIrQI4y>9o&G77}$y;J>ml z0KLEqLsG>C>iQ~EnRHd6Vh@<4Ye-wb-b}}Sya$PuN*szWX-TK5lMUdDfux#9me*2N zs^;$T=9WTL22|BVVlb5jYNCSn@`;W_TSX>IZd|&oB%aR1;+b^zr<*_0UjFxP=tIhE zh#^u4s}}Ut0splrkxeAFZ-^O^vSLmCbz{ws`P$*HYgV>=SdDaEDl3 z={7fTlm1BX?&JEO(?|5NcW6efk_=>;pz!MZ*2tcFQ0IQgIW?}Xu`AfpUm|c@|9cye zq;VlCjx9IC6c;)W>fy{S<}BXnzQH-=Cz*y5*jYX`KIcWo0FRgAILwhtsUKBs8Y!uO6l`|v{%aWmihytioYX{tx55FEH z9hzRfUt_JQJ9^{Vo$Hp3q0_FDVG4E<=ZP~O5D!3PNFR0cA9+34%yjzq_FnaL+hdqF z$TqULG`V2D<5gq+d_lVWL6gH~Z}x~jqV3JVq)z3z;$CEQ0G*Rje#*V~7hey~fq|e@ zjS?ktzr4eJ@T0E>FPe9%CxRKt=ypLT(MTaEVO%bgOZhQ!E_AYkl7@QGp1G`tL?9hM z5>OGUry;!|^EE#at3binpwOh3z_hQh-_#X$YVo{mn8mtrz2cz@Y#@0ef0>cl!TKHx z+lb1R_2L3R=f-)pmY+|e!A$aUW(#$rq}{;Fz?1Ldq{^c2T-3Cu=v*|mx7Ho}mDhu- z`XZpkDYem9+zW~@U&hJ#DA#YFKRZliu64i98J$DuB6_~Gv0nRJ6|byKrB}aaBn_t`wwcLwmdA2s zsY3YqnnpNOr9cN2<4nMc(v<7OV@)d60go`2sr%oV1ot*o~pS~XKU&c8QvN>kjh`nKvQKM=; z`ZYm(|4cQ#A#Ubk9CnZU@$bAI?Am7y7>#Cu*h7Uujh1S1Tvn}g20cX79AKVAy}zN< zi(HsR?ULE61L6RKyL+!gJ#&lFVw*`c`4OY8i;{N#{WKoD5*|KA-C(eFGp6hny0ruO zXS8>U>ViDZLtWnZ4EfBKY@;{WUI3bbJ8G7XX|}Gi0FqUm4}>D+R6Xg{ebCsAs?S|) zajU=kda$v~yjy+)!44z;<*sJi_ku0;ayQGKmvDNLgmeUe9DSBs>Ym;Hz2L@(Ao>>u zT>Fmi1qTUwkY+^vV2NAg_XbskKB`SPS&&Ndw3RH{1nn$Z4)SMR7gw#9vE3{y7QhTv zsaCLS_ic(q)O?a%4~$puPsmlag`=LfRxXyb z|CCiD9vfimRo!(54VLv}I&3vQj!DRCu$M>QQZVGfYO(1Sg7O0^FkP^)?-?dbUt`v@zUarp7 zq^O{lu!m+?7b{qcMa}Ph#_Wj^bnd$eu+t~5_ z;8#eNW*B>2zW@8d7i5+HIgK?++%p5;4<2qN(F?kG{ET;^qx*eSR$oeP*gP z>+y(liZ_WqP9ogpg;sLaa=aQ4-&R(~YFUi?H|Dv%m+8 zS#A%7!10yj)j?Sl0xXS3X)Ep%qiemCpW||wORkZ}_mn+P%Dr=JEfAr8G2te*Z}e~7 zq3dAXgLG*bmYZF4Vy(B@Mz_XoX1ymy=>q5|eB41db8f9yGgoZX1;xB#q`W~dG_FTF z4|=RXWO(-uwsl&HwtQ!xWX+N$%GVEkNq)`tDovN$Y0b~LC>#$hJWV3L4One*F&+~a zMdgpnir*jPtYpEUC!e$lwAAgLWbEA(%htJ2O)OsCn2lvqv91g)60k_XsmaylvH;a3 z3U?@ZiN%OiffqwuEhCEsgQGpsl{~O|XIZ?ZJh!JF6DC%dXozEd)MQeXs>n%}R|8|5 zDzA&h)7AA|!0lCT%79pd!tm17Lg-{BlgMG8WUAunDln8QQuXn~bbCEMw-~T{soV#e z|0LK}|MyrW?%0Q9oRpw3bfPgFi4Xc#oO>V7Khkfo6&qkL6hA==uU+MJ3*BPUOT`MY zMg0!qXx<;a{jl*8-xN1QQJbyQv?VRoA3lpem)qE>+*B6|(L@+;i?F?ZZC&8qgKo*x zT5s{Jj|hH3N32+(C5~D-d-O2~vM4XiHuLomD_c3@NXkQR1K)QahjjRD&1Ddh1>|=a zG8iJY`+n}>|Nfuka|VUO(AGCbH|#)t#rCJ|)2(+u{>DM?`&i=3$@=3;*RfC3sSD~c zTV%P(z1?~w^uBAegjysmO;>T%%a3^L<~*vi;C>uZ4FvW$O$5-K7)99#$!ix_Mp4pDW3d>;5#Ktn-1LINpjLdW z^Y-E%IxqL8uNw9>vF+0HEY|p8O|un`k!mw}IX`FNJ`J!WQ@I>yCJv=FAgjJyJ;!rNyoP6|P#Peha4+)|k>1lC<7y`fmwY zS^leNn?X!aATBSySgPVM>5Gt2u&*>B>b5%Z&g&uaWym1CBCtpw)rTb1YkBu&deSUQ zl+29!z=9m^IyWBi`nH-5)>|-(#8YcIAGeR(8D<>4ApHvi`a_bbdCKh5uX*HtyzKsU z(-E(!GN~#6qeu;hp!X!Q-5Z;acv}ufXsv`_V9df|dh!*InoC4PFUIDEfu>i3lG zMSGv6ICZS>Kz3-bv^2=)Qeg7V!!5JNyfZ)&q4+8&Xc|zpJAe0>x3tEKsG%gMSzC{t zC5Lp$EnexA+w|NquQRxC(@n9`q9BPx+fJ8%{+PF=#-qkTXGv6L3KH`xOtx%rUwPq} zw`94sSJJgWwxwwkf=n#C+&)^C{#mBwb?Sf}emu6PJ%YkE7!uG1{`ANDNa zk*O>8IxlL%cSk@9=1m;`B6BgYH1 z5JgwCWOGb;7Z2P=zHy9pQ(tGpPFq_T~64A#ky|8PvCxQSWT6K+&rpAWoCU9z^EF#$8?Tc&D$y8yGMA>-aC+lJv(lTOn{=t-0fG3`7PNfih$r?;oK-;R5J9fnr^|`7z zwWK85(t0+Y?oRC~i&bY|98V|8Q>QpYZ1V>wCWfJTNQh8HVl~fd^)8+KB z%_Uvn=rOOiWeGxT2_81D@IXG98}UI5AxKcZ6|9lhPPvU$d2fHrX# zL1)ulFSsAC!@-94^hx#} z7TeoeFE>|(2r#7ywT&P_fc)2)YcAE8_v*_1ita5zh)vu)8Y~N_}XrIky&3lTQX+46l-Nla@ z$_YZKz8l@Kmb_QJC#ZUrlk6ap0Bc81r}d=C7udwwW6B}-9yvnX~Gxz1Pp!MY{HVBSnqcv(S&ds_ZO zQ|xaLCZPlT;u)ROQ7gq_QB;eHal=3RwpTKqKQFt>FOt)XHv@>1Hwk3V(zsOBVEP=K znN_;8(0(6%o+Y4f;3t#vwMy>Ui}mh6ciyXU7g?^NUTSg{p<+xV>e0gePuRTGZR>$} z=1TD(se!lrFLp#4teYE`#pacJgd@8INr*>5k*{;yp<1od3w{Z8I21#e0Z!ltBJBJO zJrS%scq0TEJrd?=@l&g0<}_zt!Mo#IF?Mj){Z4P*%Vdx`6j>lD{UWRV?rLA&Ygwg{ z*d_*BXfM;!w~^aTfJjs@m6`W4mriTuomcqqn)|CI%=b1wf_9uF8B4~p`sd-ts)Phv zmHXh*yw|@55A-zd9Gv3E*m^P)QOjnexRslMm=4=zG$!paz;nYfsv^E??l%YXUj2|U z9Fg=L&0G4No5scxrQJSvdS%{gUTqU#omlZD+0C2L zB+!N)U2sWAlXO7YYXpr7<|Zfy5zN)Eg5S8aEUV`h_i#*7oP=F+Sq3K|<+H3d*+&rn zI#0`Ev~-`(li9_q@3>f{&jU*r>B!^SsuwPghW+jw4;>aNI{O+MV4UC=ziV3T3yzY56 z*ML?F0i5T}yDp0)wqMsE(18@4A5V$AM;Xga@DU$_Id^nN-rI4yWcCqM1T^>xp2@(} zHWs-hEY5;-Lq569oTlVzeVcx<1EtV(caj?&K0Gy z*=*NV9t#c%(eW1)+IQ3)*q8U-IuUuKRBB=^)ohq7Y+%WZf}ZtpLqWcS;`fq)Cqj|g zSs-VykR|bNkyS;vAtteY0Z59V6U$vG28Ir5+R?&xcjX|WcP?bvP!Eh~ZN6A|eE>5X zdeTrn8GrgfJXxKHt&7EIM-Wd{RyFn|6SYa;ge$=i&QzB*#*!cc=c;hJ;GiLZ9H(6r z?FVAiict~|ObH27xpJa2scf!{kH(dTScRR=v3)T}!m%TPz3s3~hqFV9paQJHhGo=Vy&lqWKc zNiwoXpE^_B5G&Ny#FFGYt5)Bt=|clgl>RP@C!Tni9{F~#EmZoTA#>Sa^4q~T{tpMa zH)p;bjJ}KL!@I%}@0Y_-u*Je?-JMlErgf*&AAlj{h@98Pj-|*Jeb{+%#QUP>e)cOn zy@7}SeQLxj3zn2eGO3nmX~1o~GUB2ZJi&Jk3ckQl1T$yEx3zPncYVGe01nJ8k7`ksQp z2VKDtBj*7Wof1YeoX>|l+2Y>)-VyJE5w+~oPsGM2_5&GS1O03Yy9aE1m!`NwO+7f%4P45c+LAgQfB?@b#xOt zUyHeqccWu}i&%|?WYMA?MipC+7iY5}v>&g>#xpZYB`xD7@fBlLV`^(a04Oc7ZZBp@t z5vsB?KBjk1FVjK&M9!8D5|sY`yz%KG*qwopta25Nowix%-%*N@ULT%Gdh6aD6AN4)(W!qUC{H%7eP zoPlNMiLUa5NGk#|Tiidhr(YWSAx*i#?Pfr2ZPHT&i(x!5a9VdMk|wLE*=FqaURL9L zD2b$^%FwWc)1C^;*qT!6glI+=@;YL8bxDn>|1GHAZDiTyeuCvtJQ76pSUAcVv#$E{ zBi?40XIYu}#4aOj!O%Cks}D!Kb@xB;OK&WFnE&k&?;}C?;@7#*!^D?Hys7}L+}*$N zdzo4Yorm%^>YhvYa?QH{5K7az?B>5Q;_W4f`AFus{vl)Sev0K5_xCJ&bK$WIq~!b0 za+Rc8VnpuhAB}i}Q5p%uxz4$N;@2&p^z?nr;n!lx&35+H>ywpN@F#Bvn7EEI90%|BMHjQ$WnHBey5&Idhj>#f3J*iJ-Lnc{V*G zCH`zdp3z2Kuoxda8HuA9$^AKVO@Zh`?60@!#xwC-kKG12i3$0s7)zp$a{H{%D+nOZ zL=*Og&dhJ%zO5^yk*oF}7(j~+U2>bh4Qr|8h^5`y=V#ynnhhNh9D8|_oBj?TM05Qa z6997DMcnM`@Tc`9BEtvL2Rns%Vrhgc^_H6oB2#Ky6_zGEWNw5`johJv^tr?C{+}~* z-8Wfoc29nH#On!^y48Q7ZQfswcq=zjBxA|w#&jlvA#xCkEdD~MMCPjR?YqInb|W`1 zAr-_ZRC|f38Ta+?jo>GIgJo;5bkeQ-D;QcdK|@oL>)fP%xu0RVty85qm&f70(!MK$ z!Pyml)Z&KX4%b8v6@iyGyPx~7Bi`$Cp`02d9Yvu?ZNt@8hQ3mlEH68nsH`m)8f#`{ z3=N0!_Uv0nQXOSS*TxgwiH7oAGCfyTK^La@vo%YbE2|T=lyg;WT00o8s4cHl$L~y% zloT|Ta`k-5g49--OIH98n<;ywn|$br*p7!Wc;xrJ`_0YqPbS_`TX<08t0y(4o;ax| zx%;VAuhzSx@BdD)(!D$Mkgo1u_tIX%y@f5M50^|tz1Ktk{~AmxT>g%=g$LFCHBbD= zHQje6zZ>j!M}PJ^!Pvu(50?!t_ZR?Au28OqSOMyfVR14LFF189{DkKU4?nDYZa(`lSt?XBHM0~ zRg|4C{@kw)ELg|N^Xt`>PHu>^*^J+ed84UlL736C!Q8*oYT{rXcKbO)q42DVIL+Fb z!Iri1p%=xA3yl(v4L7wq=<5FTn73*U8^z9>jfMtQ&a0G3viXd_Q>X>9>)!}toQ)|9Y|098j)o(c zewO_h=P5~Hp$UK*lakUbFINen@hPE(8ouE^FLL`w{M-3p$;~{GDzG3;%W$9h&M|K* z7=7YOy5%i;HWs0@ib@L3O?gQyAPLfl3WZbdy3cMs?lo*Nsqi?$&m@im+Dhc!HU_r+5N9=$BA~xcW4zi@nG;a&wG+1I?VScRG5MdNx|`$Tt%Z@^L!GIlt**qDdiZr>ipaxP2-8JUEP zf4lC#MM_pX`Ltvx;dS!o9cW$l4g7|!2mFj1bMTVe&QX(jO)AautY&$s`Qe&M1E?yJ zVwdHK>DTRMs107?5Es6?mzCe;!@|;mhx%``)wljxQ`t;?(J}02cdyF zi@eRPU(F};BH3ONFOa;(S~k01h_N6Kdmo&6YOB6N@z69?se)M;-eMyVeBqw7<1y*FZRrB%%sjtuY zEsC1u>qwz;p$=K=ra_RtXXTnJSm(rPYAEP81%)+o;3~1C7b4b>P&e)Mqa!<6T?+e> z68Hjxl?#R3?bjfJGHR}<fXU_Gs7r#lRQw{V@zqhdTW z2)?AAO@2R=gCO83Mr?|-NTHkL-bci`RxM|7SPqV;g?r?|F2qDOJE&)oA6RU#k`EHB z+~EHHcaD2CO^Q6233Qtz1_R^J;{z^b2`Js}6JO>fsOcW1uW-=oCL-B?Vk1fswB-{vKP)0^ng}qVHlW5`2|{htyX2f^Hkve)lckXM)z4oLO|sw6I`s>|s}U!BJ+Jo|_zwF+WJnK{WE-BwclRgavt3%L)q;)umOcsa$x0Rosoi zG55@09{1LTUu_7ye8dg@)p741B7BItLXT_w>*L-h@%1B_w{vvIicnB+qY~%4&1vih ziw?Sbe|H>EMV}yL!O+q|pV#6oM>V(2h1GA9!Ghjgq3^B^9HdAC3*FB%QHZYKyBsOK z0hbK?LB#{iZ;4XCsws?10Uphh!muFPJ3)#*$)*L*z3cCfd$AJ0NEC#Mx_{y40h;by zx@F%+!?QCKSJY+pLY@c~=f4mMmABL8D$zpE^;+up>8;sO2C`ClrkU!A6uKR$L75(+ zxYcwH=*cw2`eN~HS)v;xfWl6oeQAkB&0v}uh*YA^O8@YR^=85Fm!qmOeiD#hJYn<< z$Yv7s1dXQ>*|JlgDbG3fV*{+z z(c=q%$+CFUQ0fD?p!()w=7M@6-3(`n4vtQMw#}Qb=0#(2QZMmE?tO=Ui7v;duY}`VXl<)b`#92uTfQbp~oTQ&)CGJXg$jg?h z=2XmYv#ZYyd3Vh4-6D~1NuOil0@oyCpN#9~2V7IdkXK&^f}19`4{Wwg`rrhr`+v9= z_~@wn1CBTaAkld&J#!jZi`-uEm-WnVHg0Bhldim8sn&&RS=FZ_V3f*Rutl480@={`4Wk!4(t@O_Nu;f@yiHP-NJ}TEq(2jNIWgHQT9ml4njx>VO)(xO?`ujxZC@sn zs#lWWxcm#J&1rDh?WrB|wpYdcBTWz8XBj;@X0Q8?>}>$j#8uS|dA$jA5Aq9#$j@Jo(gWxnTSBQeZKiBNf3I7R-5a;vD7V+M$|z+<9R? z8)(QZ&XPP=I2AFBCrODTr#P~!LDJB$WtaG=ON$Mr6J4+rK?_!UIoAQ!~ z_M?wct%>a3(KO`sBtkQCS1#%XdH3UkLtaY|IJ8f*(kv>e(pcg%WML0Qvo08J8cDDQ z^s}(+&Wy5%ygtg55%REFapSfS)M~E&EKug$hor6vYN&i9uN_87A!R#JO%f#p=I1F% zo&s%u4jG2#Yaka#qq<*x>lHUbG;K2@h5i%Y~d62j} zqP^QfrJ1|foD&!Bj2qYB)4QgXL*A++^$rtx;>r42mF{h9tJ@br>R!Ku7r#y?=S)L+ zf(x2+L_Vz5nhvuUwKuQvFoo(ySaL>WRtQ?~YN69rtse5)2gAzClg>p|o-}+-0R6m$ zMyGIrXkM2+Yu$=z^!59k*4XbSawZfETQX!qOb?kO!o+87W6VoC>w8JglO*5l&aL6o z0U2^@Vq)6te`M?l_v>qiynlANO+(&}{^G-Jw)ZIyM$QlNhfEP;y`f&0wsw>3Mv+2h zGqZe!Xie$fBfd{hPkjfEk|IwEGEK$9rIUX2M^gI$y9eCbEkoW0oT_xyv@6~Vm%6p@ z9rBv0OKx2AbLuP4oGS(F9ipbw}) zcAtIUkT+28+nm)M>|Cw1I^RcO2H6ew-(Mc`me7BG+#P;p$Xo8-&ayTEx$oxioR^%* zyH)S!$%wU&q5%+$l%hwwuQB&2wl8!44@9f?#&$kk@K+IT2-&V8Bfpc>zYP?|zf zMH7`;;clcj12QA>IYV+cHDiy3vrcigTB} z7o$_B3MpHX(d3>Qk5~RI4Pwzg#FIwx|D(%F-7b`g^INx(e)k)TQ1w%x@ZGz{I?X1* zc2`o%!ZsaTVK`EU%|Er;Y%`hXeaN^#_g*YowBkKFu2mxYn4bJ@NFkQpwsnR3uOH-z zi9QgBFpuc7!5~JvWy#*5VXobEP#4%L(Q?fkU6C8wkSb+4Y0_*#N2FW4(71~4$WWPe z-5=q>OR&|I2={{P_=O?wS_Arw0v^(gHsAub!IUOO>d@tJm-`r}tP(rs_3ce}guFX> zq{tnP*+F^~BV^lQ6MPkhcso0`dBJJ-=bT$bf|yMmY3Db@<`y+iGt&L9CV0Y@6UMkJ zwOk5b#^bamYE%#i`chnM#=hjvswQXwj<#)KV@jG+yAK{uWQi0NFj2aL(j;NGa3H^ z-CxxVMVi45_VDd4U`!4xTtD`!L*6@Dl&DS?hk2+56nE=XVkr$ww3Hp@*8DnZO?xCv zXiYSp4+F!l^g!d5RL|G-74avUp*D?;#0Sz77dvtXUawUNu9eN z{lL=X+t5H-8dfA)NaK`z3zT z_iEz0k45f&?>C3MBfy4TmeHKoEuaa=Rd1}Q4sL~Jv6bc2-`a)u@G`;H<|+%?S%mv} z)DP4g#0@oCsQqT!N);$<5gFPDp&=-%&wPPgc~p|8M{^o5!_fHAnOl5svjaC3FzW*+ ziZ?sP`hdu|-Osw0UUEcpz|hk3(m}6Z(^Wt?@hcrIP7!v0{RI@v&evoTJYOoSVP=fQ zesPstrKy_nsLmsM<+>Yw2nkdveFinm9+6#T=j2ma=y31&ZDdm!>8+O_4`nXanAOtk zzRQlWT>5~!(_wGuKVdO!*S;ho~V7idi+a`h)H_2C8)yWG9)cZR$++JBA- zIzryv7u>&ndC1$mEM}RKqTnpTTpFuFXB43m;F@O9s1HXh6UJex$$nS&Rd_Rfm0&U$ zq{q2wfedyArk5l4jm z$J)qq94Q|N1xKOGV>%8IF6BV0O|WW8+ye02@yHxx6b_N?#^`Pl18D3prbUJS^tem{ zebi|$GINJqPd>CsyVPnnmaCu7l1TOx&Exps8QqR{Td9x^nzrR}#9Sv0qF`GQ3RI)mqY0PFD>qzg9tpJQMre5gj znoMh&;9pe8>+Fu#57Z&l&uh1{VJX(fR^*+`YZdf$5S za2Va78UyydiZ>r$%Hj^vnw&bmW3|R1B@!^d_iBYzj052|l8M2uqnvP3(p9zPyZNy` zKwrRsH{Ko5$&~@h;)lFrn&Io*;XfHtqEl#0bI#Y@a%PA>o~wieWrMA1igc|6$1cvOD|(j37$aM?zya_ldz;Ls8D#|igCcH}6-qSu50$6sR) zZeiw^!j@QNxbLZvXNJx38>I~31xzvh04h*Hf~Pg}f@`FmJt-t(-lniP$S*ZMDHxpM z$|8i41n&#deDC{Ea+?q`**2@HF!)oGsl6)hETBw|t zjoV06;tgQ?OiO-PBf+ZgcDJj0oC?*`uPrDoc z!bj}$y+B;>VsVFMDFfnFdh(l|rZB!PTyzf`t=l*rbd!PBqwz-4sVA-mTJWz-DRs4e*x7fNCY#lqN44HeWvQLh(aH4&^{GeRRmo9cOvs%tqqy` z{!}~!;DMzYar72bcw#}_AeVBV^@hEj9{tPR`p~dfAAI1sXISap!l@iRBxY;n2}4C$ zvzM(w8z8MMsnB&cB8QdZR>2nNPHKzW8Xop4p2Y8~UZo~B)>P_P3Ot#O)O2wy=iQN# zahdhgR&pRZ9@K=UldRu-`Edf=n} z%t6(T((VpfhA%F6{Fm}>-czu}-aHplAVn0vE*u{9^L+Kao^_v#4SP!}OYkmgp76BC z*$ivo)o;3{xE^n5V%YmB_f3{(=RB%L{3%VFH_PJIWyV!=7E2ZS$=yq)f8u&2h0}$j z)#(~KK9Iw!K!W{?Q(i_187a3kFa$Fkx%eJP=QdMPD0JL;c)t2%>h`W-A9pwd< zrw7Rf8lR+5NHMiwVWq~iRJ5|NlLoQF-Wr9FkPjw>drSuk>#KTV?}b%HYf?rN;jkYW zTC`8n-O9GJq2PIv9IyD-q=s-$RfC+%xNKlvo;6(G7NsMf2P~bA00-Wk5GR>Y_G5=E_@}#hc<9Q-7|hsB78GA#DTSX7CB)HRsBF=#J*T5lB4!&=>R8>EHf zCK8&tnG}=S%g?){Zp^w593S?o&Pim5QOav@i)x3%1%Goc7rMDo!s9_D94EEEPJqh_?l{r%9ew+yZ~p{ta-=ZA;Ahkqu@9?}~&bSwA5JF*(c`fIE7< zZ9u~s#Er#|1d#v?S8)zcgrn!JIc-rP!W3h~^&L)!OLTI-jGw#04HP(LWbr0HyWQZ^ z8V7s>iaD-u|G>`{4urEFaaYekB&JiVw-$%@6vTXP$xVQ%$EpQV7z@j-D0kmD%X`ns zZDsLkd8X7>KwI)QjqQZ_7RsW39eW4RYHjn6)Dmm-(vo1Oz4SVlZZ#}4MA3Ihb)KfI5 z;Rc%J;w}B!rs-}{bxhyvmTuijS25)eXcijkYG*b~pB64J#icQ?^O`eS?oD&|LVtx6 z+wIl`K{|QbRA|d)+ZJt?OtMKiV7Iavn21COv!B-`r9obC|M@pyBTwpLWp&uwFg;6I zvL}?ocbBhDNQdf`EF^uC>iYa;wa9pkJ$6PjRrT!X_i8N8!BZ03CGJ;$bJ$y%C{}mL zzTD>Keha$d0|pAUe&Di^BMB(bOP+Adg!|;@d7|Tf-0o?1L3h`$7jsFc`Q5FOD>Eec zk+(Rva)SyhslS4dHRn!Ie`V~Ob@D{zyIB}=Km5Y5R}QJ7_L|K?WCN{88PJQ;wN6@0 zL_Uk>{Z<0qbmKJ5P?7|;gfaezB?=wgPf^mH>!XmXFN;=+ZTO<=Fl!wGVqM?^Q8jOZ zFXFzo?S!{+ll7?Itdl$C!`{7It6iF4SU2+3zBZvP@gBCcXgq7pB~mIati=7r&J$ie zsSnc=Op{*MyZeN9h=~I|X~32gDs^rXsulbF=K`+R6lzJHEt*DtZoqP*b?P z%Nhu_QsqYNh34-vUCa7!pL$9jijG*A=!_=AB)=M-)9%4kgf8xhbTOk*b0M5I_i<36 z_P7h}JK?pK#bMUaq(tC78|*Ikcl%Fxbz8%9mK8~ghACO*i`d0aOPJ;ivtkpsS-#dJ zWUKDDI|%nW*PAw4U+3O;@PtF71jIx+$8cR;nVKghn`3}o~ z{peNqH`h*hopYh;O%1Vf<-*X|8h1iE*47~~P%61l4QXUb@z_&M@k%iIl5MF(Du?R< zbn7f>E|sZeJ@lIo251~OfUbtMW_S+3ho z&#`p8th2njcS~%Ts;~@aC+flZ14Dt!@2G37Kfxv9)pa$=rHK}judAsqixWDXla3mN)%WbTJYeh*-8i=jnQKcJ$N@`LpC6JEov(n0L(DM%J7*I2A094TL5 z9!tbxmIab2;SbxPhQ=4*;CwIHQKYtM>OwNzYc{#3Zg8!+V%x)YVRJlMyFuKGe7A#~ zaN4}PRW!z`T55m!JZX;;?w0OVBXVs#E_xo?J^Ur*Oh8qYpqG$fphpme_Jh{|Ql@SRCLA zfJ#y!rSoOj&){z52^2cH1#4COiLHlK)Nfy`Ksr0(a%TDtQ`aOMZhM86HgOn13W0cv z!Hz|7;pb6&<=Cbsgf+7rHqkoc%7qxSdy&M^K;bF(zUNPPA4{RWAaWRdjZ~MreD8!; zJFUR}gMr{h> zkqtUr_w?h|80o>zl6O9lw9jo z=c}qyT~%GVs&lJzZb>b5t6Mp>S~*KsQmd8KN#Ux4q*lI?+UMFl#@Jlj1RERQ`dS*o z5QjKxy#cPUJ}1pV;kP@zfbAnwPsjPS3399iQoCc&ilVL z(mj+rVBzjyw~4BMRgg1c7e=H7N=kYV(aWdxo)w-)B8zWzUE7ay;I%NJB{u+D z;5k>ea{vXBv1!usZK)HG4XD(zqp2-$Rturk3rEW^g$FTI=<~c(%ljmRK~6AYdZ6+ySFO-TP+H#5(DkuH z?wema?LFuMgPvcc^_%`C-bbl(1}&@Sm0W&Hqi*=GPJ30`UllGl4V@Ia8&|KstG-+o zq7D;Q>-lx{r14lliIf!qK_jF5Lto}0*th8AbL!=6&VU!J1uNaozdr4C@3$3avedR! zJgMIDpR5|mX|19bjb{Vhj)C98oP$s~Ijgh+^{H3Yg0TCIzdh}(tqXuD*GYLZb#XEs z(Ch8)vww$7vS>rTiyKZTrtC#6drb_rblFSnuMUhr#`M=k;-ChO2i{dv?rbX`B& zjzz-Pf`vP;W?_%JBjU_B(T^rT*pTj(0Op6H1U=$UXNdM3*$|;$o{w|klTyDJ{RJgO zuA!s4eh4G?&GARFrpqv^`VI4FSr@gxnUF7hXL(a(DlyN{XvsO(T+{M~iwJh1mt%}U4cFfGh~`a~ zKBQlQTB}BHvcTqUBszWVjzUk(M?ca|5b`*XTBgA)_@`}TURMn`0RiY)RF&bCzWKwp zsS*1F<%ekz>Mzx-)ym#sR61qiz-}cB8M33mu=l?Gp;50^V)qk?E_qSQQyS{k7K^4? zywcYr$PZM*#P4rgV3^r&_|5M^@ehBZ=+Z>hlhBEB!(ks6424=C0UBuiixnN|ARq^{Ks4`tAOq5f@&geC$r z87R=?um;mbisx$vQFv8K-jy#PVIw;u&Zknfxy+$dI^CSe7HSiPTtQ+!XDBL%si6l{XfoTCY)I!53F;T5a&^^}iEIE8(c@yr&ta~0XO`p$&6!fLEL#`t$J-f5 z4MDtsCn@rkAz{>P2q`ehG@8hHTF~pfvWItxkoBJ%xCvod#236k*$o|xv1wH}Opw4} z^vkH`VmNkl8cl6coC2*M0|e1uU}G5-S}tAVxe>#y3JNm5@)SdasxC3iVpA0YPGExF zg3OYFMrs7-%=RDy$`h{GYqB2p(O@CkYcQO0nWO_v);-=?jeHihQsH4GLj6DhP|_Ln zn%g?}&{)qMT`N1b+N^UVyCFB>XQu$5zF|Pu9!ZEb_cgfxYxShJe0wyGZB&GSW>0f^ z6TpxEtTn%3DFz~ldwD4u7Z2twU8kaYNUGAkvv$&JAQs@>lngM^RgU+fyq_=7jVCS1^w+I(N?Z{B#o2N(&F&mF)Ykr%@eePXky>AH4Hi(^owQ|~pxb4K6VMZz*v>oU8AaKbHao`eL7N2y01>Vcc$ z)F(pjtujI<@N$!AIaXd}&WyS>VSeoJsTaX8U6qd@0FufOcEYi{A6@eB`$G$^?2k#&Z?^nt#-OT^IMD<*JHgw#JEbL0&jb$>fTlPU?K!Zc~$ zkDKE|AL#O5w7={-bl4H{kRY(zRf?F z(HHa!NBj8`_varU_gb0=j?y6O1dM|d_xL`L9Vj`EmB;_s`?s9LBdz&u=9Q>-@7uIMpZ33bb zRpaW$)#=F;n-SBV+5$Eo$kuzy$+Cb)Se_odhIy}fxC)6=(OZ{Y=^K>JS`!qLg+wyh}M9L!uxb#Bq zEV@mP<&p!tB~OjCX|7#}lwT!2glCAUEz<+?nww+*Xz8gHmvptL(;X1M0)lrbhNX=U z+4$4rSXGoBJ)z-Ab78&eAHLgLDPb18NOHV85k{;HI;gu8upnQ-(fU*YavaY^^VQ|n zm!6hgq@u#wYy59Vm)f;2inDBiDQu*DG7@`Tg5KOUH}Ui1unRmYyylACCHk;$xo$!v zAOM>t=tns*b2QTy$U!_DLGcb-nrrcFjb95Sfk5$~KA>#c} zXw?#i5jxw}8e5L~OxvD6;?*kK_rat7i_T!}JpJ~y^U1-N_@R{PpL}^>=#2NX|N9kG zSN@{I?*5+nZ@>GSKkre!>-gO-05$M~pdzjO-``#7{&5Fn@MYvZaW4!`z=wg7-l%)pDGNzJP+_)P-rjn?;+%|NR%k8gvAnA8)9Ez+sR93RG#xny$Tf90Jb{F7>vde3-|5>WB|r0 zL2WH{pvQ6LESX%IKgOX=i&2tz#5D}@!>}hPsf;d^QZ?(AY%&50}MJ)P&Y87Ii5`S-$#qKGn8RLWb4E;VUvOr+- zr(btJk{k7Q4kb~x5s#%J56LE@Nu?E;wU%jbqb6`$ow)2ZpaYq-&M%CTNKv8%Qr*rU zPJ5ak}Jgn^?j@cX^kB1HMXM7c}_cs{5eJ;Udt~?$UeUTAoEB8&2douUR zA!L#iWnXo2i~GB(QEybYmG7O8Ne58rapC7IgJ2kBa$ydKopNB{z+8WZGB+ z5u!oV+aibd#T3hZ%3Z2OS8;#BcEBC0V?X?Sz&&NB(ZJy}XscaM{U~w$LJ{QKOh2kJ z1$L*27ORHzx_Zd64ImFcWk|N=v_CoS*u2tUq3A;@TjU`U9)6O9tTp?PG|<04B(@@^$< z>t&j1vIooEKg87!Gq3oaAJoZch=y<7m2qBD)6JwC?i%%mDuXp+!6xvUAfDEp?jH5p z8{?h|#GA5B=COh=QP}l|T)Q)FL(ix;nK8a^DXCuQGYJ>!9R-hw2neikOrR09 zYX!f=7`1qwPa6Ckyz7A>Z9a(aE|gkglP*z4@*H*$=>w*(j1$wvs*#mQ2J{`qfiyIy z(B=dE)xNz3LBMTYi8Y~t7;ZXF(}IjP?lVr-W`4VQcW%|F*GoKug;7dY7!Tq*t#t1Z z_q%;eIIXACqBVa0)n{5pSRaxST-f9cBDf?c?Bdd$rq?DVp;~3jb3%v>F!|f`kSdY~ zL81$ItOZ{kb6@Vqkg#a}HSnZ})ZkhAzMT>oZlDlQe3~J6%CCd8L6cLodzz(#1-JAl zo7?L#g=^7T6xYf~3?v((#kkkHr9vusM_F9yg&L|?y$ zB*0gwf2qPVSISq_GeBpald;E;Le88I#6%OuLuR4fDq-oNW>~HDng870zr9D#&&nLo zZBQ`*%j@^0wKn@rF;29Zd%^^j73CHHY0}clm>XX=>a7hY7Tg!u=|R%z;_?Gnon9yM zPRsW)#NJ{W_VVLIGzwIkyxY&^qwrgzu{-xmT_qkgi)0mQ-KukAQSp<7q_DTF-*+WV zS&`>;$i8h!rfS>_SlpOGo&2~A9(KU>H}H#OV8%p&qJAio2wVsOS*o%1Cv(^~vtvtZ zIj{C0YN=INi$nfu6ZNai2vXC?wKaj$a|OG%taE%z?C`yaCRe#c+7d-JF_VoCu%_Q@@y-U^~B=a~{WxVR&RRu}Y&)uCR8C*6vH zo#Z6GGS=y4$6;%Q915u4AAdX(qOCVwd}_JZhcyqa)x%EsHgtz0B$O zEX-7y#H!kSL;het&T0xr7jmGe7TV?OuB^<~6cLeom&?|q=*OgApFl8%!f0rfBsk~B zb|D$8DuGmA#{0KTL#oO8q>h$4iDo^tftP}XXOe&c9$q;vd&l)?f=hNvgWRj(Z?OkT$(%GZ%SpJ(9PFng z1J%c<8>u7@OS^b2Rzo5ft8p#YA1#q($qeV*9~>CBBrsJbfOCh$~OJUpRyax6z1-;WN%3=IkcXglAOh zQ8fx`m+Bc+wvMp9=*M8x*8Xu9KRW7NOvlanZhZehh1+m^ltNSq2G>fqv_XJbt?xo$ zH|`UGTh`dA2U&s75$mu6`aK{TIvNWQt>HKp?Xg$Zi@<5pBii3Rpe3>`8cBeLH@yJH zj_C7#?p!E~mK+xD-<}xtqLg@(i67}2vv#x$=dlDElL}grrdJ*3u1+)&q7oa_t^(!V z@LObcq}2+mJlDKwM`ls|sen>V_bc_G~jD=97T?qD+2s_RFwu7 z*n1r0v2NpAu2uGvPD&r1;rKR!IZ6`DKG!@t>a`{n5@jCl?~Ay1IMRMo>~9k;T@0C~ zRf$YpN=h>k^=%PZBR+(W?O~7HUG7H#!vXPJtm%3wy44J*)!^b2FTpGKsj2uxABkj} zS>ptLdH2OJ*zb`DtPs^3!Zl5lijX8m679zh8Ux=9PLyH6!XIqCE5x{GU_LV|# zS$gV4S9WgH+th7djRPEbW`Y9gdJ5byJLj;j8?{xr!WFr?W|7rM_zNnf1eCKDyq2T$ z&P5`M&wV9f=_Me6$k$@L#Z%2#)|w6BhG2Zm3Dd4ox)hHvkaPlO7*pf;o)=vpL=sbh zxzR~J)~>k7ctpJKNWc??IS^nW_=Y;=Cr$lTM|M_A89-E{v5jgVcwS7qoC{q-_^yQ#!)F=;dX^z_$EQlv4rCFmnvrkKg%m8!5n(62$q8^xSz5(Qo zYH)(mX&&hR1e7r|jC#zddp3$O`(b5ZEs0iaH~_hk#AHNxQ#_&)FI!65@&*wMtk<-2 zg>EB+H%L&Hwz!v67-~GQY}Fg>C3kMYeRFaYBbS91*q}vxQGPOY`Se!ycGwI#7zN}` zzWVzd0ws@3NM^pZEeKBD$#HT8nVl=yn{5^SXo>jZ+&-0a3^Y*WbXr>GP4nAXisOWR z$YMbhYp2eEISAt^1sAAuZp*@OBB2M-pG-Ql@svY%X^ACPAL3k?>_Wa=+pxjIB9~T2?|?cCWYJN-UQpCtpi+GRmo~ z)g#u^ZwSzU^=u{!@Ni2A7iJo%)RbdW?-`6n$0w($Ue8Bx z@UF`}81)`3Mu#erBlUIF8!ERcXfw4+)vVHmjaAw7)T(4_E>}}QZDz2;GXUTc^r@l& zb99u>!lS2j~aspoVOe{D?-A*0lu&k#2X=t;H)F@Jfo10dbn`V>_hGwC+s zOVi2Pd`nG!e=>oG7ca4#$caL#VQ0Fwx;@4768Y*>E?-R@1C#_1T+-cS?$+nh*sLo3 z`q~_nn} zV&>ko`}7Zy((b;&c4ba{!I>YmN+j!u``{0Q{^Nd@?O>bWKYXYDTxmpW-#T?@y9nHj zqRfih+?T)w*^KXUTEyOI(9;{eGMtk1x9iV^A!qRm*UzUwD}3vs{9 z_5&a}VlnrfL1PyzsIFZ6?(GHl89+W(Bhbsfq1JZjYgiD383EjSiU*BD0I&N+lWo8$ zz2!UOK0A1wvC<~cPe7A!AJpg!IzvnxxqfC<)qu)6| zRM4F7j6&T-=tylvkM^oF$3$Mq)}_wULuEK$WV{Q$YT5VnH{_J-z`s6J?}wD!s37 zI;1h4Ea-9Vbqqn}xR|=J&UJ&x zvCe&*?KbzvY+DC$ffa|j6ef4xTWk3ar z;f6R(UZ;Hg?k@Xj8}hm;*Y_#DVLem!s$Y~mcF08N?G}SqJgOFK0wDp+i{f_asnNaL z#c)oJu<_j9PlNu@Q)=@mU3}12vM-3B5*?h$)~08zV+Oll#Hb9(Vr_ z+nUpn@J&9^Mgt2YqmWm#0GgXuH(b__o*mj!D$S_66N%p`DK7Y2#6<(82qt#h6V5if z&fhrcb&@6tc`u&S-K0POcrC5xDAFi0zMEygL5rSpY($hf(rj3{7*eny?W2OS10yU14uwV8Aav;>5wtDzzw)!7b|CDzT4t zi3@Ize$&O6x|qNcMs`xg=B6@DoaEsZ?gQXpkQ5rR$`ekct<&`aVKLBwxaB0audbWd zQvh}_x})JKXFd@kUwqAdflKQaO%%2jN`WAwHS6Lco@=?bL-TZ#j8X15dnZhE6xXei zXj>HBodC%Gtx{Xu+VIM%+b#Yo#MXmZ-Al^g>hvWE{{cR=C zieMBH?t4E6574+Cyg#kX0I>onD1-?QPB0yI+M4c@1Ti0E_YAx5_|J5s=NBv7SJ?Yna|v#t zXtFQx?LwS#5?3n(wlMErex9YA1=mYDjYEScgm%c){1<3Z<0B}n-y5n5xd{ra5t$`uNko2fSoZOJ_~)B~a{ zQ77?X1f>DZk*dTRm#JH!qL}$qYf?f5at3H@)Dp@7$dPHww1TRU@SkMTRf%j>;-kZ% zjtb-Qg2Cut7R{danavkomVe=-_ad?uFpNi*isx3*qaX?18prv|Xcw>YyUJ7Ud~rQJ zbRc&D+OIzTi@!SQU8)I($0z)vP1ybjX_LY38uzb3foQ!R^$@0fXEW`f_{(aqYzk)- z;~+aiFW!Qg>ku8Y(XaJDTNPH8)08KL_6E}sr>Y;TM-YXAynUDaFWN9ze%%vsG0vU@ zJ#5@9eg(2{qFk8mGVd@;uJDWt5t$a?g*P>=$bJn_8XT%(=y5_@zdZ)Lfs|=GsBG-3 zCDsUX^9}bk;2nnD@vp*xb26TM%VSEsHynEVaj4aOj>F&4M4p}*50K2AiIDwR7Fi}H zCXKiqUuP=g!$Bp&avt)RyLUL!wUr2aCf#XTc_I>i44D$Szjj{B3 zo@O|F@Y`?=+L0!C)UjF>Rx27i+^n20;>sika%yABeG+JbI`=8IJ=cN=^d%9%(@OIV zSWc@5@59w}T^kuEk@5SYbyA|o#cSLUC;SY=YC=>%Hm){PZ_q}V^HTfQ$^%!_P#qlA z#^p2QO}cGtYpc~0MTt3n37S__^qKoCC)=h`>=s}XMYRCq8|4n2EfrEEgxcoJvImeY z{`eBp>yMPpO~V`DO?u`5c_uQ5g9tV@1q!0~;~Gk{XHwwdmirvZ_>D~weeeXA5As$s zJ4j6EG>Zevwd2Go)I>2$V_FRnIQ}(*u#y;YfyTic_OXkahtMp6<_1(!OZAajQW3@9 zis{Q_lZ#lB-ktQ42CvCF>y{Y+PAnOspbiHgp=tA7dgz2-#zS)Mb<*bBYsg=n9Jh$+ z;%z+}iIz^<>yDE}zcMQMyLi=&kSyN?qa=@jo?630uDkb;4}bkgSy)G2*PUAfR_p$B4Ud;%po4{|K#J)n~GcN@IiZ-4)W;zqQ(wiI`iYP=2&e3 zIVg10r&oj_)i4KuCO$x9U~a*cpF zec~2{T;1vaF744BHTIH*y|m!)Y4;_L4Xb2)|_yf&+~`@!C;DroC;&na({a1l((kWi%w5ZXqcB|>Bt|{ z)?cQW2zQ6>UvWJ>!2g;Ob?z8>{M})1(!Iq_%f>L1&!sqbn9C#M@_CyKIVDy&jrc|o z2g5?ML;JlzyOcn3&UKTf-`O2x?H8Z%x}9sosW4(#&7&UcF9=UDw9M_KC12IbcKY!;UI0kD6@{=4xJ7)h}<6%RXbk8W`{P9+$yr) zTWjCVi4O!?hDpjBE426DYngb+Tt!)ub_XvsljKz|LK-|R77e13!<}hz!njGzJOvaR zR8dU4Xr`SV!1uF=mn84{+vFA%H#AF6O4b~|*X+N6AA5kDf*=*%cNaLh=r1#4dvO;J zZ4QU8GCHPI#w_9888O%#Cc)H&8P`gY7XmtDRA<~ z@4QaByq%#8aw!wu_3)CFW(HgSs*?5_8_fS8Vo^d<(oc5Z-Z{Kwb?EJeb zV^i&%*;UJC>p`{Gb4~kBd%aog>mo;@dF%1ExbNpEUY%FT>cu_o_c^jZLXP@lcbVMs z?^+$S#1yb0TO^oTX^jM9e=}XZphQnZJfodu?sFuN*CNy0V3imPTHC8D)8Y^(jEwe` z^2d#-E|`|F*}ZXuoF(^bY}d&Q$j#Dr50@6a+B<7ToM*Mn_F8OUsixe@S}#65dGi+K z0TCm%*;+cA#rF$~yW_&qBrR zyl7Qj7u!?fQ^|m+0MVtN_5X<6ixE$n35ND;d)XMCMmLw;Ar8rwSJgpTrATHGQPSu z(D=7-^sX7UNi@Qg>$GT}M!cJk(4elcKWhG!;107qxPX0H4Uw_51DrUw^agiih!!=KQlsX# zyHQez*R-Mf&(bf5l_64>DWR+I`J%j(dm5^#=X7JzeS@^(I(P6Hd3cCZQr9w6As;kl6_#z*)1{xF;aWc*JNHkW;yA3Rl zKB6Af$~1UDmBHCK^xsc=Eta=Zl&*5g@3z)sOjbL0xleGuA){a)6uO1AC z6otGB9D86Ja6QEVG|+m_g%LI@CAGa4i_m?N#Z9RL98-!NkdYZDV>U*GVanN71_eRbUIs2xJ;_=&6OPk*<1o#g+d)lGXP!~)l>PV4$vyAQdweF^2v^TN2Wd5 zTu}i6dOBHy<-NL)OjlC!_nqTuuf4z1q?)xzHNqla5%1TmRqd3(7Q00vCCuR0cTaj9 zlFeuNPOb1OW`N1Mt$QZD6@)@PxIPX^lP(nps8(QUkaZj<(5-RoS4TK;(PR~gNo|rm zMqVD>H|Z5Z?%MuIuTxQBHv6%1&AWFv)Z>x|CMg>sn~ol}+x-B)2gAjE?sM#P*9DTl zk;=SA0A=1T9CAN&a1xl~;wJYe?5u(rF}F^-^@sI1*|bf)aG@iUURQlIGA%6Iz_i^Y z`E5KVC?+iAf58RK)yQc#gxe}N8|TPJ?ZtjTWl3#tR850&-qo2?88(RJG)X|&z(7JMGAp0X53dfe>Tg);;YT# z!0Aiw??xxR+MaU5YcU@OCJUaRMK~wN=IkncNiBU&UmkP+bcV|hL_OAx9wKHt-KbG5 zNGzNX52?E%L4Omme@eSGMzxV38RFoK_Mb8lC*Zhs?&kSPPiO^@X05+-u^7`3T1^w8 z@fc($PQf}AuPRAGyJEt+bmGz5+Ff znFJ%1em1J^Cjh>{?1!3;V~Of=oqfZBWP4wIxso!#izLYk3=A4dfb>mZ$B=X=1k`33q z2&c_vV(cbIMs%S6nzsO-l|I0PxVp`{e+~TrRk*=>D@{6-yfht)JP`be8Byn{GcbRT zWhW-nXT|r56(Fo&+|@LzGH1=Ah{-^>?DoBJhR*5iv}C;{4N?rP0lPOtX5G<_b!_^v zMi9*x4@L6EwQDoe_iqHrCbbCAW!;HvID7{=$ONXAu!f;bP?%?1R3#VV!XiRRUh~8Df4Va05WhgSlvD-G12W=8r+gA88Cy;H( zrSt4PYgH$0Y+|=L3i_Ssv3rAKPdlJZTqHA1y{7G9JmM{(eY@CQt0BE@WLd4n4Z!Po zedxR^o1OGFOBY8ZpJjiD%H6Vd@jD}ZuD9<-S>&oFpc&}>J?zN(vWQ~a%a-(B{ddcOQ5#=}lKhqr$NoXO5dSkHO**JKTpJPI^`2 zCf7&_?zAW}x02nf@~IKHATb8d&a?>GF4}W6i3>#OpGK`3%=)Q0wq$XB&_Yn}`{@bLai%V>`+)p#N=(9J&o@zQ${Y0Z? z{dw9g>+q0ZUPYMR8_MifjlKj^0{QL zCXqpED4fltI{}#Hftl)DMXo?ulnM+cWPulWDwdK=BAclZ+EZdhBS4^4+2#a~&89YU zs3!j~y`u8y#@tY2+TYwfom);-GvWjiiQ#nqoe!tINDJk{|0vv2wIrKKV2h7uZ}KVC zL{+*+n<%Bd81J8(FXe$P@Xf;!HX}0mw2F`dLmothzX)-tD-gnCM7ISggVG!7vE~st z@laRqmCiUMA`<*w54OuRafo{8j71Sm>awKN|9O$uWYip9N8EoMp$_$;(A#IGG0VKb zloj%iYFs99{umIP5-BIRrz(Z0*B&H5wQxeA2masRj zt1olm8{x7EWitlhyWgj_)O8r~*&J~#hbiD}QqS{;E_d{bcX*LJko!UZ$$fiEE-w&t zf_}CjBpt|@wPKmNeazP0nv}$4ORSrh>3<`oKxlx`_=p(jr8pnjLb?nlrWbY#PDVm= z?s4vk@>312q}N*v3?PPqK#?mrs4>FlGXAWDgoW0Jlal}*@$CVugbi&gY0?;eh-_2; zVTmR@PNQ*Z0~>@AnljDabyH(DsEDw*z9DRYE8d|q{PZ{u~US#$*|#D({+zdCtuP z$kW_}b>0Z1ahROav2uw+aa%C2m66Z|kj}uOV$GZwS$6=nV~*`ZfdSWyD*Mg2)g@=> z-2(+RClNGSCK7lRA7li0g~re==z?5eI4P>yfM1i79KOZuFf}Eohq(3%OsLmyR7sXF znR}gq?l?(F4Q~GL`6TxbY@07xV2nG)gD(-=H%q_TCqUV$jb>&JunU61HBQt0nK2=! zl?7C)1aiK-rfC{61Fm9PMVa6U5OtHG4ekKII`7-<#gx`zd}l_Vu!9~zVz{pTD$U96 zgHcmAP23wa>1l>H?18`V*{`v?&wc$LXm1NfSS1bw^6Mo`b%O5qm#X!s9$<4^+t*Kf zpeM^Sd0PkDU`#VeDr)@e0?45u8Wov<(|(y;{X=WD^$BheRE~Yybd<}dOp+(dq?9dI zv~Y@T9>KSfTvRCU`|M9dpxgp3x zEl%kC1!n`@<{MoG4BOQP`e1Vxa-3IB#fRw&zF)-iQJDeLfM)01@fnz+Ir1Jgp(jPN@GWSdJ|T)C6Yjx}sf z+A3KirS2MlFq($!t`WM+wLl7O<9AD01gIOB{F#7_0If@4+1-UhMFlvRs6JB-$J4-rID;i$>i{n3+J2gXn~s6|`P=t~NQd?VAm z1i=~UI{QTVcq8L^OP6$@^)cs`Iyh{Yuf;R$Jpjn&TeZ$FBLMh3em^vG>-Ecu!(@Pq z8Cr-gD*1GqR@ye~9fYo!#&?0=z>b^1KF@yO930_-fp{;!7kk)jJi+Fy+ZR`U=K|Zy zly72KM&d}zo~?dwRu`KQAh%wR-)$O&2~4x@9Esu0WbwjYoR*5e)_sISHQi-|_!b{> ztFTy=`MspRJcs5&(3@h`{ahyjVQyoB2-smH^rGa$Gac<*RUP-tbE;`^vK)0>Y0)@Jn@~l%LVZW#MA3zoxHjI6#c`xpzcqW(!tGuf0B53Ruw@XZ@v*~ z2o?L>kLF2t0}~fD$=rup7i}g3BqaQM}grj-;$AP-rhckwa1 zmt#TRs_Uy}UU!w-7Y9a^Hjx8zmSUix8$n)@Z~_F#v|Hlh+T~@@ASb-!WiM0b)G8|+ zzg0^O`4sNw*sfR%983jMqEcK_%0#g_NGXJeCB7B)H7U0+Dd}?wq;VWd%F$=KwyP<_ai`{V=Pf@?OrTC%H&*|JY`EwpN~L$4TKt*zyVnEwTe$*kYyn#s6c zw-{tu2ceV&6NzHMcUc40_$KJK8eu!mBSBh(VrU5+^2Mo!nHcxX0#Gz>M$(weP0oPS z5ad$_R>}1m@H3^9YDQV}Yil&_zPW;c@U-tFRa1C{mYs7u$ds-lYL!uE;6yyuQio;I z!fL1ZHLaV+pdbAXL)NP&bk=>#9t4Gp7-Z zT2mF&n%-W8QFvv#DVHm>fZ{7CtYo3Omf-2;RC6L#-!)Fzp^a_H=2Q)K-%KsFsi{)g z(2nJJC5eqWszwmJ^;&&yBr7nkY_hc?x4dcxAy_Gz0~XgRYFJisO)7UIokZ_T_tqx1 zR8%B#xkP1_pzG$eLawSzj?I@J7A2Oji@Almx;c`bLK1rMto^=FBBTs`SJYa*7jR7;X zLj5Fg0z?8Wk-rPO;SD{HysHQ9`|p7Y0id*U0AP})00;$DOL-l4RJ(omSun%|-9_D9 z(nGFzWdw6@^^#>r%fXkC``0fMWwXoJJ>ra_rH5vBqO`t7^ zha5Ieo3K!Evj$&upL_%%^{7$geuKUJ>ti>RA}&#UH8)(x)o(tuz50NtFJ<fUE7ZOcu9~>pCJK?3x;c zGYFn^LBHNp25DVzb5BRTrh1AWF}Wm{Y+I*uSZE~RVp(yqXFM}z32KBGEWC#-K(lTy z1>&L0`lNy3>4r3n=vE+rR87b!Xqy*DFP$WifR7k4v3jDhl5mQUWd}rK{zmuY zeQ*KyHrt-V)LW2aQ&eO?5^D5--U>H(MaON01YbfOpV_MZCft`otF5a)5T{ z-TCi?GVu`Z-QvEJ9|xPlKpdKP=E@mN91BRUmf?R<`cnPt?$6#&XEE&8B(X{=-JY|! zMf19pyZ3z;T|?Qgg?l&ooQ-N)zb(Z^jN4eZgW#UkU`^h6G)t0N5IwHq4ANSQM`_C& zM_^bJbylQ&huLw8*Eqajn%4;D{P=PS6UT@#B$Cn`^5CCNYU&k-b>97}4~}}dR!u1* z;vI5m(p=4jtopo{(Z-7H(%&sSmvwCS%W&;J$Xi z$Y4jOY7uXlv6P4)_7R`_19^FH1WHznmiN`l3!{-XQ^;DC>kcHY=SSVi50851-6y^W z*(E1>VQSaDLo#O1yW#JJJkka{ON;Io__67{xihqko&?r&%`tu*(HeN_>xJ7$5Hg%V z-xTnUwxIi^ofmi0F>5w$vEaQeTszCEF-g@g3!QMk_5GvXd))^<%7=rzgpjvnwl8qi z9{_1f+oWayxjh$bHkmk3*WiBO2S>g9 zo+vP6ca?}C%lTEaMKtNMjd)y0mkmha883nY#WSsSF(VnvtTEHNcBi}lN%+)qs*#P8 zE3=*_@kZ4Qvkwblp>RuYk9wEdfi4srnuXe}w3)T+fu4X-W7>?3#Y*?h;;71>luKU1 ziEc6^PsC;{)OL43(>-NDHvvy6JIC2)Wii#m){I?}$%WvJ06NAvTA4)cE_uQ>o?`RR zgg3Jx0IPusI}n(Q7jqaqwil`~6EEr+t4)FpT;MJ0a9S=2>JCeJ8sf#$Hj|2HX)t%< zk$htfQQ%2Jz&q;@9Qq14y$k7dHTGzVZWDl)s!pl6Au@yl?P^F8Yu=s%+LKyRiBwy@ ze+5vX6lF}O7n217@qlw^TTU2X4H4fw;dm2A(#bWInQT2F<%l~(jVIIn7`3yxR1e`b z73pjB)c4+zsH3u@pCwl;lb)(vU760DB!^6aK%h6-;it|u3Rvp zp=H1e@^{&?k7b5K)zv21+X%d?_yIuY) zw@d@yk`DZrK@>KbT6gAUZ<62X2&p81&OpHy`E@~+1ffFGavDWK8u0BA@6HfvVJpy^ z-7D(tTdHh8o4ArrmHz;{kPSP{5>!g=RI$3g2t#54~xmb zM~w)W@x#oJD~0x>L=Or2xaa|(rC-d#L8=|KJXB6B2<oV^qWdwXvvbcOo{9wN;FU?B%_=hGBqr4Q(3f~1uN_{3Pj-FJguO6 z#K4Hcw4A=c0yN?8*Rj>hwJj&2d|wds(wsK&oFaN0UoY#^AfGGyVjKI%9Ye$2V6D9Uu(i5Pv4McX7;hW z$_bcI-)?bx{|Oed2|rlg7QhPWyp@ulFB=Qp!(N}QFi>;#4nu?PE1{Ml@n8DmGhPiD z$F~AA?N+XTeZ4Mhmv%oGwp~4x>OMEF!OMXf`_nTXP(P->KXQlv3?Nd*7_t2@mrXw9 zj-5TF?zV1gGhU!EYSmm?MbZLeCWqfsy`z7C%|*0a7^2%unctK&W6m7b7dJ!#m%VW>L}f-%ylOm()5<={jD}~dNXITYNiJC$gfG4pLICSkxtK5i`F$h)bGy#l2fx%a_i0 z?G)3X9pzkoh@k?LhSrm~#i{z&h2Ck#jg!W;yCo1Kq%r2EJN0705Y5u6>8V#;g-IiU zL5%7~uz?qtFP7~_U?FzhdARUBo-r%?hpd285~#L^p7**ZUq0jQc3b`$Ow00k;20*M z@00w#cV2EPOXu6IDRM~eTSzsnzRliUvU0@HZIF(ag=K}4QF>|bC{l$5X*nD|;Q)YiprG^2Cd!rs-p z1kxSSkFDW2X$*7V_0nbH)64mp%Ph9g>*q(Wc{Gd1~uTQx<; zyVuw@f(bJ3KF?kQMXE(G73t(}XDn$$4>#7h@3}hW?dfHuBHr3uj@mRdeRGw8ZkoZh z284w>%y9PuH^#hu?n`W&7ljfr!wm@waH9{zpfw2kdmh7 zg)*PYR3;DzlY5XRj{-{otU#iTl#;bAHMs}%$qg-i-RWGuB4-(ff!nrVLSa1HL$B5Q zOSOFI@>u`W4Fa-e-VNknt^>ZvG}f@J!Q)_7#=vZ`2NddYR*?+cvlawXD*E8gYa|fg zL8M~rZ*u++^7g%3Mq_RoiyMq27N*_D-_Ke&Cj4`OU7B_HAo7J(-NEI=jian#Lm)Pj z8V6>gWSz4-#6BluZ02IIYxfBH(E~((cDsM|7HiA>4BN`65Rr-%?*Hb;>NRE-l?>Jg zEs&mJwtA5CSX>ysK6wRlrlud+%r)ye+}0)LOASS(aoUIrPQ|n`i+I{dL3JN~ZnNOt zor$2m*sRM4ziJKuXCw`Se66A+=FK8H-Q1F;@UP8ADYl5N?^URB;4>|}LJc;b+_Er* z;4SdiUme!$JHyrWVTF*x%lut5Zvi&{1dHU$QI7nfF{ zBQsU%-6EGPx4IIRWqq?utr`M%3%S~CZ_6dwlP5`YcIaFk;VnV_bO$H0gB&9OMm{_S z-lXKMW+_-BmU$fk$ArQyc=thAvYepvCcB73pOsR{^lwKKKqgQox?~Vd+95HGF3Z8# zqSqdF8$LDWt;&ZUSRf=PPs(lqmHHsZTRkvB-HuO>dEe{a|CurG196=81c_XoasT>1 zjCp;O4!cPo%M5!`%|7iu{%g=S0-eozEcX3|De0Z=E1X!hI}&~{_pYniv#*zhZ?EFS zaA7rSUBvy)lA>nXIP)JepxtBn8a>dB{3qT)-(rB3Bs|#5Mj7y+6j{6^X~nk4Bw}5Q zl+6U)dR(8|O@M|~9dag2q6gfviq?Ujp3jkxZW%uN%u6h?{80RPK7ggz>fwyi!;1sE zIXY*MHzo$}Dg!AEN+9`in<*LX_IaiuP^tdjtXup|W^x?svRX3YzWcLdnA5(@wuhxF z`@~_(Xz|lF7Y}pQ)r%?$LE6Tz|JIndi%(`Q&@gKH=n;fgU%MuA8S@Wspf@|qwAju* zakD@v5=y~-`+98DjU(|I^6@9RIFO005TtE7*17A)&w8zae9s*E6@Gn{#-cmVOwHfHKrcc6 zjD>R8C&b-jjNF25K6!I|U!7O8GlD%J8ITI06r;yi|7M?^eg z9J}?PRfjE_)Sn^0WkGtQ7H=2$DNtEcC|B{Rn%aYB&U*WDVUo|U^OKmS`cPS@<>gnrKlg1?tuocwRK?ZQ8ybsR=hhojyi_W+3b|VCPX-ZlybX z<*e6Tu<_RiU&4;atY3QKzQT!hi`hb&zv*0aCJR%}rz(eVHsLIyyf`>Lq*V@_PBsG? z(By|Jvzwcn8x!3*i@ zFBO#`fg;NC7YU#`L(%fAykc!Ds|%Ur0q(*Wgs+Oal_~#eKAC7~!!D$Uq*6!TtS?ai zW=-OwA8u?9yi^si?X{rUAHpA(m&0+@_*oCc;C_TVw{POC*Oj--V6B#eftEb%{+Qzr z8={IZzR3jd;@rL!Ovpl_e?Uyp9d*AweU>mn&(c??INvAB0KF(X!x~#EZRG7j=|w2U zHPv_7{Ly=EU)4IOB%O(HA19pE5kDsO)472i?KzXGzoX2y-K3IRZD`;f1d=y^K~@VDW*SweTQ9B8f@SioX_*#3o*)lo|=3 zawHIX7D_YErJL+vTnvciHV61O(MK0(veZ^ENwK; z!(#0k=g)fm?k?MonE2M6nCC`so%J>~GbRzcSTz~V*h&hQ5bjLJt8stBRX-F>unGy0 z`TFg%-XBu7SzK+E?pnv94DAwkH-DZE0if}~?pOD1kvIpeJ)eAxp150B5icX(iS_nM z%xa;2Hf&YjJue@IE!=Pz5GaLfnh;^&jX{J6u-zfI>Hb-7^F`noCJ6`yGu8ARGQ6pl zfUQJr=rx_x#$!;;xNS$5hta?$=E1}>sV56}=6&Wu%z54;-0DjW%+-dP{ypx>9IMuGP5BnkRBYLCr$W z!fYR8xlA5%zxfo}>B^rmZdsmdw36U5X3b$z-p+bWtII|F0%bp_hubNRSfgciS-BxB zF}exfemc7W)=V9n%TvY z&39Z^Q;(KgGT3JK+W&FZTix=mKwB4&-nu?7KbZ~Ltsrc2+!G-?+&btmm;~#BE82Fku+QRuZs{=2oV^hn>#-%6BttV#W)y#uX)Y-d5oz zcjPVTSC3p31bHrr&XY(!J*9BIz|y)W;AuvcPC3fMcomzlVuSZuk{5QzP!CXh%hj-g zIFH$e0#t^WoPNd4I@L`+ja%`Nv)&fZ3(vaK-*cA0M5Ky_p3teB@(4bMvPnFF*S6 zv);$Ui+5pLiN)&1BrL5iK~O#Z28t!uSJf_0$U{;wm~N;8?2zXatmqVv+J|cc!nE998GJU|&$mN2YS4 zk9RvTppa87AH;2q++u^`=t?Hi5$@O#DW4ms-isM+EM0aDl_CNY`UTFf5apOGg${{} z*O;-xTqp~)A21sO!$Y#2?+`&9}#~v!u>~Z_iGl>;0)5qc)&eg z7+~&4dH&|8o)Q@2Oe^b`OLs#wSwh~&ObU;Y$L#=-F7!D+^kwN1mVSWzu}x`{fls{G z;H?AKf4ju~N8@hqMjYdS#X=)#ps8^C7@527Cjr7=4lKWQSt%T}18PYSbI=EFnkTR- zX#@61P8{r$S?&B8HoI+c?2~vMlTELVz&XXXe-KV|8g^K==|53?n2fGGL+YkCcWkKxt_F3rKTQQ)bL zP`J#@?*_O*dQRCj!|w=4BoXau_Zi*q*=6SZ?UPKs6J`_-;Yy?Xwz*&4O$}-^9 zo8zWZ^|?>%A^d(md1c=A4AyT_H&%sKFDUB%k2X;b}`@_A(8l6 zU%d%Dx}ac+=hTwHG6;3xdLE(<1$GNgnNoSp%%3tTt)Z+7m+sKwJ`gM8X4cJ;DE?7` zW;K#F?N|$ii$YSpsSg zxQ1u5(}{e~+P&8AgEExtAf=7FJa&nYm3IK!dFbQ;wQ*B$np0oJ3yJXUs{) z=(N%4Y}W-~l?zz8Xjj(5DUxZ?b#1#bDLr+^GKJi!3+DZ;jM&l%5>P$(}xWRJNfIQ;lj9g?Efb@7%;1)89 zAgxW3rKR6@1v627QrFH4~jkbdJVETq18w*5igTuJlXMq^^ zbn$>`@yE2=if4ibnKz;W#PD}HKm%{+waP-lwA>RZ4{+6uT$XY6Xs|$yIJR0p_Ilwn zx0qR?Z7Tu-5BVqUL^9X{2Z87lX1m2L)!-wVhZ%{x+d$VyB{EpCyFt4HH~Fen+<4nL z@YZ)OVv5B^hFz_^CIaCTFIwsS)qf za+v~7V8t7_dC_dtLsq$KD>Wkj8B(;G90!I;vfRVH@pAYvrRIaI6rNkcM7Hq4L9NJ} zB@pxCepfd^yeN3o2>lZET1;uwr%W3CHVaw+jta?P_-%fIm7<6;L!X(Z^Uc612tU7L zx#4FzQ?4`a%G9XWw}*8w&8>=W@auT>JOH&zwfYrR#vuIlATI>a4PHknQFObgft#Bf zaV)?ZIOsk*&9jaL_BpdoC)ac7R`JG!D1Tm@4yr~Nl=@zeC-I8Vs{rhFzv=c}tz2|Z zxrwHdPrLjzg3sLvwk@a`kNBzp)h-=moUAoISyTfnjQQ;uW^EwCCxX`S`M}RA;>g&_kcd|q$BPFMZ^1-xI$W&KmumEM6 zt5R(hb%{z6Q#naBmny=hQ&qkB%3NYRTb-^Tz9?IrNhe#fP286w{3o5R1tKH2ywFft zn@{FJrzE-=&rk+jj3iLig+e}?$|nlFiPYYD%une=V*yyoB)Ol3>U@<78D|b+vMS{F z*Kr^J!LZlOtJ+aoQ)EWP2VRctN`ObT?-n93zmX>7Y%SZ3cdLKxA zC~_s^y^LJRdi%4kZPTBG3m>{PpY_<}w8?8z(56D0N^PpNsn(`On_6w^w5iu-xi$^j zG-}i2y}UHv?EOefWZ$ySFLSjYZuZ`C|Bh{oZGSHGXCHh1{!CqT=MQ&yhr%EGS045}H}L7D(Ds)-pKSJi zimG9!J|8N$-{;U5;@QNq?)it0u6^ty&wCqU>v#S{i?=K62L8UuTmGTAYxdZ*Xw#}q zn>Ov*bZFD5O_w&^+Vp7CtIY~+R%)|Kn?7w;YqLh1er*P{S*y*UHbdI1(`LOk8?@P| z%_i?<+->$6K9x7cXPx=*BH7<18{p-4$ELimh1bRU?_M7lhP5MNAvDl+9NYE(ug3TC zv$a#+KnyozBGwR3$EmiR$<&8l?rNFxE|z)U@iebE`C)tMMtkY9?5cP_@qM6z<8)H| z4gtsDgo*?Wvj(Qi0w`ITU!YoMtiR%({nC_IT@{JL6tMWn1|nJNMp^m7xck{(p7L6+ z0h@!x$MSwi+{e{VgtZ>Nzk&-JHnXWMCz6%Vvv8zLEUsEZTnRprbDFQbD!Y|LN zR=hSc+d1Vz&v`|yJTX* zQ}(u-1mwBPzs?uC|G>6=QGg+4$$diAhZ)4~EnEoG;5)RpQdS})ZeuLKzgle}bIp&d z3^9qDMz0Ni5^s$@@Z3k%ybbYV_6Xt)m&8MkSOe$T zyGj7yECpUHX{?3l2psW>%Nfz|5v3A1(F|&&!(@+cOG7*8R{jp(RuHl@0-<`vq$J`Y z!oREG#DRAU@SEa@bgRJ#(RARQTF5h(KD30_qTYWd2#WyhOU5lz5Dy8W!-U<<64q~t zf$hXLE{UjFUD2H9$m11kZf;_8H5^_*8k2msiT3EShy{vJp@_@`_l4h^@*0M~!&;ac zM_SJ|9f{{O zecl4ohGm$a2ANEZu|o}Qm9jO1nNPzde*cDR{DUd4^W_D$YeVj*|8UAX;zFOF@^*HW zJ($KNUs8S#`w~kJaVL6_*+Pb-dZpfQKf%Sl?oZjS&3hJuESYCW#`#Y^etG@BOnLdx zVmN{*fFLZ};SkZ}lA5(R`_;m8QpfHdkZgc^hUq6I%EKDKVQJH=?Dy)x<5aAcM41nVAA``QH})g6@cr)ipG|qYj)p@+ z#6anRr^DfKT4r6<6ZR(VW6qS+*%>aIypC}|Q=H4Tg~L~INXXYZ5e{DmRar_6&#}P! zeSb0Kjq#)zd~8wzT1i;2>~w-q`B^KYz$=@ozsx4@R*SPXpq%kAJ~jg^pU|sD=m42M zEnRJsyZogouX|nmKJjpNku26c69g9w`x+~Lobk#hrf*V=eoh*wO`Wutm~=J&W6Eo0 z(Mr-hr^QrFK;@lju?d@k`#{WOjNW$t@K;mb;$k!oZ0yuMvtnx4K;JK$v7%5W#kEls zi69MHX6kKR9_>RChF3|2s1NeuY(YJibXQv^+3A9zTz17hf#aB-zCj2_X7RkKcO<0n z8r*Yudzt&~uS|jW`m28rzgYADO$t02TtTq}w9r!YZfhj|5CUxZz-R-QoGICLb)M1* zyu+xMa*MSHZ*%LUoHfYyd-b{oFLvE36th0Ia`FxkfL83@qICDHe!^y-`=6W~Yy@FXXT_n2(53hHuy-Gq6|3!l>;C$b_o+@JbUJ<@ z5|x^**=>OmePWrY9EQpDr{9?JhTOexPI+rm#Hq<;c`KA6Bj?i`dI$G2xy7frewSBf zLrshUS$Lq7H{~nx=^BK=Y^oqB#0cRXi1W)C;7TeGPNRy zp|-LCmuDI%mUKJCP{33}9IZ^h*^M#dzICzvJ|MpoV%ic3K;({a&8{}I}h?H zc2_Ni!3;H^m>$5`7{xJ%x0N0{Li)Q!4T?auY6)+0zjvOdc{mGQ{=$^E8QAAL60qLa zp>*U%_u}%Dw<%m%>o#1O@;01_h7}&OmpkXpv@slwP(PgIDhhIXT=T2DEHZ0OBdIwX zqVf5uM^8N5H?cNEg$J!dEAsz_SeX z0$9D+_VV`Jl(#(;_9E_!cOgut$|ASS!!M3@uwC7{ri{mO>m80@EM}c)k9t)4f+;?& zeoU(6lN?P9-P3&!L;}`f8A}kL3SwJC!ERF=%Q{rjEN-HEbE1~Urnf*xEwaTNR2`IzHO6iX`KZ|lgRHu) z{T2-rG)S{;(44{RT29!4fJ z<4Koz6ItT81+ADxIH znP{HB#r3}rVQSHvxCcwy&Mn~L3({*DVESHHK+ z52vqIH)rovRZ`V7HS90TSCB(9lk}ga_IKvTQt3Aj^x`jS-AIOSChu=dCH?JNiDS&B z(_Jc$fOkniPPu$-D)G+ews?^%E;5|U6#!HkPq7rWpI|A@@iBA7AeQURQeFck-Td8}7v|xahruU`1i?z4u-Qm?0Vg zkRZSTScaSeU5%}Ekz{hLSh6#kj|44^Em@YVM7CTcT2}I`*G{~$lX#t|M3&caOCl+8 z5?f=-`TgH>FF4xl?(mt5@3ilH=WB2OznpBi2VQg+5*PeTue?PC&AbdO!f(0!N*|fy{UeQmu5Lp@0xye#P7FseFck4J`4%uJ&l_4 z(dKH?A2!7F1uG?SU5$hRxQE-;UYB3V@-ctYX)g8Q@Mq#$;3bwbzi0z7Kv^tzYg78I zt_=JqoAi87L_ImL!P&fmpE-3~4a69?&F4;k5L0r#koXrb>16!nwrIOUl&O*L#1Lk6D-2Eoc&fA`=F|NGK&y_xXGn!UlQ8l|v=IXHJQWc5G zfFL&3bl<(=4r4fvn-opQOXP!1H@H2CRJQ~Ck%BJzzD6F10z~{#T=C7@>{>WZDguSm z%(_2(OMMb?BLwss3d`4|KQe}en6Wj&jYJNWmZsvY`_#{lkO?dGu@QfDe}K`m zl=H_hb1{2OFA63R7(}w-1}g>^`U!YA;7YKfb$)!r|5r`Ir>CPeTI`vlW4CY3S&Y<# zYB}r;YK=Cx_0uDMEqH)X zZs{-1`5qwbZ@p|@f4jEs2W5##Aj|1;2;!9c$DaYqbwHlnk|9hTvc`|y&}`AV)f8GO zMR}ma5mX_1o*A;G5I^mS9*?D~x-vkBg5x?s`8v;;(n#>MN%ho-ig) zr2+jIV)4VM8(lr?ntz3k=&*#uL1dr8L8OWfESE5#kQix+pL5^kR_)K`0JYxz)aOTh zP~lA=IL!?ewuXA7ZyzX_>^1jKP4VLe$&gzpc2i@~O41Twtr+~-i|)(6roA>m0$rzR z@{*C_UiAUP%IsaMf!tfLFtLO~d6YSbKy>_T+!PaN4*kab2)v*2_>s<#Eg+F@DZSeHN&#VCL?ifp}}gec(&%Zvj_U z;*S0nAe-|=j|9_w44eO&adP;6!q(-T8QLJClT4vzwO%McgrKUywp5me<4Q>oh{J=r zV~>;^D+>v54RfK(58uBn-=r;EFDu=J3Me(-nf0P~=9wYag&Ux6U6F#3n`F5JDu`Rzh8OJOU&ud~^cZn8|2W!lnn2k9*Z|JwD)TC0AL*c>X8SR=d z=#8g4bJ=iY9*v3im^R%d_zra?CNwmu=u9l0NDE=JF=s1cxQp(~CDW+-s|gS$_&Cv% zIFEx2-ZkW?>`yf-uavw=Q`La5RN`yexTmJ)T<2Lbfg~zd=1Q|`D=SGrRi3G>O_bHG z&J0y1E3)<5R##{9&zAzZN%V0gp(|yHY9z+eTK;dyWHB6+ZmmtM%8<6InmX`HO($yh zR^gCSihFA#wt`%y3}2oj-AZ|ttxi>y(U2-KY-Unl+_}|{p8RMujWlM`ULSnhYP?rF zvYidb@{j7>JIN8huO-<#H!*Wp$cgHLWqkDE|2b zB1oiXVKC6#rbhf-mbn9>)sPl_RB=mCbiz9K)>Tnt`GQR z_d*%dGEIm(A)agoy1U0cO3>*bK6MsfcL~V$hgIHRF>UlZnjzQ+@ z>dkBO4P2fiuhrGbd0fgdvzpcs@E=~SJz!-YKQ~HEPxb=E6Z+f}3W^pX(H?b*JWX;p zXSJT-5D^8=&Lj0sC|t7>*)Ei(*w$Dv0k_PaAr%-pfeIBKtnzPK0;FT#d)T_f?mh9>rPvaG9Nt%Kn$sKvIfm?*O zTAlB7UuXrdJ*OxV%SA~34YibF|2o+dkUsYEK(DoE)OEJQv#gR2q85)d{-obR zcV`|Kno;L%$d(y{YSXR3y{`kQrxK0_DybBRVwj0{pw#8ob;3Z58Rmv2;4a9a46nvt zH~JA=KSk>UX-E9PRc^ZBMXsUiE`YF%c^YfOV;O-PFdo1#9-TX4~r5>bz8ixzj>3JH9hN18F*W@EU|$wb4L+tXFcdE z;uOs(r7GgxP%H&cbz(b^72MNvM8mSE#QfBIaNOuOnF2-?3b614Tq={Ed$~=t#-;8@ zSC9CaYI9`>QW(S$BbiY!XK>d7PSZU!l0B5=dzRYD9C5DN5rBdwtBE><5E? zUKSh!12DhAB?2!s)4Rrf50K_ex=j=#UU*v31xCSdEQ+{8$jg#nb@%OX?C#YmZep}G z25^yrkCG~g~Q^S__L;<9kEEQU;|xFoXyMG2GnJN-+BvHoU+k zt|aQ+qrs+=-spQG+8b4c!AniL=QkmGl>6Q|{O>&;2C3QhyglwGw!pTdo@IuKE5JpC zYEbG5UEDTdjUYN;2+^^4m_0UdsW`7Y8lw?-W7${eI{Y{E@wTO{7f;uEMYDC3Wvx|B zml zC2M-XI!RYowE$I;g{jC#0Y<6FHZJ62BSBIb5M?KJRM3&;7yM1)!8oP>x4yVRQ605jf9*aE~fUER_-IZrmQ`=m9(6w zkE&Yh60NdT2ioOCLA!hq=_mizu!u0axJ(6GudQ*cs0@;zQ8CZO;IXBHt#FC| zc-p@MnO88RW@eZB1I{e1l!1=5Ey3{+AvdIp5U>2%|9sl-2($pVUGKL~`}O+^!oEn^ zi}2J?S=&)>$#8>ka-H+F;W#89NJnRGKr7kq1VLK_%lzoAr+-*>#@`omTPn##88JPy zdzJFZ7%IY{X+-CLQFX@uI67LqLIdj#Zmt$;N5IzCs?YeRs!X43dqJtO+y^vsj=SHf zA(dzxBxe(z-1=JHP%Z^%z(=7snv~J`wEN4tGyY0+5h7QF?SHcVjQ=AS{m9g~S;s}N zmUFLQ+jw62qb7K1SB>Y@gCZx^@SgKTi(fKK$d-|IW$cf-nIXj5yr z4gdzqX7XOpAEB2cq!5AYG6$q31@IKJuaj++{X_d>Z-SrlaOi%ZR@yosl4L1}i^iC=m_Iz#YAW^Q9@ zXOC2U=+1D?5Z`&7FReP(zcHM`I1YN=#I4D3GfRtoghQFb#^~N$cgDZp57?tQj=ZcI z(Blv;7zAxz;MSCIzyeR<<>^AEy9sx411YMTj9C!bN?FcB;A8H>SOiKBJnw2Zp7GyI zvccn#Z&H*S+jhp^blgL~H%;iT6V6w29^kHF&<0rn+5=CD7>iR76Vekd!Hd9HY`O%f zGS02`qa(yL6p2Z~J$`V;KTax2={(SQaLW$&+`}_|dkXPdw9UwG*!>CTw!4*YoWWad zkl)6mffE{Xm}V=_;WWx?j91#Bg+Ar0M}WS^tSSaVtjf!N0%SyUmSx)x(58Fw@ptP! zOp@E0m!RphqXb&ZS08Y%e&mc_mx3Gx3$rrxc$51o=MFHv=4PNafhKfc1m02e z!%U?}ptE2DJ<=R%uuZ##5Fb|1gyMCzm1Er1Y*fd*?2~0?LJ3^VOnse!<58{BQ)1s{ zRcV}~DP^>hE?b|t;f(w4TlAF|jkuvl-5h19=&{G~kbCiGNs&GO-dMQ|5!rNQS@Lp!YGo_om}T!hpG{uO zuPVJTSGRIT7 zvefpbQVbi3s&qw7rZ$m1OU7xkXC>2p7-3U6Tm*?K%_hq?ac|-%$YRMaeg-MJ<-@X> z2FamojjAolbVqu}XKuN=$wB}0ybQ|b+948gq_80t+#Ks;0kVwgu&&>sAI_)E4N_v^ zT7%`-fRiR<=u-N9|mgf_@D_Y|NW#N7kgfz)ZM1wl46rG8}8f zT+B~+&B6$&isPUvvHhB%cArsCF;1A%r`^sQgXFK9%PI2rg_wTb7SMEwF+7xgE}=W%oaI(8K{;izX-_2Rf+}1 z+p$gJ;9?#jV>U7Ovpy@%wxXymUf(0Zf+2xG0s-*{;fg3VIC`r1orjZbiPKl?U!6iHuZXdvkb5HLM`ZeR0TngQ#hFdnBK=pxS&w%J1uMs&5WISUpTC+VI zzJFiB&^!nC{4gFJ?0~f#DE}?5wJ~f#2T7C~)?5~!Nd+&s9rp*xMOJkCIIbJmYj27u zw7Fm9;w`G=ol>Z+HDH&W?oXa zdP-xvEP=ehSD!;Sm|sF5oqbyo3F1B)WJ$2I`qCxtAM%5KWve`l0zVd1Gz^%{ZxT#N zQrCB1b>DjLpucZt$-NuXB!&YtHxQ=tRKhJwR9Cn3K_y1oy0!H+d(oj`&3+Vfy55SI zqmd>SLfQm9B$7~$wbg*5wbn=lF^g)n zu=4h~>K`5S&-f_%+$~BgT;Gok`t2785L3Md`gWaEd_(tmU`P$w4Y2Oyl&KAdscwHG zKSDsXnLgkBiVLL@8;2P;cV<38^Iose~{lFk}JnT;oVZ1a^tybat|L;x$Apl&@Zo5XaP3= zAa8EU{6F&T!4*Cb{e6v~FXaF^nV(hun5tRcd7UaFKNe74iwMp z_%>+QkB>w+nQ-6w=|R8S3*UCtKf_L+3|J-;OrO5S86b7Vj37shy3f63w|Z{VBWCP; z7=NTnyyr9Jh^SIp4XF~WnLje zw?Ldg5l7hE-`GgjC^Bv*lY7hSvsIb*mO%KWFDE-?s;@njt{^*AMLo|}fGmzwoLPZ> z9C;PtmOFFcH&xJxMli_%1x@w7z9wCnAPgY$-sQcehRGDD$E%I7$1}H{-w%~%U#_WDN=oQ>>neqe_A`!ioH^y*}8GV-84y6Tf#HNk( zkrO1N7!y8VpwHMRtLJJr^X&n@=ejxOni;3vynhUK_<)%U!%?2i2T($`<#n+*X9Ptc z2?Aq?0U+30w~|>RkcB12twAKgSDMX1Te2?iAV4!S zqe{k&{`G)=ave;J1OTZ}rn{9=XGh)>8E6$Ri$;h2!4x4owZFaywSohvaG(9}1AbqL zu+j9oc9;Gi1E6&k$c3%oO3|$=Ff&sKG~#df=9~FNhoT*aQeE6Pgh!)exLg&f2{7fi zMG{QJs?2L|>o!qgTii2b&)YW?Yjh`M)~PMgEb@P@X=lxe@9Y{BZoKJOw;u%oQDYS(WoW}MV2mk(9H3k4 z^=Qud;X(g+!n~F1I8os~#EFh0aS!roA;L|0Gx}JJ&Hbo9BUbI8z9bQZdTvoY^``$e z&a}zYFI_7*dpgEXt=ktF^n0~mNgrH@TJ674xyVZg{R1_uMeI)ImxeA-MhTP2*1JFB^66Aj;>3aP%_~oT zFE!|YDFjW*ulJsA$`1MuL(ji&8MwsB@}6Y1Vt~>+%91CWvK!lTIUwlDlS^~ybj{`c zd#aM9`FJ{2w!WFf3ZNu!NYs>8*VboS@GwREDSbYbORjBMR$5h6-b48Q7DT6H1KY0j za*bvOtSU$_2TFRcjt$R}_|ouN*1Gs72K*U3>`(Q!ET8g09-;Xo=M=ru4Aj z;?XghX70oay=bYVt&^s@ZMJDvBN=1Jk6H97i{Dg8S(o@UyN3J7FAcye{a1d`aET{& z=RZ5(cO$iuk^9&`9l#{=+x)I~iO&s?IIpmC%y94m3!0CWax)(?esAd}UUb{+PJ6`q z?a{~X@xk?UpZ`@VT??j_T%OF^s!v^W$QEu!RkU5@m^7kjlVn#HyNCL4YRJ9%YXg2Q z1}d#KZj5cyf=#*K<@DOkc$dHfg4!cV66+3wv0AmAV&7%~+~RC!Ve}-m7$%#Ooomc} z;nxTJn{MZC==<~hR=LOg9;hq^0ZIdY7L%R`%1-wyU!W8Ao3La%-cED(CUq4O%Oj2K zi=Yt8et^D?qtm9!Jfb(Pj~f!-DvIkwHPOVzo(_P9HO(*S%71gfUri2NmVLik?uFwB zov!yw1AZqWBD|LrgIK%*G(zj|JCXC8V_T>HtsTcSf1d-Q$dq&1X`e%|!xVzI3%rm` zz`Y{m%kKr4psU=a-{S3!k%)Fw#EuGGB$ND{!tC8Jz)PXdr(3@~;C~w9t_c7drE4Af zIQgG5XC?g%1f3g5Eua|C8J@mkqgfgyGgJf~s+4Z~rfEIvKJ&j1_yfy~C}^0ETC7iy z;%L8=w0!emg_w`+$+pH^wHx?9n5jo&Q$ypy8nDk<0T4ZLVu24MuEyxN&9ktM6j(5C z2v0UnUN|;AN5(iDa!ph4s`_QEyYo9tc(9;Yq9TzqZr$$=_^qU3H2)rvrcETd!KN*F zda1r>AI|kN%wA@d7G#ef8yg)D6q(wJ&muX9XEaz_GPp=&DlmFKpYbG4N9j@Vz2GH*Xx+?6tALj71nLS`izVL4c{5^mME0wafd#e!30PaDI zQs=8@$z;c#jAm&o?IlMo!zHa`ciOhPCGP51*$GMYAsMO&d4oRs1790Z9K~xDDU3|% zOtLOnnyaWTODC3PTS}X|R_$MpCr$2J*UB7PJDgnbY$0^w=8CHHrquSbWNorDnOmK# ztV~o8)7z1GeH&r9gj9?Gg;PODZfUwQ2`o-Uio5`j!`f7?4xJvFKkQ*yELZ23wsepe zAe+gxEx&xI0$kVa&n#9IMj2z76Cn=?`JAA5HUv;S({En#FNR#^cfRK(KK%KWAJ5RC zdq4cOl^;Ld62>oF`Y%)K9tt2-PS7P6gV?<7A3neOWl#oFx!$tjq+d-ier z@NRYLGO_imwM!E+!T8($7)(~Jnh`FXK+hq2ia2utG|!G}D|jU2w|s4v95pbte)kdB zQyC=^u%&rT_wIL_e-_BIwFP~o7+LL)OAAb?ZL7P&@v$jPBl;j`>YWO<)M=b(KL+?$ z9G^1@e7oE$9B$uhF7{?Y-X)Q-4zvs2gLC1tTt?TP*D37Xw&%hS%yMH-6+hL@T)9mI z+s|L}|2LNB?2sYk7}-6p4d6yWKzPxT(pJ~Ho1df&4Lilf-B4ClsF>}{^+ z7cTh?n*%^l5ri?Et!3GPo}AVFdr{AmD#Of;T)v2c3`!ed8C3hpTkh$n!1hv(`e)AG zN3{EPi=4K*nqQ>;41uTe)MF(`e9pMfaP}&y&itV3 z6>hdIH)#mcflp~GZr)OR1ZwhHZ8!-=)&|ewS9V0=V>dzG9=k0GgUi?E__@J$r&egQ z-T-sXtT2y>HGavRN#KwKIx9JBtNWABUhC=MuWMMt7|X|^;Rv{Jx5i=3GL8F zJb7`83z$+{5if9W@FOIo;7zjrq@}H2TT=&jhD!JqE?-LN(_k`2#{?r`9`Hny&dHp_ z*E2CfU`s|rPyfR&U-Ew_^z=)gzvRD%P>$Hl^t~HOZft>DRohg{c70rvRE@8-@)P$! z-ZXTXKQVpL@^K%|Is+&OugmWBjLNsFDY^G=&kbxlXQF@JAPD}1H#7WZk+<|HitFhZ~)d*0g zOq;sG{n>8;TnAVJOWguNpR;_P);+7R_5r&JTPFa#yfb32=g1XIk9a zf5vF}1hcval$Mjyh^e85f@%xN+QMDCQ}BS;g}{Z=Zjn*gr;CV^`kfUC)L!lb|NN5Q z0}cc4w1i=m$5#9sH& zSy-p2gaJG|%H{_AsF zH&$ItC)Z`#mDi?M=%v|Iu48|7d0jq6^dOQVUa2^8R5aE!WYT2^%9=rSBZ1AP&Weh% z^y}5HFX_zYGL@-ZHDQJsEMQ5}_f$erlCpL4WzlaHOC#Ft#ge-ur+gXd(n|k%#SL z8TZhnc_h~mb1= zEt%2=fajmjZ{&9$E^YzDsp*-Q|097b1i4eu}7*s3hB5H634gk3FwqXyQEQa8VjF`bXx$LEiY zY)CKY^aOuuyjYtTA$DaB)t8A_&`-6& z#_OVCvF6uOs`&@m2FLP<17Ll`PC{`@p7|zA2$?1bPQf39%Y~jKjuo(pS|{zU{S=$+G9R~L-X^8_ ztYMqGQ(`qDyTpvXsFAr7)7Nfsmrt|v=S)o#sL`<6!4wR*eP;&!^+YZ+4{R}1nS-&JCjUWNHb zr-IBNH?&h;4@c&J3Z2cjxjHCcWpdyQE(SruFDXl6s7{9Q+m$nd3tyyjfVyMDOTRVC zTbAZ?rV8zF-{54u>$x=Ocdal`GYeLD#q)0rvy#-Jdh(_}vqUbJudwTLKQSUF3*Q@Z ze@AJ>Zu=r52z5ppmte*&Fnj3tG_2}{R=$UFXW&+-koFqd+P00K{ch73jffH6#)FgY zWsVx%Z}8jiO0Ew2TepMD!Zt70{XB3li5bMY(Xnw^nggbCsafA73XGKSvs3%SQZdhY z;O*vI$pjTv6R^qh(eTjEhI&6jd7qoqRoudEE8NJkhm$IaNoN~N>#=5Z3FVjYv8e$oEW!WXKd{RN$52zYUOO2#E|4!=3(-QGbAl zkC~APT&Ed9$&ZBr(R|8p_ua>TbkyI7hXjFKIdyt3tI9R}80a~8m1&d4UifDmzTw{d z@lk)pS}k95pd8Gkb^jhyX{;v;?~U7LT-V7>jEG#mozaC(ckTV)-?YrUOULxTz$#}j zd*?qe>H{XTyd%>Zdb;VssQ-cRK4SM}0H?LL$}(c{%xcAV>~GhbvJzqLB~{!k0)>Nx zI0GmCN{1beT`x?Kyny?$rXpU=JC$R|LNgl5} z+-~XG>)rS#LDax6d}<2yyuA%CpaR>s6gw?!)peeHtq>mZ)_T1mV-8Qod95+Y&u7Ue zBOPI}NhcEg5F^7fsBqu<1+c}CUfKM$s7kfGN_9irWQ-*Nc{M@T46cW4-A;4EX8V@q z+FM%OpMQ$}V*$WF?Q(~IQFvvzDZ`fxxNmUO26X_P!rlKgFh+j9zQ*nT%&5N=tR@56 zGOoBAr`zeFQ8o)T(o$I~-gTPqd8J&u8WA88`b0!X7i|1-yZeoQGKxcBK}EHJOT(CE zW$-gPvP!gisTTLkQdShO&TNcogp(rxE7!yooT`;0#^@jEW2WGY0u&2EhD2k;i;Naf z`rkUl!E0tkUN7ph+*5xwm`ZrR`)R6i68KUd?ylu!0#AyZ^57Vvr2@m4? zmdTr?wyJhiP-nD3)ADv+gfso#SoJ`be5VL=$y~l}MNK-ry|gazflI0O^-Uiv`OQQ} zqORnZOManbq2wb!_>U|9pZ{F;zwGtTx)y%-+He2UQObW4oiF*FCH+4u)bY@gC8Zzw zOtEzNElNMUPFKICb78Lj(?9xuT&0y?{ie?Ol>VKSyd_Jj|C^PlZ(Yf=XRQ=UtX^_5 zsD;x0ue|3y^Sqei*56h&D)s-fVyXK#i>0Q|7fTgCXC)eQ`AtgiqodaSs#Q%B)>T=_ zOWj#=GI$-O{lV)fZRK^mgHnI+HcH(czgaw4cnK#fe!nK&(tE8mzn0=lR$N1A+DiSDMy=FG>9Uo2 zDV?-Z52gK9T1{!Il~z&ex6(>V-BwybsmV&qDFq#~j8ekRbq6VWUG&iozx@Nt_W2)J zwx9nG@c%*o3(F4q|Mn-M=a!7e{&b0pKRD!naewAP=7%%)GB?tHpZ>4uKTm)C|Nmd= zBmeLJ+WqvP($im_%A{UK=UW3>nML+UbaoDPP=lum^b9)AvdCB1iNW~Qc=yoaN$A&w?c2foHZ z4+rLoPju8P95-`(dwTjl#R`fFg_xTHe|h@WOPoSS2v5N~=kKJ>`G2jWiLuFBl>c01 zq>IT}4!+6(I@|Hdn;iU}4yZ>^DAOE&QO7rjrl%->R^>^HeIjL zgNMhT9igoLYz$@er!SP&pXH&H{KG;;J~b5HR>!H7W(I* zn%#nw(t#tX$8Gjma# zGjcR>Yz{<7f`Dth%!ijuhN|>un0E4KUj4^k^&fxKfBaGZ@kjl~AN3!9)PMX@|M5rt z#~-zmKk7dIsQdV%?kluYaT@VLd1~zLWYk($tu&0*rm0Xhy=IN#j~c}vwTVA!6Mxhu z{-{m-QJeUqHt|Po;*Z+IAGL`;Y7>9dCjO{R{85|U`pN;n`zN{|9rF1(>_6>(bj1JK zzmI#~iY4(+cq@LTtfivadzuIDcRuw>9~u2=V@5(1$j}6g)0&*z8gIBKe~a(Q zJdlYN{{4Y#p$|zP-2^CwTw5PEbAWpZo(odeUc1827Tl+9wTOW{ zCo4yv-g_1oyl-@bek`WV`KxI$|Bc%x0~6bf2SFN{XK&wZl@~ z^~fxE&*c~5v?$e5L12*l{2t%swzM=V=fnhGwO*$m zrM!70Mc4B$0FxpZM;k5kd9)HZ1XNBd%r)t;)V28?MNG`c`*;YG zJy92YGnbZbpc6*jU&v`NQS=jh+~@l6|EmO0V05UkE{@<>Jw3|1Y>XzO{pP9oSSH22 z9u*x=X|ChBev7cM$70uCz{}#s*N=z1&`0iuKHSEt2!-C*_B59p^i!TZ5i{mXdS9Bh z>>1ZlG3bA;hv*%q$8sK@Gy$&Mq{6;>PE@w=Q(6EXdu%dXz1!X}=(lb*1Iwekb$n_) zP`2R&|A)1ZSCvxv__Ao22m}VqhG1i0ZCOxzue(2{f+iPhq#C!1-;P@Jc`LzHlCFDQ zx)*Kj?ffGNKLhS7T(4RuIr6bN`JeW~*Cq*Hd}JE%WBtsP75S_my?%Ro2-Jc{>g-lO zK84-Iy@kD{v2QB>=rAXHHO4()Ct$9K=M8+RMyB!e=2&IDH)K1~cK2h=IG+;xgKo@h zb4^9N%m=QA-WYeE!&b9ewcT+4H^mMz-5^FiHlT8z7Gdg-M=4&k?Qn~GfW@Y>(WX_<$%k<_ zoDMwJ9?vlb`4w(Ewwo$+9#StbExw#~@8?XN&j#wYV$rE1Z22~>5w_|NVLmWd!L{xm zxYk)JA=Rc{zOU5X#FkT0!N^jNA378INP95B-ni--y9fQx9;RnkHdJY59UnD|j;}Aj z=7sw6kEAo)=7rbvt=W`+B#C{Oj6w^VDfyLte0Yes3f#@}k2OIe?(dh=t!@Y_QA4}5 z4R)HOIA*?kZ1&Ak`3OCdu_b@ZjbZBPn2&^C!eJu+cpY^B>M#9@_R)JMc1Ax*G zvjMw>J~$pG;Jcpf@9}+(b_+}*SGz?4vVzxbboT2Dy_ux zDp3Urvhv%dSK&wS9Uop-1ITzpLkhNc^aW=Xi0 z|MHJ-u#>*7<+oY`p3gwV|Mqg|=gLE`4{1s*EzyS1=Y@LTeRg?7XIJ?lDwqzvZc{Mr zd3|fS>65pp=jAGvNAV!v1%~zf;!(TjugBiRn_nN(E3&nozv0~{%IZCTwev_I?N&sit}5;q2hx*;n4cR zY25eL6e~e9ySBG*9`$1J$-Z!CP2nuLKG&(NX4lb_P3soFswrrJmkx#dd;2ylo^PQ! z>bv<*ihw^)r1M1nW2Y#tM7_6oSHBlpZwFks3IDTrp)cgEFTVXq$lIX7v6^1g{`2Fz zLO-Lm(H!zOuH96;^a^vAvW=m7VTA^(x!?2F6gyxqzKGoMa6I%=G($7sxex!^$G&|S zBy?ovTYMo;Ov;dRJc%#Z%oKUj7YD4oCiVVxfmSKJUYMW-oTejJH}5OH_3pfyyWEQ-V9UXLJgDS(&!3u`2`brs zo9yDFl-aS%qaD%evW5mPMR42@l4cOk9^9BZ=dqF6i&r&=yx}p*H0Yq2hU~?8zXo5@ zVuJ`PpPigH9yn<222akfP%e9JsmvNyIvy&Kl&))Y!I>#9iXK92Q1Ik#FN}^t7x}zw zK1^(&dBO!J@~JivO{*&z3X{`KP2t#02pS1PIZ%!n0M{M1#wi0PHc1rKgV&SeOi}R@1N-nE@O^ zHxt|g{AW!TIU&|vpQ-YzZh%K3Tn~nqsE=sP)&mXr-bUa3eZUXnS1o`&t8PD@+j4cY zgXIFHvC;seiQAXW6tx5Y;lgKK#*u~dI&woFdLHjAO$)g78N!nnYq}6j9?k+kq> zb!c?10ZETu25Yi)WLZ8EipiNqkvR71yCGg6%=nMph3xh;pCO-%49y?AYk8tCJ{OO1 zW@e@^Ik(OahkRLqKXx}=f3R>zVR8(AEY4}CX)3`#Q>w1Q37{jp%r>GdPb<>DND#Y+%`h=>npU169?=RlPokigh;A@d!Af!t@>JkNi^#?Vup;CS2O6A0?e-N3i)@3 z3Sar6N6u?K#WLt>@#J_|*qiq-FWLPVe;U#qmL;_m>_*((gpx=C@hq{U=~S)~w>JSl z0L)*SYsvwDl*lGBX?{`_upcR$c)CWsU z#|#VdX4R4<(KjF)8*k0ioIA9D9IsG>JM`|l=Iu>Il3;p@)VnEy?ghSWoNv0L)lt#y z#mJ@rvIJ9Jx3`WH>O*o+JIDk4D%zo^_64Nl4x(Kynr(u1)RkmQEvK%ml)?RL{}*ba zItfnGWU&`ku>~ogGq5nhBS*ZFxw#qQb>u{0Z^9di!Pd8|ZEgUjP}D~)Ao@j9LdBbm zAlA%j`rp2BUx60s+Hx;43%Z%^)aKQIh)*P6@b>c7MY^PmtM3|N(o^R`QFd8d6!sX* zinbjq?+Qe&;Gh=|s44jm+2MSC3#c({AnGxyx&Mrs-9b_c#j7tB>6tz#lkW+GlUs1@ zwkHw+Hf&INeUYT;<_#Lj=-BX(!Y_jBd*o|wKJ3BqAzV-2Md#Flx=`4_uYwzVmauj+ zU3tk%{r~~w+z${y-E%$^y9$me=sv+SH#}t>59(SKsLJdBhg~C$^Xj0@_-Pt(wB9-# zir^q28leg=773vaE_g9=(oWA6CtJ&SC_G_gQdeiR*q{R{xBmd?)0xRd(su`LF%(I( zi1f|JmbYZ#P(=3bREg|W@2yV9S5-cvdwO`;GrFh4V@0~B2KU`H!l&~i`i|nn*<@5t zr-v4)-kmfLlvF2A7Af9*p`V@)<}5dN7f7CFd+lDrYOmp8RQ%xPVL!G=0abN2RLJoW zba8T#{OR%a&6hm})8--fP8CSu9i_Tby2*xkZSeM|+d2yQyMND2$@uM{o(*d4SZ zp>SzeF18`lQvNOysAmqbe`p!ffqAB#y+q|ukshjL)u8ajNUI6iE6ks3i?mLaYK2S}HgE(J{ix(Q-}VyEiLGtfoS(-29VRcIAS46{UU;W&^j zC({iMOxYX=3)GOsEsEn@sxkr85^_H72B|OJJO+#smWXe8o%7$6wC*9Tw_yVL8={M` z0*#eCN8 zf0)g;<+liy#4>v;tUkbv{(J&ySCY*F``5jmx3mw#bvEAZE>u2!Q+1 z#nAh9QQ?HIJhk{gN!eOB*C6!q#b-JQXt2l?3>h!NZGnc6lXIuN%w0c(R!}JcYO5+f_`OBfFD@IOn&kv`Uf6 zaM2!JyqQ@zS3GE|^8so7flnBa6!VQveK(Cd>BX_?&fK*Qw(4+Wp5^g>914AEtvmIT zTm7vo(R!gsx)5|r4WW>L{Fz8$9}tLNg-6!8Prtd9K`hu9OPn1%=*C`F;_aJM|D{($?=#cK3Mr0G?~?=S zC9^ZxFs_q3Y_UVxvMOmYC+`Tw zve>kWaBR#S`{g)-r&dp8IB^3HYH}}|QK9fS;SXd3H1+4=gW%)LO+bZ<71jAE`UuxT z_!g!aI{m`KjU(N%e@%0(7o^*R7uhOX9|tTHKabncf5F4uiN{DxZgD&nZ7!U z8*wnB_OLzB1h%0nSjMv@9s9vBfuwMi4r=n_vy=CUl3~LrR)bp{$V$&XXT1^s;?)g) z3=C5oyq`^vjYx}U)iidlB($y>Us(50*pJ6K8M4v#zgAJf~=>SaN;(dp_1W=a~_kM7g4||atz_Ayq z6X@TOup{T3-?Gt<5p<;tA;Eae5&Os%&*Ij$*%iePxiEF7kky&%>`fnkCG@^c?vvk& z5#oh8f|L`cRx7sWBs?ZEt7=po+ohO#yFNiNMoJoKm28G@=R~#Ecb9%}544pemtmMx zMV#_NUka411TUJicuP+r^5=Sk`fA3rGKJn)HGKIMGLM1u?lGRv$;ABk8hhG^{+!R z!+vCox=oA-1ed`meysr{F%23*mNWB&))cwAH5eis}|dE4;h+3 zq-S&HWh8%+*;%9du{n(qcWU91#V1|?dsUh`W0H1)2TmT!;PzAqe2`%#0_{5n37Utu zFlRCrghnGuoZlIRFB_;);U+6)6N-8rBAIjp{xmq9AvXr_tR(o z*xMcFPE|~@$Mb*ewaxp0C%=oRX2}8~%*A5GouLvX7h~GncFqe>zl<(&kLB}9I2C6Qu;4V5+d^BHNOE5|J~0-A4;3G4EobpU?&pj1 z=mL?I#m%5!9p0kNpo2k|p4PP8Z)c2mODmI-@xp=!%eS-|+X1q=ZnFAyI=V*A+tyL* z?XgUZeWmAATREc((txNTFPI0piAh;_kP~RL=jLo^3yr@P!L?#sJ7Hn0Q$7i3u%sG$ zQ8-uPDRGibjUy22sj(4ssloSan%1JV9oJGX+&&itKD~|^72$wMYgt#wDRQ$NZE1{zL(|7 zsi`8HE=M_7R$h@Qt4~#ts0B^o{)$X#T~)=7(#o>ZG*^(5h{?!xmL0*?iCS@QIci5# zjYQ=NoIRH%rF<#w*??OlNFbl7tVvZ8^YPqriD-yqWmTnRWmzh!s;DZfAx@;MB3U6o zi$KWo5wh^3%~ZyE@wpq)eyJ~~D@bz}Y?vZxvo>-$Br7ndpY4mc*<>dXn~F1PQ-~C~ zP?4a2Pw1g3Lf}!biQOm+(=jgry6W8g96Z95&7}3bp`d?H+OD}X3hL##K+b*r#PLIsPB&4c`{?NI}?+4iE8{9WePsuT7_ z3)lq3jd0SW$7h^#7C{;N+%2IdsHb-E&?qV|q3_}5W^}j8Ph#x3Ia!1nD%|!$IELUF zFhJ5_H2E>I)M;sn>6o{wfH=Fa$*SuY{W!6zqk-l?qesArrC77~(vOMC1nK3baWW}9 zQIDJE5HkAPl?fEvu^3>-IBflkFn=tgD&=56;G4nX^sb8cMM`cA zlQ=A>_+qHizJIkJ$0{d{Oo1%_qj1{qJ^=Uw?=Q~rE{&80iz6q?7Rg)GKUv)FU{U#E zk^YPyl{isc$@{`3v+iFc(#op}`in%u!Y3Y5G&ZPzx>IU|4$b?e%-KoE2A)F2&y0vU zK-X%u1H)^cuC_;=liK%saABMYGIHJG+!truF48`V7n1y!PamtSN6V=hI3IeSFzMIc ztFWy%E@8v-B12clkQ3}RCs72I>4;1a?B+6Ua%0J?irAv_Fd5C;MlC@3?Mj-wJf5-CMNBJ% zp@Zlm3Ys_R6q;Ddr0+u(EzE|}7(6a4Yk|Z74;!*|zLuM9x7i(vx?eh+M($8#X7N7w z2#};k3XhCrAoJWP6rtGAft1#T7Rf9W+uWZe8h zkxZ%FxtCRHK|LRhjLZ&^T*0O%(ZFnxi@S;!5XL-uG`K>PY{q_Q=y`smRudF2UnF89 zfwogzKu0p}6JE}`aOo4{Nlo*A!uLmE}l^v#!8rept=in-*$F+fI&aPL5#?h{D zU*(>bdC#AlMRQSjc#9VS3YiU}cw(#k(Ssi3$(I4mlfvD;q!CW$hQ6A`EImSlB9XU| zYel(^3(J7hdzeG=87#bEU(|b7_50`j1R*H50E8Hk>|VHujIgExC{8H)0!>1|NT|oC z_O8dtBuJ17P!`Lpeh)7NvsF`)8w|C?_HAyAl!yx-x0%4TDQNq!MbvC5Y%tt&)Mv}l z#uOG4IZUSwm0p&wYw>_s5$w{> zHjRunjX@xkhR~B1v|G#2GLaEZ*c-*iuCS*P$*cWeUAEizUlRXY7zLs+MfwUy!=U26 z>(LRDh^B4beB*Mope{eXJmoKCr=D{0mCUZ~)DOc@+!T4mRY_^4g(*}!5df4Fj;@(E z1+!I>;AZ!g1yt#TP#1XIKip{fk|CASO=zS{EgdhW|s zlVqbzJ`&knMJ34IxylW-h)fOHN<1h^D>4nZLR6OJOLAoZewSsJld=-21XEGAoKzkJ zxMNyMl&4P;%U)Rl#9vFgp^DSlipt7NBMzfvuB^@y7++C|Z$=s^tF(qpmN<~MmLc=V z{*>9A!zVP|bsKrD%A)y_Utf}RyS~}(zxlM~(OU1Lv0rIvsrbkKh99Xn8&f#Ei4~j``PjDdu1nJ zB}tuTYWc!I-9gZl_Bf7aiF6jjqVd$9Q3!;Ut}!O4K!XDxgJ1BHkF!OtcSAGZ_qOAn zfi+;Hz)dl1cOxF^zv;QfWYC3owMKndqs4i=E*cJ2sd$|l9}eu6*>{X}WD}ZXmcu05 zBrAO6G-@ffpyFc7dGUKUmADcQx#G@PAM$R)$QbLq)+-e{%wmLwE%~dc!nEa!+_fIm zwrFg*gtHwne(sCOCHeHNMG|wqq${SS3z!##s?e0RvfSHhn?DqYf?9c`;+sYbVXq&F zh7xyJlp31I|FFvD3O+}6uv4PMW`gnU zrPPs6!yBSzHr}tYh9rA(kS%t@?ua)(8Av8PcLF~YwD|TYMC5pLJI>m{VNR}dslzKP zsxa?fFMd&V;Pql30?;G|0UQ0z(i>IONJBl3vCBYIi#-J3h}s{hElHyqp1%h#O!K&T zlb+a!MvVHk5=1J`>m06uUd(!OY@?|Q<{w=qLupCA zS=uzVXFa*xj*QjY$dLtD~QvsZIP$THih#3O$%`fAgO%_$$a*Ws|^Ov`nLV z@D+ZV;z1IohXbJp$K1rXFMv|5N)Bq(;$ea)uZg`+drem-F-+ zF)km|BfwjlEoI@fTYl=I-%_TJUl91ywTK7Lw6MiJ;`|#WVp1Lsh8~99Cr)1!bTU){ zc4J|JTUSZdWz&)aG99oQ7Yr&RR;ssUyx1h$*bI!-lax-ZFQLyDY)o1TpV`NgyJXv1 zFmSnEeMxO##amdWXZo0lLpSma<^#pyx&LzRqF=ryj!s{Tk}uN-E|`QC#!ZP`Q|E0a z4?Q^PK7XF}H)1nDMtBHlV>1Hon^!v78oDmY}!e&jn z?lMU@8#Hgr@w?E3*S^l=d8nCt)dHWEbW>c0Y~X4xUG#h1FZ0`$j)kQV(7dY;J=pE) zFJJVJwkcj~!F1qVHEPAd5?H^7NBNR6!km1@%Kg=I7ybV;p75osSvcax1~2;E2TMh= z@(Y@bcTz^n9=;lSU~x~C;+pbn3<`N#vn$ta2qZ3{iviG7%|@-NVUxFV=r9v8-T@DqCD$6QYbUC z@|NuZs5sQu3;TKQKvc7k*-;sKaK~*Ky6CS$hlgiYaUUaGQ5|uWd;872uy_H#2%0-x z*i!1<-QkOVXD(s&oenA5I?ks&IOl$!3#&UUN%a%M^QuW8RiZe0BEfsw7W65^r3aVX z3nLf(9`|qgZ70hg8wMNg32yS;kBwd=6)=HZ(7FXh7ahN?FY2`^duWZy!1J+?k0H@l zhu#p0YRPJ~-Ku7KOopFlO$gFw;ehV#5_tTRR!y80{xa^mgw9@@9Ul}4J!AvY}Iebt-i{v39zjfj=AVKBji2kbdwZ@*sJJ|1qi(h=Qy|K z0zdl{va-*hQ`u?ksUBt_o%Qf$aCkow2>PtNaEKK$!fTGiBN1SfFk?Nu9NP8Jwwf{v zdn-+hs~J7^0rx@?pl*$)UpUHpw)gULO3|^Ut8Dg^*~;j4Zt5aN@kn$k@J(8HQFSyR z=A&aZW!J(|JsCsKHGNz7yHD0}yc;x9oFVx{ZJ2jtbZ1P?=-GBdwWbFjYHz=<6|{=2 zUH951vnwGat_4G=S*P9TNmYC;&$X)io@`JRRazx`uy}*FpcvhUV{F-++95cc&@qD+ zTwvk8hk@&eM+Jl4zOiAsXvvZd9qMpbJz zmpA4rbJ?Zqs-G*ZNi`($wadwQM5?1~sx_I&trCJ*uCBQ;QF^NFa#{XLZ)sI&s*l9J zwaJ>~CK4m2J9n0*Hj^f?IoaHlE<2lhrE8Etz9wA%lFhM}?PNYor{KAW>syg2UEf$y z)0#+Usx~IGW#Yc}8~2qp?kkq*N7;~HxW+QgG)FCo;rVc{!k`}xhaT)wzx1e|^BwsC zK8&z5I#{#r75C&L=l!KPoQ}e9oaYR(5evSPn-7$T<(zBQbEnlgCxMfrcTR>L7^734 z*Y>hTa@-g`9JUAbxv%`pdB5R6-WK7l2Ch{r3O=p7j%b%TzJ{MM<5=w;#)7t3tYnuT z9u~hB?D9BJ%(!2F^Soc*P6*}g{KAWTU3YxF0*t%$z4$1!bm+VXxFpje+JGx} z>fvoPHeglaXmDSTCAc;Y%K^{}^o)aJ5haFPm{Jw+7(8wtgivn_8h-MD_yo_-ALQ1EQaJ1_tZ;uxp(%mGPOvW9+`T8W4?&_|KmAJHS^&z4`D2Ll^}n6tcd;g+6xPuUrjRqFkE~Z-HrObHKuVsRB-A zhMhbTdP9RBc)_i5AK)Q?s>4@}W4@-(?XaEvd2WI|5`*#NoKB}qi3PW2azb9v7cvJL zbI!fu`9?&ZXLa*|7_-BRMO4cU{Ic1+i%fh=L{1d~!z|5X;{Xc)+ zZ_8-wr}9b`U72Xv4{`RG>;1%ee@)GkO=@sS@Q_WPliF?i-5a_*4=vcy16ZH>|;kfqAzDR znBk7{Kui^7**MkZqL|phc*%>D_Co<>WfMnmD-@BRBRuNlTtJ^}KSZdUL0^vUo(@*mqXA%B zJrjD^?QZ-RcBipOvVcu%5so%rxotEOCquG&fVbLwCPMNatbc)hIix*!kw@Gp0CjQ4 z8e;HbEX`%W^c+za)VW{(>+^nZCzugTW!sXEu{@al&3ae9o!?C;Auw0LV88O;&ig&{ z@wg%rEm-TxZmwq$L?#M*d;TEK)cBm5rfPACHN?VZr*pQ{o;_DOhq4W>EB zUbmnLyCTUC`72orq7sb}y#zT1n_&JS$Pv;P z8b)E_I{x;&-@W7EJ)TakGu(jk!it?>`M;6nRdhR}aT2-43%wySHDbP4hdjNpn`{_k z?r*83z2t%Bn^%%w4|{~nuYy(~>n zj zAN{-Y{z*#}v(V~x{yj@$CCV|TaX}Sg)A(XIMliAYWG=K&<#BdXR;YNcZ+`#0zdC9Z zqSDQL^MYSlA|e6Nd$7!Xm*ef3!U8df2hd~qe;K>$s1Zf-Sg8QKd!&KdHg`W$C#Spf24(E=X)Z>0m`l$J; zhQ!ijJwX%gWVIw%qNv(ZRKennF!H{W4W27okRD=rR=- zq5c@@!sfw|Xv4}0@7E{TOYj2ECAUQb?@LQ~#CU}UW#TAjH6_EM1p7_IBNTk$uJ?uW zlWy~1SyB+_1|`Zxj)p8tO6e$vZ;kVF$Jbq!J2D$f#%FFN2 zU}uJ(g`)Bd?IqhTCwIM57ba2M`EpfBDz=T)30Z1N6Wl%_S+m@cMaT@d)sxTNms2(i z6x#CQY0y4YFxm!fyh-1`y{uOhJBiWY`!zJmQGwemgH02vSCHxeEvgbYE;GQ;o zyk~ELCD)rUA++^2B`>5nmkzWfehOz}iv})rb8?kRxnBD6q`U2ck4id4MOP8{l6Jkx zXNG!cf38BZO{Ev#DAku=_}heg&Mt(bkB9)WUAFQ7{?z-z6^P>z69h%n>IJ8!tbfk< zImVd8_vuTD?YNxCVXXBLqYiN;XyWUz zAY>R02*PJXRUk&eUWu0CS9TzN*}Z9SWR$8{K&O3eXtDM&Cq#_g-M2Zvt{16{W$RJ8I z^032#aOu`=es1V!u~^MOH{f(aw3bYs)QhY?F`O4T(UJ80o<$VXvKU`kumf5d6f<46NNxP27QQgVt<$tZ~~g! z7+85qdWy41Ep8$alZvO&2*HZ(zAt`%N*Bp;=AkBmjIWId0YUrYtieXgo#w|uu zCLvcMUrAzck86S;W^FTseINvbb!-imIull@!B-~_lxa%K?hoH-ggm# z@jmzp{Zm-Mv1|%kdx&tdOn1Om!nW0BYeo-tn>*+z| zUjqx-!w5^v%voOcHnx5F8kEj>D~m{VE}Pf;F^<+<#4|vyC?)Z-eUcCsrr;a!+$#x< zZ3?@1rc?yY!?xkNN&JO?gPKszK?Fic&>`1LMDK4|-E{Nby~m(NB`srD+%o2#W)CC= zJR9U^ivY35%RhnTIKOPFw@pP&uc?J?)Fj_~@@RpLE}x8Ir+wN46Rtl&R@7c-V~Puy zX59D-JQ9q@1Os08{^2tujE2$y?rk=XzcDK5n+-7$KqYs@Yj{41TlECLeM=Q;*(x(% zd6q}cxPhm|(hZJoDoI#Lj21BsHzX%pmYl8B(Pie!r!|glH$nh60S@$Dk%AVD@ScPB zcwh2En<0xF`X?>;w7*1;(7MVCwX|f`pKhVb4k4S<5n=07%v&h3ONodcXZ@(yaw2 z(ZyM1uaO=vu)Np1`QD`a_ghSZYZ~J{ruae!z_MNd_7j1Xjo!cfCiv(MN+?cS+6(Bw zie`Pgw)-s|y$XpjJLUboB6!!E{K)`?2z;-ra)H}J20UB5|Lao#ITOzyCIT5)D2Y!i zPiV0|qgi%h9L5|Lrrcqx?>Ntp6e?f&0_P57sT+6$n}lVHcgH*XX;!(OwA%9a@mKU2 zv2GF_Uq~+7{LPc@(B3e)4$6`dcGxxqMA4(G+;!;r3`Y=*pSAT+rtZisbVSalJ=~CqRS4AcZd<%jI4o4adhs)%(ipIgD0x z4nA_oV9A{pP=)wY@UhmEw|8aI{Sz{p-7x*6C63x|wF$Ns93k1gaJ;-_Oank4#;lz- zZvA~jXd^jYKOkYDv0!;MR~`X8%ZuS)e{~JDeF@JcWkqiT?&xrVm`nGN-+vR1>V@?7 zOp-|5J)ONZ@uhUSIh$BFlO^_+Tv{-Ysk)9>O+1&OJOLgQsT1*@TzYGsOc!-q3&}$B z+SYsumax4!RoGOOqmUvoyM^jZT_^tS*<5XLZ*Ff>M*=HsBk4uc)rEBWc$RtweUosq z_;!#gJf8kkuqn~vXII`rNN>l+*)?nI?*smQ%-<(#)@=AH`9~*><7_gHGn#>9ABjsr z_Ba3cRd;47I&f#<*^GqrvRV3?#6`~74t3(19NeQT^y|`Yoo{o9lg$I`K;{0)I}^{*QUc`d(p)r~mI1K!y$Uv>XEa87C) z*|78+dSkZfX|ebRynp*|C}X{Zr3SviqzP)|&EG;(1j0+}gJb^cZxc5joU#S|q^;uzb%)kV`~p(lMiG=l%;X^`FR? zxm1#2`7&@0f|jY_Y=ob?ZtS+a{}&e3TvRM0Bbs%5(@o+<{t3ms7U3NnRW0VLw3)N1 za8w3j6moEX6)Mn4L5hl_SxKtp?xOb7)49R%}n0bqN(F||!e)~_ZxmOpwD8PS7n5I!7zU0#%RcH(jcT?Yba%p@p${Z@B8mp-QGH%581bg+b?|M z%{4R+%ZI(p|G4U|bxK#f102-x3^P9HJ>aCeP_fo)Al=2y8c4|dIqq!Uv#d!N)si0F z0xmncIdz%iG3to{LBgAd+56+aB(Wtyzx1eEr@bN*t4D*W((CkR16P%1+;Va*5PiQLE!ZCVOjVXPk>$P_PsB%K==CkA zw?Ng)7rooTDfdXi6oFUeezM*B8do-X)1fK1aDY?_U{~W(H)yUOXq%ivOkNGb^{t_Y z5y)6Ayy0aT4U^BnRI;xE)ahb~OV}w1vKM~T4kK|W8M_daIj)g>&>b^v9ft_QIG>#6 z#?>};w(lT^OY{6pRa{PdrRus{y4z;*{yEw7wWHP*wTQ)mYL4#*!R`o|raTEGz0XFb z+{T*FYSn6gs4YrWwsPu&bH{#s#|NLE`SBWWdGa@$q+#H$#rMy5?v(aOlQzaQTQm|nCNJ%*`2S=CwW!2 zuDPl)<>K!7IdYD7teg!U^Ui&hjN?Z5(-3}T9N!G`PfFWVseizpy~Yge@ijWe8}^&U z`x1PyEcCGMd%REgPr8eHL#ntcrL(+$PGA{kZx~NC+A1`>JH^k#Xwct`YBTG52+4)V z`^pB?=d#yIr63XE6YRXj9=C`*8 zWF@zN@(kB!VitF()xw{}FlSa~hWaGbR5~s57O1+-r7aa_y7C21(rIy#m=`q(k36Atr2$Wk$i7MUT-@|p=t)@jf5ZhUm(M*W2|IhTm*!(8Z0-~_i0PZ3 z2Km|LjSgWlSVF5*Sv`{LKO{pxU|JS|YKyF9SVw~Pxu>lWf1@kaU$IBL^JXI{n6r8U z%f|ogysLYT_TrX`YS>f(1idHhe?!zJa(lif*p-%9|QSIqsC6dw+|AV-6~kuX3;_hKH?abvf!yk1+Y3r{6dU zZFo0M3}-y&AS#lhwqbnpKUv1xk@v!rprkH9jdMigK-QDaMW>B2iuq5}p z`q_`8(rq7nD4P-RC0uH1%nLGjjf8TV9f?ctgNCA0YA9RVI%7uO;^w1B$S;mu7IhqC z&iJ4;nh-Zio*qub3~i{!*+v`t5@V;`p$@gEE@n8M1;i0~($^hd^;+I;;|X+T$VhiK3*+Fg3g(NS$fe=PCXItwBz+30(z zI>D4)(=)pwvX;Ur##u1Dqyx+S-hVnd>Ari#_Iz2iDQ+5ps~o+BxOqdVh|Q_)hG}-w z!m%mCv4?DMdkkBSa`iz4!Zn&}C_0(NbAkTA@)mFQ%%uC%^-;WxDoICdno#(dG5VNy z;Vck19S7?C8&+3gP92x?bT(7LJR**pi(C2S!}x5m`yCNw5+&!2jd63grnNI7uYY_x z<>kb#3XFzBWJ#U(5@VA%LY2fAb??)Bob2WIN|pFdOVn39piEkle`*6OMo+^}xc4k& z%Xy=+@%MomkXvD3*+9lZ-?vS9M5^DoIj8m8YIN%z^~^atSZpEdKYC0q#&#gFamuyRh^@c&s*BMF2 zU6HC}F_5lJb=NhKH@%~pK$dKKBgsS4BveavCiC?NQw=%Ntkq{~^VzO=q-u96k*X`C z@|WvKul8h9E?Ix6raIYGm&_FMP5F(9BXx=Pb=lL~C&)@( zEZZD*$Q&`130vJM)>zY@CTtP6;EH{DR$-dPD2*4*_P0~A-q|1$S9y#h%F&}muQa|R z+u9=Yk5^B~+|vzxlU*d>W4!X1xA||*yLFw**Lk+8XoJ8K%OIpIe%JT-=IxCEM@Mh(iPvxRr@(C#PUfm7oK$Ytu;5BEF(B1 zHP<7HYbzd?QoAfJYS<(YxYUi_pU}Puh-D>jd;23WK*JRmiAyv*sjryViWgJJI~Ct! ziQC0i6NEQz&~Z{Eh&qgn>zTA9i6}leSIro4vGNVol*!>8U1}b%atNgxJTwCh0a(Nz z?H8x#KxF3S6d)7Gpc==LY_`%y9qz}mi9Up}v)q-%=GW?s^==vj^|Qbl^%HSB-zSIO|grf77lBj z7fMaKR|ts^&3Fr?cm`q`4=i_j_tKN@bMlEjBbtTamepl>8KU|P3KyZ~o8IZHa6`g3 zJ)FXNw0v7H-5BRLJt7#rWTWU1DtxcP?yZD4xv`F)rUkVouHD>X3S0>iYt8&TT zuEY|(qedOa_1j)?{Xy4Y>`hEa)C=Yr1vWZU43t^{y^Y0IsH;6~i`ik8o}kv@v@{Y& zWg}%myaJ}GbtXHVGPbhD1kkXgrVVB(QP_2(^r8HVt9wrsoDR-J6*RE5C^f=+Z%9HY zf;~*qhF;PW3ERT4D~0wO;7?&WXD|#(ihDoBIIG$>=vAE|+3uWNjvn75j+aS%nBLw*_zRvP-N|qwfWd)ezqAwtMj=Kw5t}@@T*Oe?v9#d(EPqi?RqUmS&{#WrFGt?n}KZa zFZpehU*@hBdR`*jXXXz3Q1lrVA&Cl!&Szff(O$vp1O4SyTFBK&!4Y5rsNiTeEdac|e*A3KcONz>yB$hP8+g9Dc z|ISdD>1mKxFw{;4P|02JzS=SA{y`xY^!;9?Ou1*T8uQw^SWs8?$d?>-y`?-*N>9w> z*tETvq;WPBfya~+9N`3tJ zNRCnslx$On@MADx|E?6W-`^)6%nEydnT@h6QE}W@?mgx(xkJ3NkJ#nxQncJRPXT$+ zT7qaK`>mbRoo&8(aVHnHha&e(6Tq-Vs+-|;3FbjHrs)sViK)I;jPQG(r5iOXCZKGa zF-f%};cf|N<(+EZMxidNNs+Os7+)YU171ZS5PWp-tx4L~c7*YntvBNimy<_thm6RU0xby={Z! zV$U=-D3NS|iZNBmLcF)PCslR&>BELY>08OfTyIrAnXRi!6z5Yt{WaO9)JQrznmnJ{ z-x1GNC$bF|ZzzAKoyG_y&H5C~94#7idR0^K3g0J^TVVzS1xb>(V!tS`<5E5Kdf7wg z-M zW%233oZ7ED$KkYiD)0M_op;v{WVAq{p;7*D-ylEI$%U5&Ol=9$&Y&Nf;5I%r!`|nQ zpLg5xCWe_Jp$m^Vz^2tZcJe%Ggo+;^I+m|+KJ0q|?)I*nI`1}0Z!ffMBoGCITx-k1 zQoU^ZM02r{$y`k+$5`G&&XSWPUIs~^aDA_#Q=hlo91Z}rZW zigA)7Sr%06cs*R-NY{^)71!^&-pJWzz2!iZJdLu&mAYs*26zG`Wz&re;Q%7<9>Y#p zE+3+gSn#>%Fo^~qnhjrWel>v=(a^aL!DqNHitYoNtBKqlF-G=QzzkpK#JM$jTmJod zceynx3w;$A*876_sv|k*p7oD-jUS(Pcc#LwkSW$5yqDH{Kg6}RU8|&hRIk}4s?K^C zgV+*|-uInVnJclb=_ugzyh6l}ct8IK=iN>PaEs?b_)oJ{4W9O;tuMp)yQnD$9`k*$ zPnrOe!;?$qMz{pI*-Bsc7MphY5w9@e=F&5c62Yu#2SUMGvKP*QxQ|)7s2p}G{f`S^ z;7P#Q8I7ISUgrHR}b zcAj92H*!JFMHUtXjP0DD@fI~#XtZc9Yi0>PE<83~*}>C+m3mIw?(oyx%+JH1LwXo! znW=U}D$Btn$r2=Ckf{Jh)WsBD7DyipdE z9t^7VAFmctyXOV}f_ZXEN4y&x4ACF&wKxg+wDtkY-W~Cfu0HN zO$St^KJ{4y^6q!T!ky|*AJDR$ zAA+%brdUvusk@-Z&@ern$rMZbbwWl5a6>um{rO))YL~LPV$<&3odndKYu}WZInhpG z8M2lna@kLv?W`>xNGB52)roi&UO1?ERC)%}TwlJJjc0~7D9wINs;!Xf?8w)Q*7Vml z)FvrfL*={rY<;>eb)A5~8${>j4s`cYS1;F8z*#3#-?@oia*3m~O_E22G%8h9$*M#` z0ekn1-$@w1vnI1IFanoTDI@L!!@X?8Wg2~s{uSAMm~@}4gsFofKNV5_$NJQElVa?! zKZuh(jtdHpV3uB}=;q2P?@#`69KmC`=cAwbt8w@D0gAxQzz^=8aL2CTd36g4AuR-a z0H7mR`IYxL-5exUI_Sl~oE5u8_(-vQm^*i+f-tb`guw{_JId_v` zpO(0a6j)mXcQ%9eBiMk^+q4|fY&YrA8cAwvov`=EkqI|_Am+a?$3-_7rN9mp2I13s z+F*`4ZS0Y?k>FPKun8p%Qz=dYkre{=*!yC1!tL|E#&6w{@Bg+MlYH7DgK#;P6o2O| z&yOn!y08+o9O`(M>%GQb9xsaJIjS!ynCfXYNQOz|W5g&uvX~QF(%r$>jfFce6DA$FTkq{nOt=g9G0~V>^?aE=WPQYW!SMIfF}ZcXu+Q12X~=Qi?t-MlY!{>VhkI^&z6ii}{6 zt9J$Yd!;?-@Q#d4xE*hk4vTapz`?4A@!?Q>HG3sE5zmu^074RE9D#x-8$>1>1XiGF zC07JZCj;+G6m5}5e`yOx>0ns#r?B9tU^O3Pq4=j06YlP?&%1iX^AqG04N|_K^n^)p zG9e=!wRm_7%0qBmU)m=A6{0 zo@Lcb%HZJCRmoXi>KyAj7`#KR98Q3WGx<=H0cqa*%S*gsoBvtmw|E#<4_{aNB!YgQ zpqIpLl%R6+H;Vy-# zMrJ$LP~mw$u*Fx*v|FvfRUEW46v9gX=uWXLh`B(eT3^>Et_xZNq}c8_B05*xMo#n_ zynf8bupviqZ_HZ1u?2@md5V-y3*#)4^st$AilH{igEAR?TfV z`I2t#Fyc8(xPbAHrcA^U*Bpb)3Fk?JRUh!ZSCRw*v6>Bbqes+R7ntrIH zSb?{NYZioG)@fT=NYAKpm@x1&JZ2#RC%u&~PPm7?-2cg` z@5IVzqT@h2deHloUzl*8EJYnD0gd_Hj1u3tbymX`Y^|>=_HAw5bfdq4_qvpi7|s`e8BOtA5AE}++=Tq z8TG^J0IGr@c1AIp&YM9)Am1KTW=hkEzu(CD6Pf34gBy`hE$hLB=UlLqClIQ@0paj#pXVXlo`k{a<6sdy!)$5rXIl8#^j)uFja#wdwqH`nSm9;PdSsS zi?6FrCP`SZj%0F)jVOl-op>`B@=vI-hf`8Kk&dT(J8G&r^4Z2*Jb7Rp`XH(i)x~ot zj#}Z7YSM{hB9-XcxC<{NV&Bp=$wW=(>G)NAle>~ftK*X?I4wCRryHnVRCFmfoM}iV z){}mY)N;kUmLA)9qqy-#(abC#bE5daYd6$4M+YbrYh^g0$WpHumK_XhRuftscJ?!% zabY#$B?njo0H*aIZ$A3rcQxn1D8l0lu{WCaQOgv3*H8c|f*n+=7LRLA=NXdN3u~8p z^p4~_%{$%*)$Ljt>=AeI-dpbR+@BvOiL1X~3_y1n;Wf9Uqakg9TRaYS1=pAllDcd) z{J%|y@ZB$zxzltJ+a=-MlC@*bM>X$-e1qP~UfPZZMb6v9!CNXN;QK4or??balB^OE z8GMgK!}!jZtJHV80)vYJ6O-wC%(OZzDmXF1&zWH8nMp2Xv<8G`TB=MQ*Cw!v>hr|u zi0M3}+xheSzMU6kW$)7Ln6B;)2A5`LA@60W?hXVax9>bwNgN_~INvPVJ>OyCp6~x~ z!1mRuZt5M{w5)F9+kCaU>%9(cRnj#)Bp` zveNiDYPN0{C-@ySss$LRY$7b%vWVe9=>1Y)Y?#9*CQCMmz8(WsD5vNrXBr7Q3l`(# zf8#Oy3z;bhkUoVBZd%iB9q$dHc4GP#>_oDqV!!+dPck3=@)rp!hoF?DG(1Qa^&83- zP&%f((c>h0zH5m%49IJ6y(gV!vGfr0Tyak@5tgz)jG{d_i#ErXaihXbfwz4S79csw zA5eN*Zzs#|9I=I#P2;&%vRGe%sf*~Q@S!jveOE^FoA5sKTjOrCA60R}`>IYFg!Rg@ zlotCf%;{V}I@wO#ExiZ7O#>8q_iiAv@q8o2-=sWR^)aF@HbTD9gKfUGyB~{oB>;vV z?}sT^uxR^~Jr`K3x;l(oUqHIZg%^t8GmqYrN?0^aq>~mI?`b?*mNs73v`0zP!4+ij{ccO+0-sXQk?(XpB`K=9G z%+ILztDLku%UvIR_Fs;>xquh=f4Ir6kO*AqhBI;2@;xfnZX_5;9H&?OsgIn(=e9Mw z;SZLdd^zfU{$Gu|gK{k`{=vBWG`L^x$TI7lgM7bV&1Y@jC^>~%>J)mCGp5b$7F9yK zDbB1UbaW75P>(F%@RENt?v8uE$M5h}cl({~czM%cPEkI_!?qF`Ch(fpj1BbyN5Q(P zR%zn#;YrvwY|-l7mo6d?9S3l&?crXUBTv_I|cQCHS(5LVSswiB#Lm6`E5WnS5P>dJ@T8b#FRHjfp1mGGZU01Yf4EkVxcr zbSC<-sbr*JNDw$wlRZ-Vsoe>b3Ey_EE|a-Jn?y1h--s(pI+5+HX{<@-KXuKI-)Ud- zL3Fvfai5XLnE8yX$qdB@NIbJJf7>Tge8i%mV+mz*A?2_;&xbg^OQ($Ne>gDi9-2@P zF>J$%nNyF&x|pM?%t0;WVS-#?u$nb%JCzz6pnnWNNx(A?4BcoH=Ox-STG2Bl11k@` zUm6^DtGYsAsej-JEu&A3*5LR(ezF#KH!e-vOK*6~xZ4ynjo?Gnq+XHpHd2(J69&Mv zjCU+nTyo3=YWDdBmA@#K#W9VAlDUXR5fQ6MI4d?qnOTjVwaAj&xRSS3m8-o{+9*s@}>z`|^%)cZ;*!`O#1A8h8IVu+nqr{Jd;7cDJli6x8R30#s#-GQ zR8in@GFCD7n5>hKB)y%~UA(Z*`<}l8U`&LfXmKomZN*<@lP?$5%J#iIn4tI!Xjf55 zEXhGV*&j?0qJ*7C5l>nIU0fS{6H0}jKcm$KS9&QUo%Oh&-=pnjl0L1 zq{tTgLZX6PU4PUYe!Tp!LWo~E_Y=1!yB*rH} zyIn_$6ck_qR}$(LM|t+kw%<;ZNJbSKO#;4RvsN(jSMN>y@VHy(b>Ti?m3=2W+uUqn zjra_)R6b*a=HiTZ`Ze4^*i2oc-fwV%mbT0L-Vev!Uz`%>MF)kz`%*(*K&1yfnKn>d z5tr_})bcj8FBWF&MoB^UEx)9(F?$uQ{gRMMHs=wVhahQzs)KMw41AmSXFodbuJ`)? zKC9tydWM52xxJT~#!v zU%AiC6L*~@@eKWL7_Wf~5R?2GggLl+WG1)bZh{qrLT> zj`xMaM_3@(JeC>zC_53=H73fkzH459?X%&#P@1CywLMcMp))J39jX&$4?_^#?EUdi zjl18KwheGk9aW?4@=pBBxZC02jK9LcHt*l@+tX`o8d*~5<)~4^aSL1EbaO2~kO8e$ zmv{01;2CfXie-V%IXLbNdX5zdAyHB9VoH`^!dt~Ep5>+s^39>3)YY5;XVi@b^YIH! zq`m2@?_EoF!Ax#_uKCj&YH>$RWU`s4coM{aQr*Y7M3H55`U)zve(GdQ$nn=Zuj z)Df7xq~t8AM8M?BalR&WAhgwzbYM83kr5BDK~Av>{{e?wyX6 z6QHGOnCnzfu`!(3qKp&U3fZ$z!QCz4-5b~jfYku6uEkLh0P`9SkGZ#M#1xlDxP0Gr zKy0{5qjkFK-8ni&vaL|$CTa?KFqkDqORzf>oK=xvvzxe~FyXc48)g_V9rDZ8ltpuk z8|6{SKB#0MIR=9RWrGJ7!MJrpguK5fa&R#gfM}fNh{`Fmv+PmpJ--Qy8dR%t+AKIM zUs2EPE`loXB(Zjn)n=Do>8w{cIcDiPxwY4Oz)AOrY36M>M}p21P>3L>x4?y#ZX?Kj5U%|wTrC!>HZ8PX?>B3ib?aC6~sLS2G{ z_>v1)9Z-kd)fG3-&FZ8b>Q$yLFUV{3C;!QqJABUa-J6zO{@7F~GG5-k`X+&<3k%e% zDqp4#DwR}@@-|Q>6ow%&(AF&Rf@f=GGVy-)x5nJgGZt?*aFGY^kdrGg8cjtrez5!3 zD+1ZtQB~=QZ+o)SQ7Rki!{EYjb&@VKisjn-(cd0(n+rztDh9(l(x$_s|H8i?BSdex zSntWsa{7D5MDF|3jSld{ZUqMP73{YMKVujA4q=BpDc{KpJ`H+^l~%E@qQ>uA+sPHHlKPP0UE;AQ#0;vU28kwY+#QlqY#cRfm`0U*N?koTTxU1xro2L0k*0azDpt;9(=cW zY;2&on|@xRcF>T<`Cx?tE${cft!dnSwPZu8%n^*qy*XxybVVx;4_&pDIAd%0z@Nrj zeih`>Gj3C}6KT9yHd&@SSeMIWbEkU~Z^!pksVrqf91VDKM|(U$3gC`Hx~V!9&Bhb) zNF8NV9>;+;6w|2Rlb=Jl?`r$1N-;o5y;DY0Bhb{QHL=Vs&}tp_iW46_|BF*@b8sv^ zFs-~wK0hs?_yjuV=jIH%k+W^CulgbKDb|O=552Z+ zqi$8qbjGerH0V!q-qCI;vG2g(u%=)ab09Bk@4dn#FLu&v+&=2=a7q`vOB}R%OZ;wH zicmGeL`e&uz3%gE;&={Ab{w(2Wa0Iu&D#@--beKGGiPW(ZBo;%#hr>#n@rde@net8 zE6fqFrcHLsh@jw>OyiwWU1H1fGh*LDY8VWh2G4c)VZRmbgw^NxfH0qZ{+Xw6F zIi6*Py??QL)UBriVkN!ejli-Pp|!>VjGK$$1I|$f!zEA!hrt>@xQ5DlDyU?VB}TD^ zz;cJzG&JfC5}yyQH5cfu-ko2GxP#u@{!urvBm8wyv?RB*ZEp0%eIa|Ol5h6in5g)- z&**y#)O8jvKJnn3yUQV?`}JRoxP2e}@{@D!UT3$Gz$za`u{0`)xPX5N`@Dj!s3eM* zFr;3#F#D^7_nw@#dc5y?=bXEnr1(5smd1txGE`4SO6h%d&OJc#H}$&R`y6Kj-kex55O>*xXq1+YFYS!0;uv1ukqS<(hIEjk^DVuu0i~_i77;f>CwvG5v*6nmUQ-?bS zgvH{ge8;ifs5b~OG*E|78x?NyBN2^i3>ygAh@2dVd+D;vJe!-*b>+o60?V4;JzbJG#|Pq6f8fCBFBfwlQTBP;bg$YEnx?Qpt8A zuvEOoZzaOGpv%1^!=6^g-6_pRZ+uv>+2$O3CThzjq7r|jIf~&=OQa+OrlJ-<8wvx_mZ^kIXxtQT_-YD9B0nQZ z_2Kl)_O#9Wq2D{_R$mD&EGpfP_V2k$JlJ}UyCZUxD|PDGW;ga6LE0CsEW^QbC*iBH zxGX;&k^*q#GoDF^#Y)WkpI<)bZreb*4Lp$WIKo$aMFjdG7Fa<2UF`Gdm&LmJ z4v8>laql;O|D1bqN&Y#0daq2ylg$rx=+uP0{MNO3vb|#^%~6Cam5CQ})wQ+Rnm9@0 z6Zhlo@j^1$lu6abbBB*n-1wWjbE(A1#L*q;V!WC9$Vqwgr}DV+XS0+#uCA)h#OvzX zQ@Ms*6`pGOhT(!6xtoxwwb}?oxMFI>XmoE1*ZYq?^{;;4xgSU&gU!G2eI82>y=`Cq zeW&Aq(mWaB-H5>(B<7o}c8Emma6@-|pZRA2H?}y9#^;VX(!3-|2X01qvX%~c3;*W# zoyH{}M~$xKv7tvy*~|fnsM9fX_cVXkow%~$${-bvF+JU~OeMv)_sYi5dx)Q76@>0< zK~*>-@W6qkCzn#1zNA@uhLIN3)89BcL{K$!LU zgC9FL+3!C`4B$`s)Cc&s(ymdRs zfx*rMmgl^8j(qI2tlCE;sputL;qW3NqddDLV_e$I4|N5(v(TP$LymGcu;m;_|y1f*A@=ZF~Rb>2ruKXwjzL&q4@ zjuq+WNA$h3=lJP&!eook?zKV1^*I@lJgQ$&aNa~T+*zBwT_-+v+Rt0UFmlf05{OX5 zW{TXH1C6nrEGFDRb;G2KE8gnLgvB(HF(7a~oD1qhTQr+!o=h`iDD@Czz{`$)>{K;T zmi4Az8oP7?99pbz4kjg6z>`1pj<PhAMY^g5s<6gT`f-*HM!@YYWD&wceqvM2;X*?BjHdeXs+UOTz~Yr z8#^i8>I>WE8$`*s$9Ev!`iQZ>%84w`1*2`@u<6wHm{Y(R?I~O^p{>U_IvgZZkUR@5 z0%EpCl7dBto!hK0KO(BIr-fv~rd0QJqsZn`G)${O65dxz4U{U9f~&+)_j$KxcDf7D zXN)wrMW3;fkMOdD$jFe{k()$e&k79`kF6%=!McI2Ry+7DZA_p2=pz_UyGhD%I7zWF z^fu4gRLIbC`xD(64&pF8FRv%x=l?{|Swi)Kbh!LZ9@G)tzAd^w6>?rIh+8n&7&7(V z2|c}Dr366oHv0uBRg35)Y~_f47XMZ}Vky>lNC$!T)_1v*CgepBEste{QXI5eS`b#b zF5JL(kVb$lZ^}=JjzJ~}*jnfP_Whmi+BV+~VThp4HS4b`!4}=xMrG?HuTZY!)_dQy z?FXE;55DP#|6|m<{wJs0ysWj0Z_1;W%e1y6x(W@M!tuee#)jI4uD)zf zrXzl-y1u@y5RYdQ4XK){-uiEO_fu;k7gDLlL~U|yJX4cN7M(r{Og3amV_j%W=i&#F z=`Ssxaf4s@Ab23qR%4W+*(gOU^A7v{Fwi>o(MNSt?mrHBg`O$5ZwJCRECIxg4<{L# zk4!AW2}ekHIbne-IQini<0o`AgLJ)jsCUZkIY{1bLffQ~lFP{pA(dk7alw1f264lH zEcB*Tm-iXk&5%_e0_$`9S83sTTl=Qmfw}>;=~V|qHAOqwC@eJXeFwMeK>N29-S@%T zDfiRxCcq>%$eZ5q`YD$b(wglv5@`Fp|H75ajXu!X#--jL>!#nhHgB)DdE=D(MZ!XS zXY@(Ew<{_+6@{Py7Vf+j5%g5I)(5=p15@sSDW58!r?rA?CyVX6y8|9ZnLkVpF<%F) zo$xLu3lCKSB5(2?4+v7UbU$O9G>JAmU9It9aC^8ad;Ap7Sc$e!gr* z()_gdAGoq(cO|m%wovyKhOl@<=+rcf?b0#al%xS!5H7*XUC@qp=GmIk)9hM)1`1vNV@Vqa&UI3+wYri({}&+?`h*e3CEj~KTB zeRo-QoYhE9=;qbvTH4nXCCDY#^$WwW)l0a8IsGBax$57$~TQnxu@_#L9Z{IbPUnrDmS>GYYJd?J~@);!XaZQR+kDUphGcE?+CRb-2;E(VgV@nlm~Lvtaw9TQ5t zuAeM!4at1Awyrgu-;htl#kc1S8@CuX4raC&%Xhp@2d7*T?hGg~Ct03uYIBLMfA70v%tg-aC8syB9S{B_SGV%E;NEm7I5UtJc>gjO!Rb60pfWyNur#s@S<8%98co z;3+m=)O8o1@a?nScXN95g7loGJnJys$4)o)NTa?f4;sJ7CccqOo9Q0NvsY2w8S|I~ zQOk);nxgR+df|GB85=^e+uqP908nSSh=}EVV(uU|snqd$JnjACvrr${1bWWs!8jTA zg!r`e6znXh)5xB3e#KlU_D~RS+D}qyNuS3|16L3aIcdnV8s+I z12#ojX$;p{*Y%QTPNrd?#@I2J5DFfX+=;hIfAZcgU&&_$?Y1}5a;M?3WK#Nq@(dU9 zCMaHom()O8P1I~s_jg2+C>)Cn@{FHXUU~u=>FwrsE!8rOrAHB0r5OBWF81Us%aU1P z)*D555usD^L}=r)ofPi4D4ZmwSke>B^^(sq$)HHeQd*i>P z$pTqE?#+ZHDzME&D~7ZbmY=nl&2hd+Z6)Qd=k{5>qdlCw?e$!nay$0PGL)@M*l@9z z#(9HtOSNS-V?D5*OmpTZ#I7<3ZD~|X@8_%H781(5e972=pka zvfgKJFuVKHhWWSh;LD=DBZ|)4{B%|f1MDmsG7q9RMit}>O`;ReBDgJ0KlZ+KQ(10( zH`8@~npth2z1l1{6XtoL^I_jR+q~pzNc%{jp=Q2p(%4>HHWy_M_X|4ZX$$TglqOKTTaz8&DQk2`JN=kCMh#f%I-a3fE= z9rNOsNZ^20pmdieJETBVjH9@xnE45|LL}!OV-Pb<04ee4ZIrH`k&H)i#J;4*lYZN0rbaFCRb?C}X+IuZ`rjykPTxgT&L`N!7NaA+V)R;_c9?gI$1Z9%BE@)y`87`C$pJ+O(DBsbCi1L+3I9-x~8!ym*00TUz6L= zlq0o&E>j!N#tT)Ms{bvL%hadQsaBDNKb^=YW3fa$(cGFy)MeW;%I4N(Tv;nz+2ERR z=7);`-w|ps22=J_AH#|bdO!FG+Q|F>BS*Ziax%E8*05=+^*tX4-HJyE&RDI_l@Rr8zL>nSi55aws%u0-HCm@SKKFNp`|>8c%_td0K>b zt2WU9j*$q?zKsoZN34G7gDKLFFSmRBoBz<+;r+AEO}YOwRJZp+Q{barpPzDn2L>{V zo#&>XplL6U-!;v&a7-tre)N1sXd|YHyc$?B7G`fJw>QBovX8aK3!Gw~V-8Py4_>o@ z^~Ns^{-HDQ(Vzdwl>0B>!QC0m@+xYz)qC;dAo-1{o}E>xU2XBL3hzSRsm(Wh=anSp zhfKbD1Ag#{R6J4rnLPxJ6*8aR^rb}#hP1`q;PRT}zmIMYF8^$WJv2ag-$L<2f#DekipIiCKl0B{DBZT*!Ifm1Fj!*u>~uix6CZ|Ao;61! zn;Zvyrd>aPiBL4E(k$V)g!%fnPMROtttJ1Ac~cvr@&e)bmMXGgg>R^s^d0|pmE*ud zTbKI+F*0QnCa;uHcBL*DN0`Q#2bHS4C`;6i`GS2Yq__>A4(uBE+t_KxZYM#>Wh_?| zJz1)Z2fw4((>biS#xh#Jy~OrB6tvmdsep^)h2KM_-NCu>zJKFLAbxuWiX!zbzE}DF!`+w&)mdGk4*^kWtT=kZ|ZA_WhP$L z?4Wjo>~ssW+^E4PC0HP31KDxkEPK*Pn0WKjCqMSU&OmsP??>vl)5A_=)wkLP*BEl5 zILYw#)#+#oqQQc9v2(q@HIRJpM0RUsOk+1#KmCFD!%BU|)d#NzBJhL8qJ0>KX|CNL zaM<#dkG|}vV5&WfudvnRv6CLq&-^3RFt^j)PW;J3a|Dzi{^63~ygLw=llHt{vcZ~7 zI_{lmO%U+2D=Yg0Q-X>p7K@Y8E{qvqPQbv!n-Fa)eLD_33J{=7w%Y8^}tT>wXC z13%i=2UBFYAkZ_JBIm_YzL3dOVR}qfQ^hczPzVYXHC2dLWpcS}b%ATCOo7y>3R3yD z&Y!Mq*7r}WSra_Bx>=<Tpys zRW^ps&VWm~Nlvu>>u~NxiEYgn97?}qwD8Y*6#rH^UUcw8T*TU}!ShtB8+n5UbYAsl z&+99XR=wHtA*fb9dNi7-|HQu6w&y8_0Jzm%u1+2WqO(NVSP@ox%OLxNh1P6k;594z zUQI6qB4px47k4y0o|yefe=On$`RItYin{@xu5x9L<5kJ=7qQIh`Mp< zJXVo{9zS8KAbaIOCx{BM(snN8kgh=|H0lL&ELBj4&LMN^!ogrL+zbugVG_&lD-#8Z^O0_}(c z&lIYNu7kbE<`4psac~rocsN8*JOgL+G=2^g;L2CgI?Me6-VpfPB{G@M)PA9Yv%X_+ z%^K(5IRk7x2_W#pHx`ye*L9X801E8y=Yg;*Imb0lM0XE;0-fo6zrmr7qK3^Rt8}a< zrhJv%(5+Q=L&pbJ5tmNzJYu$j@bbhEC8SPrZZKuKwb5{tj#|ZN+`q3`W0rMg%Nq=% z*LBtflF*_GA0d1~oBxH4&{GXbsj)r`8efojgKczcn9%XrImNPC|9gB~qdVC^`1ZYp z8}=ZlgKszp-TX!l!he=3K>8%c6{!O?NF`@|7M$=Z3!z81`7A^*E~L>2!T|pD5UH1` z1XlUZPqGhssNM-L_?}YMWh#K{9w})mpBxxb-i8l@d0~obG7E$ps>!h>_2?$U5_$tg zz`g-X=x$HcSrR(eaZ4cXYc$NXYnOI9xYNmNz;?JA)qEog&?Tszj{$Vj{s|5N?}ESy zwu8TOb@$*WwyMti*n~@;p!>RZsF+GlF$(|Wxmo4yFXFW)ksyrkVo9)G1C^LCI4I7LcIBZb(TK+>K7|p=Y#jwtO@;HcVP2C@k6O{o+CkW#2|~iocPVV z^9#=iSrpmST>#&9j*hF$Nzsyh*}Vy0yXQaK;>hvt!ziY5YA4skGjWo1wNt(gmE*k^ zz=pkHpRow)>}@BpxQMW0>>m>m1v%y^JSW)GeTuu8$Euy&bz=C#nG+n)U_HSW6Fj0f z()eAoMt&Ft->z$|TU*yJ6N3u`{*=_n?>I!@ z6XwQ51~ockWg*X`YEF2LkhSv zzksmb!b10N!$J_D@R=n_vPT~~$pr+BuS*|lm)u!g6A0a6Jo-|msMsBMk}97!fBOk< zwaX0hb|5x`ZmPmdYuMRu;7~OGLMbAdt22m9fZGn`aVwK}!N(bTOY_M~l&u9NRX%GP z95RD-sq*N?w4y9+)Tf*Xo*FZYl5Ol8tC$^OAv@WPo??M)hI~Imst<$-{Za(BJ^G%6 zR68Q?*TTJL%1LUc7hz`fCY(LCQ)0YsdqggfrswBsTKH!0VvNz!vHA_O2524aJDBFN z%RUhC_}bRG>YBQCM-GsO z{7#A#!n?IPS^b9mqE$kEgW>IMu^l+*OJQOCRXgGN+l&@LL*Kk;*f5Ida;{@%sL4l& zup)-vZ0-;G+_D-!2`<6JFhTy~EbuU3b_>lbIP*ksuN*?)S$*?Kut8ZaW{EZmJH!)Ta#=W_KH|k6AH0m6o z{t@EzDwt(HfpfVHzGd>UTWCYky2gp(=#5X*>f;Y;^DP&N7X6v%mdBPE>AqJm>gJ~vLg{T)Nhe0Nh zPvxqVmIo3c&1xc-%Owh#CF+aC`I|^JCXp8LO8w54zfd6v-~W8gn($|gmx_RL8fspo zoCI)6!BA;1m@sMn`kcfqqKSbEOdG&WMBh3RGqsbrW}O#zyP>D%qiK(1jkD6jZ?kXo zOda#po{Cl1W>W3#gu2TdWle9hev1#O1gBO!aK#rOHJ$^JBy0i8qw7?Q6xP?6Br67+ zI6HR(tFXgep9xUO9xhqS7|+lZpuNUw1dv9ZR@T zJO?Y-$A(wsXD{*xzty=%mSkHsLCG47Cza1S;yBZlKG~5{*l6tiP-xK*9Y28UyiL{| z0e~KEWNGImM{70B#jx`Hy+CkoW=1`DUy4Ub+eJzlIrCXB18+d_;U{Q``j7agQ)@M> z+$xfr{D-QHj;PVRuSwIP8wkBUeP0;JhI82PupJ&l$41g3Lx!|mf@6)rJcGgSkm=fQ zzJsL4GlF?OWh9BDWbc9jM97xJt~YEjHVZPb`i_xRN)v&7Bu{EO980AAwE$b}Uf0l) z!d3mvivx2=e{+wQ2nI0XV}skwG~T=QX6F_q$xF4W7anyey?qbu|0=K@4TR?_m`V51 z>pb&YK4RTh7ox-0?nTgO1){0r5jLrwr~PKg!tLoL;rYrUF02afHkJ^2v&UbjM|uRc z*5b4TVV#KMBJSOvNUix!5qR=WQ`l#a3k= zrvgDyJpa+jjtVix8=`XmI=GZ z4LzEjQDRt(Lxcjm-tgZ(b@*uzjws8?rdKj(aSs|K`7o`fY2pL?oQvo51@NbE*8CT-zaf$jc)R|~HFvA` z?fmvRD=)moua4jkh7BK7h3j@O@IJ2~ceuHN9^(+OQYf<0iz}Bp?vqn`F-f}_O|hQe zlQPQh(U=@#koXoXRh8)AF0l`0msDqaD~Ti2)AC96Ga`2*ukowb+!i9Y`4VESWf>*v z!gtRZXYg@Edy53C?sG4|=*uJC(?7cAZa;ug z2`W`SM5|3l+yK4?vOLoIv^Wq8X}D_D(B+{sYb+$uvk4|HsnE9r-uACub4Q{$4a9{HIKZf)$N%)2yR)9; zF6InBAY$o|!%4%UNxzr*i)(I;v%JH5%)t(%ZQnPjN2A;#cd|3`C$I`r-iiPBn%lp{ ziM+V!ZwTvxki~`BIZ|2US*$LJT0`39SUn&j0M4YY-tw+f{XttvuiE0R|Ep{6(vqXB zn@4!UvM^X(>f*p-o^oXDrng<(n-ZM7LU#?uT1}yN-wofLzK<=+-v*P|hB3p+=dajd zXcgZY<^2k=9$FDRjXHFbP*#4~y#Qft*jo%-cP}Okeyno$xc6hub$1>0Zx_v!T$Y!F zW8kurqd6pX;!$qGiWc+Pb{}layW?nFcXqg``2}w-c-=kOP9hUfHJej*`B>bg6Yaf45lkD;uxZ2Kck-tVQayG?s6 z``x6!SGp^H16SFKN&c>w&3wo}FtSIUIZx&8Jnc9)*%s%#AIV;Khr3|;rty1t!Mj=U z)69U1aqHWcHnHCqwb<$^;m(33EZ#Zcpk2A@R4l&3^CmJYD*Qh9SasS3_ z(WR!&A(UUtu3FqMkOCs0-+SJf5@)pb?bi?w7yvy?gPcfSpXI1c@Us<2yjOgEpF`{)RHl7Yd@Z-l9NxsnX80X$b6rIc zycS+K6_)^f0nLv5-(F8~awHVkcenUjXtU@VHL%N+Zo@!xrl()Ik(p`l%fI@u z({aL05O;7}j+fdG_WpsCo@fXL;piEuyxmj5_-%z%`%%%a@2bIY(8U&5d@YY+Qa>$t z)4%?)Lon836b%oHuWxf1y~Y#Ncs5VX=pr8iR%SeYJ*ysSltJ`G@%0={rzz%aUp>vq zjN_7)ilK9CRc>C(bF4#7zW&4x0bc}H3u|9>+!tukUXO4ke%19({3f3@CN%U~Zab%C zJ}w^5>UlzKKr?KDA3h@y2tH8QGK-6fK7HOa@>@~+6kp37<*L@JuUC%`IN`hA`rrQ8 zSvMR*ol4dDd)UZc57VGq{A4jBV)qPH6I266%@zc<0U-wPQG-5Pu+8D;UlfT zH7TeV!Rr&==eb{V2|nI;?0UVZ!ZR@{(11gX1$q58eK-F9oV^KjUg=rqY2Ev6`u0!z zVlCEgd6W0DEiaNS@A7V!%eB~_C0Uj&$u7zAT4nKNCoBncz)2iI|N)zry2+$VGEEZGr#|HuWVPPiaBRobw1toz3=+G&-#Cu_v~*A z7gYK>IcBNHZ6r1<)3s_pS0t#hcy(st4nM`IVrk(FFYa~wKk=s5&WzSmNS{>sKGJg2 zo^(U&I_a1eE~)Msw?_SRi(y+MY`=v8cjl+x^sW)Y2-bdS;XF6WZHE`^h)G?koy~i5pBs zx!j+wbd8^S)2nYeukzZ2*lsHVAV=oZtS;^W1pk`*B2P7D;QFnbG^ShJx=+999jy$mI80D4yHUYOQ*koalbH0Wa zLpExgJ-d^vf3$o=a?WQ1JaJQHEj4yOjYviRTXT z*0gLB2sL)2ROb6LR+}SOAxM* zrx%V>K3;Poi|{22dsV=?NCJ`s;lN-LW~EC=au7ES_mRF-Z&4i`nPJkT9)5X5g29!yh?O{v!>rd1~Yh4T+qUV5WtGwr9D@QEH`A+3U~Rwc4|jaGthOT95jxb0YjvF%s3smh_-yw$KmDx;H9exP8`nhy!V=mK#-!g2R{Hu1R(v_LirDRGTSgD$ZbS_n!$+Ys7 z9D4awwlPzet^hBun$imOS!!_yOo-HS9JBanx_W(m?aIu)RLx$%`l<_sT3xKf(IH(Z zZRkj&yg;+jj0(T1I+;#>>Dzc+<{v~Z+-u!uTwu=h7E5v`vwgF37Zq$dE_h?QVT7i? z8pSbIJPWQ>`1}%*VzJ@D-i*7bj3X}dTn11#&5+1ZdB0=fvw0zDth7CXFFt#+c(Icd z(ibgPTvuQ#4JKxrA0HVR8XT%$!wR2!EAoqXcm zw=l{B2bCa3M9Zz)nE?SC0a>$Ekw;t7lC-SncQA=X1&wLg;Xc`#@!R)C@NBfq2S)sW zF-4Vxs6xM)dI!&@TSZV)7p&(AB$KmfaPqtdWZT7S;&}yIknuZL`pIc*5<*f@4;ot# zrNGMu7hpToDErP09EKNmyVV^TfAbokHt=VGLaMpG>Z)O?)mdjsM6f?*ZBC(!6MwX- zGvhBi?%}shAtF|L1N3m)L|2Hi4aWT9-0gr(+muv*xQ)Re#BL(scwZD=AuCZ^@FtrP zS@&mM8NatO1@k#uoI(qG8S15#`ieW!o$;GMPDjCP{PJz2T-t10KVfk&vvyePzSooS zS5vhyRm})pL~?o$bMf-@gfWprYFE~1>MENIB10W(bahXR=$32awoY`lOAH}>amW3) z+-H%{EY`$E6pe$Ga5olUk5^aEwBoA>ld>L9jo zrbw!>fXPW11FD&km9n5iKV5yOxpf zd);+x)HsP)zb_XP9kj6IxzCS%-}~X`g@$q6c1)8Fwg#K?MLtn0{td|NAhpAS^i`(_ z)v*q?Ce*|BjnR3cQ#;ancn$dS(wIXZdM3W_H7^5$n69!~F2Rdi-U0z{8aH(n0?j{O z`M$Ta4^l0)g~@s3O5z}v>nNmf(-W9$^5>O9u)cynL`a)m)Ko&Niplu1c4xF+pc5y3^UcnOyoy`D4TZ z#LAYeU9x1YEBw*CSJx5fDHH?nzu*6G|6f78aqpjN@rPG2y;@DC;-n;V1(?t_54>8F%_{*6+UJO+j|V zowtkBOp_R6TA+dpcQrJL2(CEh5pLAzBt}1p0NU10i{tCPNSZ>N#-wmxxW`psp`f1^ z#d(Tby+YmtZH3Z!47%Krtdbf?Si8@&2c%`TBju+s%CcMaFe=%m&#wTQD_ z=6H^>rFa3Q{HAi)1~tXD0s$Q0`abC)dwcn*fcLbW#<;;M*$}5o%Wa2yHAvuO{k7K! z-Ws1bYJKna;$+La^y7@b^q@D+2em66m1Fc}Ne3c;&qur~bhucqb7(@eB~4N1+gYtP zMwg}?;|OGEUO%SR)VQ}O5G^K#bLu*%YaMWFd~lE_?`W+yfNqTqmzP!WsQcWT82~^1 zTW-%EXZ+S=fK^`MF{s`DcgEj=lSpE2E0l1P^)Ni02`w#Vh5xs90*? z0xcbsjfgsR8_;9g4Q;jUv)u;i{mNY?g^7a%(2$!cI9?l3e5m!P27uu1vMIOh8?NQnk-lLS zXz7fG6oy_fum|1cKV{&^)GhP)!kGICrys4B&3EAt3+SbmRD=2h0Pdpu=%2wIjXPAqtXLUH`W-{?YlU#R7%Bb<`HRHu#hgaJ5j|QD>D3-)^PuR6Dx>(3zu)?RFJFn|q%uyPtWoEG8iN}N`v!>|@Lb&G4>o$=2k zW6_bB;w1)mxBFEtbh)qdTYo~?Dp@!Z^e#qXxMH9eWdi7%hmBN=hz`N?Vv|@H;#gq3 z!l|~Is6BH`>r%aTFoM;yIO%?I55>;|%^(K>)64EE<8}*{Me)-!l)Y*eJu*F{t$2CN za;d7fyBWXaUVy@}_iwRud1(mH%!O4^3LOPp>SCdvma( z(xyzAUCMT?^`aiVmH^kZF<13yHiG*@aoRn9AmiuHOE%j2 zOiBPR0=c0;IwVC17-uK;s|n>MeP(^bX`N|Ktr44D&!LRpvd4=O5v66I(q77`qfy@9 zkmY*eE+_ZlFeIE?71;Lhv=Ak=8Jf_BvZ9Tj`WT=!0h_4M$(Y<%lyy~ffrkF*$ahCbys@$Eb5b%e2%05RZE*vjTifp1bZaYN=GP7OQEtpUsav1 zNht~~r?^r=z6tHfd8llv7%R`g$M2-f zeP>VBZ#yjX0CNvjw>Fp4X)V1vd?A6(nCDXJ#x;1^O@zzOl+Q z_w(*G7}({2;)NWe-Rsg^!p*9zY&XgUG6)U{xC2%z!vpvd6 zfW^YkN)-H*zVj%_Q3vyubaIbOz%U;MyPUzVbRKwR+=6WP$UegkS>cBQCghRoGp}lt z2&~2PMy0QKr(11Q_{kKN5%H{F8kI8{tJoZ3&Bt~D809iRB&0i8-=K!}c}cY0rA-CR z@N}T2OvdozpEp%gnTfUQ5eVg*{Jv}WtgzZqAQ)4Hj3dqI1u&yyNf5Kv=_UD7FZDo zHirq4y`$j93HBpvnp5d5uV~24k04ukCwMuDcfv&^|fW z*!Q|3Ih?{RIO<6(h?ZX6yN9s7-Pg@`pZMqfe!p#&^RD5S&|08h$7RH(${kI$HTw7^ zNHjjZL3PmNo1)>7rVbfN%;k;43z~l~+az6rsym$jEl(rkbbk+f44fH6d$GSan{7^0 z)6=Ki+DqT}s@>6#f5wZta~vm;EJG!OHTaeAi|U!U?GLqYceP8HW6pMuY9Gg8C*J?|DC?q9AFk!?->uR|DwY@_ilP=w)q*eCflSpvepzBjvsl!p1++KyBC$)s+)>(1cZisnBQ`7-%!-daS3Wu!xcO zM#uAImGWgBC2mg3NQQZDLwWQXy93il^Jya&F*2D&*MU!>Ni&*HU zy>6zZRr=&kO@gIKNixldf4reNvQ<{BFswnMPSunKqI_*B^K=b$(L!0;i74u)3Z!DKPCBvohcp*|%iucr`j$2cYQK^trcBMiE8J4mg8B#lBuqxGN zTZnV56?>H_5XhIw7f{nBbEKObNY+(k29$OwQ*k{Dew|De#C znw|gH%U=-}g>ugASh6He%>TN+b!&q@K`34q93exj501toWg9r61C*t1V|dt!lS_CQ zWp?8MC{>Mh>{%~LJlP%Hrc=lY!%(EXC~Ob@ND2bfKngYY7jn<0xu1d-xsz1#p|e zz0_ICzZw=({?6!QDo&_Ke0)syht_Zpr0>pKG$OGMK>}FW2{Se$67U89qu8-m{K8i@B&!{&EaweJ(v$MTA zTqZ;Z#opUZIbK{@oJCo*sFDip!C988Ra|9M2^mwcZ+xF_^3+Yn>%lqUHX|Lcy|l&m zaO1GU*Zep$Z2}+L;G7Wt#X3Zu1{y;d#5Is0r-*y*y^APtURZf|~?^d67E+^8}^7 zOoXPXPmAHoo}$b2MUnRg#g~TldfoHxs4bdIO+nO4T2Y$u+{WInT#^YPyIVMQM#{*Y za06YE#crwVMztakOo_u1S*T7-7!7G65J-V!t&cO%gq%E)Q=gSi@v;iPh=hrC^QjOhnacn&to5K? z%)O^D^LAMThA$kPE*knaHkwKBHa=K6W`f=&wDlQ2vwWIfRPx!eOwfA)hnRN1As4{; zGC-f7;pyJSgE0n+43#RLKKl+P!eTjXx-^zY@Bt<`C7(^8OhHMKOQZM5CkVR4r01-gOkfVzi-`o&Y1XXE<`HDny$7du)n%WM#37X>Zak zlvd;TH7ve=IYbZ8tvidj8_ZOlgH8ptn17V2L8sr5Sc$>0ybDnku~!(2LD3-AgjLy! zmC$yyVuX&aLL0;O&%$pYjGLIETf3O*a$dIQ z?w9$a+WM_3hv8q?yyq8hE(bJ>OyJkU573Syr@bVor3A&AP0@H4K+kj9Lxo}GTnV0@G{d`1n?EQ)LI6qSgc_$)KzaYc*83X!sE+2 z_-J0w-GwQ#(Abpp_B|fKq~ln`MAP+ntVC48gd8s9f5bH&+H28rc3jUPxj1ImdpU&rb~@%kVNG|Ypv@B!9cOl zM18g?4B1QtA)5*ewuhDw>dBTwc(k-CdNS|FaLs!%5y%rHIg@*Qc;g89!(oX4rJ^U2 z+WJ(*u;OeP=&>-^Bq|GT&-qCq=g6cfF;H*dMr-?+j*A}IzNcsJOcE!qNoV7~!z0f4 zuGNW0UV)q2cCpH>U8~xurCENpa!oUsjbC&K%O));QGKlY~{)&Y$x^Xs=+qO zxq54>kRdsYOQTj!ywCiI1-S>0H?ZIc44*^dUu+JHjSUH-mQ8M_uaP3dvLa=;gJ}2E zXRkmL!%dRY5b()9nRudk)@e)c+w{%e^Vk$H>IJn!sVWo$Sh%OE&39_|7SW!9AW#)~ z@?_xG8kCU@hRl5tWmqkcm(QrWeo%E~C`1yxas23DWx-58C5*({^+ z9(n?QMnXa=#_p!PQKQf30V3?L0-a*dP3J4|lu5A-S7a0UN<2ETT~t;gkt43lR3gm6 zY-L4`WXV++D6pF3a)q1_s`wu)e+2!?bX68y1-9oD7(8+_C03|1UzKUfRHy`?c{19? zvl8Ne`og`A=gc7{6On&RA{QlLLOd{m4#xZ70G0M8FaaWgT^h%9d4S#~>T1G$ry=Vf z=u<9T^IIV(1U;w4SK^y@ogK(*bK9lYL36`XhdFxP{cdB{@7YpDu_|d5N*8V&;qX=) z-S|Sb5b@0);0l+}o*II?3h1$Ypq5|*KA;s=2%lfStY}rG@?%5iP1V*XddUZvNEBaX>))|@2Jhmd(dX4qGF8er;K+#{H1&U_Sax^pS!Wq;5Pc?^^Yy{D5R zxOav=8!}ZlMxw&hqfnjg(AW~5Yq2R~?r274Jh&@uPYVF*V{NZ6YZMb*6Y~XiJ|FzB zOunb1SPF~5slK;5#CTq~&x@%Nem3KnV{K6o&1mrfT5(4SPQE6$OtV7+0AY?zx|3<= zrw28thC=?5_=#y^*kPCZp})i*)xE**`sZ-KFlPV@OEss6R+I{pmv~yvn|o35(nNV; zU?>t%3>=-vl=s(oHMs$P`(Czk>w|$lq0g()KL@rOuyLnty^L=e}YWe_A zw#PN~io#j1sfBSTqxix}PR?al$b}OK`+M%+|BW1$uq@&4!R!$_@^dJ4@yVFbw}@cn zB}KCB)fB|*nBSLInhw}pK!Eflj%$(!Y9)v+47k4UX8il^Fa9p$*LnVkJNoxHAOYh! zZq4Jl3gUqgim&mSTm&2G1ZLtv4h!zwKj8A_Elj&#;Gh?rQa)}yxXFEoD>d`1T7tHC z{tVBr3?gt2s$$?-Kmt_?VIk&H!r{SQes)FiZVy}y@Nu~a0~7eFl#WIsXlE!(zHXpp zPvP!h0#V)iV4GYFW;533*%3 zV5_8c@}#^SIKD6L5GyhGXad>FaX+&+>$iYxfgQ^RYQ1zs?pyo#K$^@3tT1z7NxH86 zS-%VPfN*dDsvfZgsQs|6O5cshkXE1MryVL|_WdB@D`N)!eXbS*|MqzVZ-nzSt`I4p zuagCwAkqhyrsWcmOxGc_R~3?3^0MVYvahQ^2cOH<=US7Q>QmLJWOY3bwjD%&bmy{! zf&fNA&gfKi_B!smm1%ekl=sN{1xm+9H;YjqoyvSMJes2m#euq7A;(&;KZdUL{qdf%(rmUY>lW%YT$qWE+zo*M;Hi+<@} z9kY1i3-_9j7!#5b&}4MI#Fpkh?ZA^?%Ea6YEoxH!e(vQj7Y{pzbz5*-PQ($ z&eR0NdYHqF?xQ~(_s^Y-)AQqF7<`Nty@2|L$ZD&s8gv~_ZhBS`_zM?QL3+VMWVUC$ zi16HPmTAKwS-b&%FC2Aye&*R{x(D=RFY&UL7`{av)tDs`XtQSe!YA(iib+!eXa8ufc zg@f8$2Wd7BTI^*bn>=G{AvZ{aXgBz(rbKg$Sab!JBP}kR<*j9P{50DTuJcJ+=8k*Y z$u^R{=5EHe`@;oe+&$$D3V8U8`wOmj?zYjmZ`SW^R$2QN+piv^$d)HqeddSO(wRhk z7THRuWf?IOWiR0=>sBSU``xuRedS+Q0+sAr7jUXStI30H0x&&W3WDPX7y&(vkoPwJ;Ul-5DydnWVnwT@uh{iYYbA$Wz zfF(CZr%j4ICesBTdR6{J#;59UouD%7 z*dez*N0+@IsmU01OR-?i^81-R@@zFGW|@skDgqJ;V7=l^RmE1zroG4-bfC;a*&ld| z_u^m84BqGd^|GwrJFo6N6u@JccdVgd+=VP@W29ZLalZx@$`pv^c7GdAU6fegNgIhY z<~RfU62uap=LU=&9U&?j5FE|o^ZoRRFxPBRu+XW7`*ugxkI&x<#(IqBFUdZN*3iNa zI3FTJ8GbmJYDL=&MZMAj8Q32|CmKL%8U1{XK%^kZNu<6})bv0ErPqiFAICTy19j05 z(8Wp^^@4Ajtu;Do-CQ56RZY?rx80w0XPGn+2t1EZxwAc4zpoQlY2kVWOKt}glFHed z-M$PSDpIi}mFS2$Vk-TE?*063CrKLmE%A@_y;*<#d`y)_Pr7i28r25wvc{gh$R=Uw zd`vJNtl{>tFrv@adQV*G69QhNEm9uBiK#9Utg_6UvN>_^8PimBTKY*NZI?+(X7P>c zdnWWr*hArs5jpaam05q!s0qF*WO*#M*rQ^9ZbSlCF_SvCh_Xk_$wjG#i4Nuh^-;_Q zNGDUk8M7$0L+=f1J;8CgLO2-eAy>9K>sNON5?xJ$XhV!BlxgdH4bF9mOD~YHNpsKr zPdt4PoHNT6V^fy9(A!1KMsunI*6T*W8u6b<}xzmr~KW<D%sMT8pOVp&n(Xl zbfqhJkKswi z>9$mEIGJmq3N=-g)yei;zK|}YtGa9Ia_HVvE|@tv{D!lc70E)|`Y(Ou3HLg0+-oY} zUUS3HW+qZg$;-i_ILY!1yrF1Tys!E2Fn^iD`z=8JCf(mFBYNVj}byy*ov zQnX9_471EcoT*hT^HOmh`IYO}@A+c#tOS*dbhv-WfKasXl}|7#wYzD`UxPvv(FQhUzaEV@r~r@fFi1)X+~9uZ4k{Rgi1LIbw@8_Tx3*ZBLuL&MnK zxZU4cmr%04g*`mpr4Bn4?iah=|IY0_^WcqQ*)&N^f)6ZTas&g8Qs`**s)=x6sAMTb zLl5#U6I@JgyX5Gznn){S`1Zl~@W^#eHyB%Wg`;Y`x6RaJVU-)Pwwd+GBIPj&f_@!a zxW#kR?&q7f`~6S!6kq;7ANTuT^)>^|!Nc z{hzPHk~cGUMQSEdZS>-S{FQKj^sRn>DFI}m)E09)zTNMyK`H7!#{uEv-|6@FloNPh z(`T>yJZW5f`X*fuElpsB^kh^whKox4C^0jkP) zliu|2`~CWXxYa}=LaE2JHF+Oj3OxCOxOEBSU6`mLx6yre@^0K!4u9&Cz9nHF3k*8?p z3pb&Pm75N))8H=KEp24xT+e!~($NY_5HoMH0&+lv2v?gdHf&9%C0kjWOs~mS=Fq{U zIx29wsH;L5lg?D9SL_Bd8~4n7t|nR8UR#}QB1k%gZ$`<>?oRin`c{?l>0SB5M9-jd zVfT~a=z}kzD#F{NA)PPv<~q0Ja~;5TWKxYS`BJS=K-iEo)icSqipt7^$t)-&sh%%= zn+WOv)1$^VwWMuoOLAV>mh!%-;^m^-RDA69c##6ed=BYgz?TlZ~F8zKzkZMXX3 zV_cp6490Ctu|?(Pl6FwqzvIHt)M#^Dzd>D17R$1-k*HAwqS}}@uohB48-iC9xnk~y zrn-d{rLZM{`3UQ(g>u6*0k)QKkl(N|Tvs?!Giy?&IM^DAqYrSuGxFGLUr$Cs7CWST zTx2_zAXFC24edybuoU308u7BtsnKwpj=9f`J@z)@T!mV~K2#oo@ThvnaIAmq)m-#s zYdS?ssu0uh5)fZCOZn?dP0<*JES&ZNdzuFqj!Z8eOp$3fFl}*XhDZBL`IxGFo6B1x z(JMkt3EpWFkehpboZ90B%gnPntYI6MqDLCpEqV8CZsYIm&$`2xAA3z6)c4 zn1z%U{!qBt{m9f~Zy)jZPkDxJG0aqN8X%Ig$S_i@kzA3HX>odtgl2H7w7;DvB&zO; zTEM1p?^QiqE*(@C7TK->rKEP(EsK1DjE!>{Q&*UZ2$-&Jqj;J_gjvw98r&C{^0Ol{ z;YwLjS^^N`jBB1@0t}HxDhMp3D(Z89IA;w4U@s>PHKI?6O4VS3txQd^e!~-w^={d+ z*DDV3mu4S(9Ujc#f97CN2c0(_dwb^tOcR`%OaSdmNgp6mvB9b=E(czetbU;ytIIBn zpD};`fl9SMCdyDcOikmK@dxQ1Ao+D=9RfW=JNV>RFBFXK|h>VaZ6)1 z+=Duw$KEpcMSgpsd$SWR`PyS|MYZBLsD{Mp9rzgFqpA)0yWDGaOJAqz zn_>d&U~U_4hDDPBS7&y`ReXOdhxJiBFQl~9Si@Q}L5{eGyxag{fFTzI%+)n+cLdf8 zaq)^k1l~g4Gq!C>?^0{}g*6(TzJxkK4B43b`}>c*=2t>P@F^ z^joco!bfaP^aU6-XWYO2z+v`e2DjLmYt?pAi(c*d6k!d8AO|@;yX<6;es4s9_;>!b84ZMxDEf_C>#^iEw3Q;Iz zg)05z)yvne7e_DODKZ;uay^H~u%g&iHxovpYvMu&yc-LE9>nJnZ_mEK(5p{QfTuJj za%sEVbIcY**jg|N1^m6NH%N<6(oS47e|<6 zl33z?1kW`F*38)37oi2_+#metV{Zugo~8`A!#~EZ)MIqicFgWZHT`*u8CNN!wjqUB zuuGM8x`7{O73@+M>1Jz0s)aoq0q&`q(T^2PFW3ZV(yHx^czCGWv!t)p$cY9Gxh)@K ziJXcWte+^H0C7x;7Co-lV0LScvPnJF$&W?+#7)u(1mmv=;pl;$kzt!u1Hj4QZr#VWD#q>bg_4y)^*5VG9J%Et$zzq_(B1 zfUD2RuV|hSY$d_V6-o7Ol5W(wntLqrRuOLrV1&rcQUo0{G_n{WzvQE zx@CL2GIe=^jaqUjV3O&267=SituU@t`E*a3%%4ls%hBUhXIjDV;iXKzvLV&mkXgPo z*@8*2o(Q5UYSpJWq&6NrvYfhAQFbR7ldgKQBF`sWT&k5#wP*pH8Ksy1wmg z>1>~DF$Y0(l0rn&JsXM7gh|*;iNxFU&zMN<&A=UB_ zm=ehl^*iVs>8W=CYg{ZcUZOYBrtXhn$XhPd;fWJ|yvL zc#$eBz$%qPj~H-KdSz3v;2wuMV(8& zQJdguQ@NMEbM3|ipk!0UsoAiqyJP;WxLj2m@ZhjpET%OgdW+Y75jA$my7gC!iDI|H zKzj=$`k=lM_qnZac^l`k%mbJc%I&C}AWLdMhnKuuL{^+8UIiMdZf_@G@Zv=&v~;!^ zQ^+h{DB+s}UgAkMx`lJJI~iL?EXyQrHhP*QpK{a<`)Z0vt|?5B5c&Cqb70Gtd9h4y zW>W%plAvECa@^CZY!MAS>1B)Km**~G!;@FAY?x~LRv(|`uyU^xsslW~Y}UGk{?Fjj z^zHrZP-Q1#%A(AqW^6D!81Jo(YQ7Y&)U-Ll?q+S#5V1MjG8IWs`K#iP&0*Q5=2f3m zR};p@*jxc?Rj{d;=qRrgS7Z;xhYT;pkw}=RIf#@!y+UD^qt=W1)Qab%DnS#;eR44$PggB#`BG-i(Oa6&ajy%jfmdBgSzy`zif~ir0 z9FUrG2i%bpkG*a40fvzH?iF&RV&yGz8>iw>Qt6XaJobTWLaYqAv)yr#Y3(oPL(eqT zE$x@Fa9_j#zbSbmi(?l4(##CqLM^18*QmUxP3U<=74apHid=YET$Xg{_Gxtp0rSke z;CWn>NNy!sZ^Q}fE-|8ZJlBNQ1PzCB=bCA>x6`#CW^aRIn+_%JdF!Za?;&i1u|p@l zi&*{C|7fcTx>~d&2`wSOdEt*VA=i1TDk-OI;>gu)QO=E{mkA|Vv?++PNU5~mDB>23 zIu=fBOQMZ_(Rxrxm7xe~C&)#-@eTo$vhMz%!1=70848ptVx(0>aQ>y~cSx05+@~Zc z^t_aj@YX4ZP}yAGQ`!?L4&}U1x)YBO2zN$(nOnSX!_yY(D)mGXC;t_4vLAU?@C!r3 zOl3s&HYS)!VoxM5uoz+OHE~|jnoPhanS5nml29dUmnLkHPiaO5!qqY$FQ~-JEWdTH zEmNd(X7BPN<*Y0LTd3uV9Md>w(7j; zpD@vAf6V&{WdIExo;&*dUrH6m)|Hs-q4Y(%ZgQ^ZBX zvqp@j!=}tJ?uC?FJX#uJ$JX|I7=#2wFJ_H4uai<{sD;Cv5VEUS6n>`UtX6*_5S>rD z)mSoW<^w~A=J%qF!@4S~MNuFkhXJzcdB7IWy|+Pw)O+a7!u^AnUMHaJN&u;^KD?=r z8P({35*4q_c2q8J21Kx|%+0^q?|%wxxJ3r$H8Vpjiw7*;0rvsy3EOaG{sDV}?PNG+ zP2O?aFdZ}=w!Fvs#&KrVG#Q^^b&Si^oEr^^qNe`+(88^Gx+Tlh41{#?B%2co+F3a3 z2Cy|$%98lR)*wTks0an*p0z1Fu>o)+tF;#R1op1AuxGOyHP-mV=&T~DGgz^dA@Os5OgnY#Kk5DlqL zrPM?!%2uQ+v!E*oE}SDERFSrpgItxZ#HO83)qv4W1ZGvL9(YyqmDMVOGn2*jQWo!Q z1py;u=fqnyv>MdabTnj}mNliw22;qD){>BH4=Kz@fu70L6Z2V@u52c=S;c3verF&} zc}P>Mflu{QeIWbb|A)GXAR%q9XQT1|-w}cF_&bsYQ{Gz1&7H7g0aCy`t^jzm7mUff z_ikA#4W!CcQcYS`Z$}c4&IFz>K#{3=dqPXNXS7p~%JFF!O|7lT70j^ws4R`4J(^8L zxK1$azC@~C<+c&@KI*>kL&yAv{XdZVQj0k6C4L~H@tKsE3-c=EvRc=upYk}FT|WDM ziaVAdo3K>ugb0Wo~BZ9NjH1T~yZ!@R!qOy^~>x@kX)m~b6Y0%wN+{!9v-`C9~#POuS~p#4a18uWU1 zT1)qly0p9A2W+3*y^Qv=P!8q9qTeKDUIM!K%RSG6JFwc75GBktEy{a^WS9i|>7&iK z`OF9_`;o5~N7aS_{mkm;u&TT7Z7HV%WDX+>mG6>o6pJ6sH{-H|H*F{B&=1U?mE zc%AiUEFM!k)iOJ;FPl$cTT)6r$Rq`5;BF`%vru_-Lg2+S7!~m`^Nir0$Vz}ljiq{W z5@D96X+Q=NY@^rpHfNO$ChuSmcs4jT5_y_Edmd0lA>K0gDbcFEP4AF3mGcSp#|Cj? zmL{=6&j3&RG_+P87ld@`I*@57se*Rl{WCc?p+H${<{>g5tB%23t?AsiA8j2LLN^luv$7D=V!fs2m_wHc2V6juih}d36s-2owgE}Lxik)U|4V_EE$H` z$lp>jr{XsHObmCFP1r`Yp1gErTUV@C;u?4deeN~A0|0w;4gej-P&9!|#pBrRC#Q(p zv{`uSFt9t}gxU+&{w#n?Y-aQ+{vr8Ro`G}0vcSlQgxr4{w2QoxA9?QQzHSMBp2-8 zm)7RmgfGLQ9b*pcW2$(P#G>u7rPa%DeF&o3#r(i|KamMw|pf{ON%whJUhvZH<>eYN)hFL%`fdFKVOsnxACPa(`Bq@asF! z$zd0NTlBm@xr!PeUV9CWRRJ$+ zWv_}QW>L_i{tW9{f@+VB5wD@r3_m;g(TnA*0rxZiJ?^J3MdEW|$^;wsRRKh!O};9> z{L-X=+n+YGRzcPu8*ft8v&T@JPl2Dx%T2fMn*r`sZ=K z@{*lTJk26)j7F<%&2bQX2(esu7DOcudUDxklS`}8vq-0SUrTqTCf(BzS9x$;TQa%W zGjKGXJM;^O{pKR#4gIbWXi_o~{FR@y3pqh_R{-Ikliu|u!=Xpw=ywQj08 zX4pqI6?@f5PY{r76%9#1+kj!-)R1cJD@;5sB+cXVAtsWYJOhc8OqRQkZ+gqCo@aUD zaA5b}hJ^%PH^Q*WJ8l$<+%ah97AyQp?=uOx#hu8<(h7Mm*rX>=5RGNe04Sy0zHM)L zjQ|KPzMo;Y2V5~+ds~#*czjgbnuf2`T^@ogrD=6Z7)#GWNFY|hMFsUZ4F=IQWhqk= z&a>RZ61RH(Q<#ZB)BGr@XKo3t(}rEt0eF8lNU2T(>UvC_3SrkOtBm5S7_fvk1e?(S zK4AvP$HZeAr%BS6J%jipjbXrEM6}0HAH6)7#)3UDuh%tR&muu#V#-xC)Zi_Z%@&$- z*_w(b>`JMM!Yg5TFRpcc(@Y_`Q{>lZ>@kD6D@~#6%tmuuDXFhIq-;c-BmUD=V zRl1@#pRTCNRTNU)g~k=+ODZ&6T%Ey#tBTia_^hCZbJf*^%oVr{kd6?KiJZgFIP>Ed zj{9G_aKbpHwSC+VB>nZ;i%GQ7Rv;6%p-h<|C zKfmJ3ztVonKmF2!7{PR{=DAfKQAB?{`|vrb zHJ`Q_(vCvi9ozVpw;b%;MH^5*)F|0lep2hx@EP|PG@BY=$z~y`gTO#DCtZ&9(RaX1 zq<1Uzz!97VChuIbI2CihKW1toIr1FnF+Zjolvqpb66%0G9D*1@u9)EX1y{5AEu2b_ zw)S$+GC#lrV>y+(;a$v6d#Gb>XGKDmc+5~SW3q1Z3aMz{%OKUy?bFq~_%2o{?>aU& z)oF_4%j49kPbarox?th4&~--iN*EW%$;)h|bcS>v%}m|u7|laxe&2*}Y-q6F`=W4r6y z-y-Q~Bw{qhT3xq=M>oF1A{Hh$GYfQ&htb0d9QTk!u473b=ao75*jtlhqcU5CMzc09 zw?@n8&QXraVN)(DzG|Gd4S?SC#GpnxSQfl_zHAAUwW{vx@36B)=g2#!nIyv3lyHCh z@nOFU?3}>Lw%y(OiD7?T%1ah60>vio$^F<*4*MNF(qWBC+ph1DvKe}027MBm08SJf zuk#@Oi*y;>^LN_p7nbnRQ zk)Ig$x3oTMv(vD?U<>3nZSl(S3z>C4_fx}uXLFcw<*vT7+m@3GyArsko^scJdf2bo zArD96b|!g!Z6fs^_CBj@L1gqQarNrDLmY2$=N=6EL#Mnk+B3_A=Od^P0{U%{Csnq! zRs}>nuoCw081b~2hUDFF8sJq+>Qt&wH8)gqZBA0bQTO3b4*RVY$WL+!*{i$$T5i-i z|5L;MiW7@wMQgi)?sjKu4+s8>Q#`gQ{N`Sc$AzLT5!3=GcZwe{WD$}ib9A34w)%-1 zmtD=L`QkC#KrAY0Ee@AVI8zC}!#??(?_FX*@6u^2^MRBFKGHMxO44Nn2{I151GbYQm8FWlmc%B8ZIpt2PM&3ua)LtBq2hk-V-W-y0`lg)Gf?>IpyIYC%c6Pe}$Y~T#$e3!FL|N*zGoBQ2ocMXAG(; zMs8U(uHg*6z(7$$QNjoheWx0Ws|7d}IXM%!^-`jNSDX^>uu|UtOW$UP{n@h^OXp3f zS-6s55f_L$U~JB-4S`v9n8QR;OXa+#aPe6SZ2%^r&TB9=)o#7^91eOEp;n=vc$*2= z$ctuGn=vTMX&tL!=XtJdRtC9O`NIDo1dxjkevPmAz~%{&d?h{h*qFWr{N9ZMXk z5>n>VCE|A@#M2nkSo=8Ho4=2qxgFY^KfKlL$K<@jJ>YjmM#dLfZ??BV_g7r&%4>qC z)vpG|=A-U|uRQiP)kQqfXszTrKY@M_XClS#>~)hD9(&8mqwt$LA9TOU`2l7)ebU>B z^K#iaKYh9Q4%Y>=(nNOwG@Pku!*K`C9T*~z0l*g!+8}ts^>_}U_68hSZtmH1M7LxUq>B?NSGC5?Ed>nQUNTghMhLoE*v2gZiXD0Q&HK{cPFb?3pP}}Pxcq{>{ zkb@UYWtydePw%Tr3)mo^+@7jQr&`HjR#y3?kDtO_KCv^t4`}1=&we@mbEo|Ko>D}7 zIr8NLk52i&{*k1&CcKaP zDvm*yE&)ph)w2s!Yn+v3#{?P6^~0$APSxXx=6{D`r&@L!?J-C3Rgwrx>2`jru{sMh zL9jG3{naBABPdZkH8GRiwvFY$&@*ji@Jh7m=P7USoU{X|7~~LnlUsMq+$_@6&Dn_i ze^7GN;D%?(#LR#?NHT>9pd-xkE=qY(TyP=+FbIh}2^OcFG}+2L7Os2QtWGZD2WEIWa7b2^P<5$K9zZ*VHYZD(jpRD_6=3B% zhX#0{R8V)H29EX4=nTFtGXTp4@n~%^-va*zxqqWo0@)4Cn_3GO!;xjeY+l>kwM4?N z18A_w^x4f*zWdKy>2}HTgnz)j!0%!AZ}?pX95i2M5NwrCl1%&Jo!NdvG!W(-qy zP|2%$U_IIq`o?&Ygp9nSYRD>rof&)EQSqIE8$0F7QVDsq!D6M3%?$?^Opx}0~QgBxE+>raBZ^ZrjL}+;3 z>#E<1lfn>RLsPe#N9kcIiI$C(c#`){gpuY}e*oG{jkViNqp+%TZ}Ho*-Mqrj2*9*M zoW~JU@gLV*C=EoTa*yK67rC<`3P|nfT#(90QY25Fb7ZRA_5Dn*{Nk~p@ zTjGBF(jwN5v0np8Q#b~^*fw$jD^icnl%aoAOylxJoftN;z?pkz(t=?%lIH|jS?b1c z%bM3~8q)f^3Y9D+K+jiwbM9;31hU07p(0z+E`A^vsNZe%Z}+2DP+IV+=H&!_Jk#zs zc(Qt4-ne&px;2QN*C8=(*A*CM6Njv5vz7EG8v#7#-*^&0HdYk-L|1AO5++es9@;`w#pblv;5Z%Sp8y*hChoXkVOf!x6BYuBxZ^#HA~|5KGA2HShs?jSI`91LmE3 zs?CNf{Q?oiZ-;2wF%#qcNI4)6ljuloadP+NON0}=!;f~+jaHMw@MQ3%jgvNo8Sy%o z#-eD#rEH{!`}q4Clfq=Nb2C;V}8#!nGo1^eo_}(?PbkE1a%K)0-tP zMUr#qKv;SU2l1@Sue<-b!+zsSlA`zPlPM(Uk;~XnX`|T7Bao(0QLJj?nuVv2 zC4qaDQ+zUKiXisG!Rcj^dEJ0_m1a+?rqWcZ``j2R)j{_+{Pq^q6-!O6N{Vaxb)Wky zT!}ZbmyJzAaka0MwxR7GDMC{xc=)(9teQ8{pm-^M_9SAfa}}+?L#NyDZdh6?trs2; zuxnLtckp8HcU4t6Wp~X~S2iufH6fX-Ha1YMh~AORgqlU zvJx!m)|RDNvb>UzJX2Lsv9zkP28Zt)006LZnGVAG>jw7~fEietuHBxmtSNL<=4!yZ zCXHA!U5m;sRg-xi+@w@|{M+A<%5TeLgnU_LOjkVAll@(4dNoaUFJQL(P-VOikQbv# zC)EiS>-66~L9}eI1qud^Bug6TfR&opO`k{2Ve!JE*vA&^uh=HRLu0K-@h)`T|QfF0{XqhM2di~INmk0yPU-&IK# znqX)Y=yIgU;kN?=O<4d#vr!;;nTX;Unh0r!7#d(~lE zSjK=QY-g$yOA5Z9_R=F9P7yJWAeX8z=&J#)z|yeY=x7tMnYXSfN=^lAiMc-?_54fS zylDll!??(H&!=tHkm5ElJhMPWVO;K#=kJ<~!}a zZPhWm73JTfEe$PxV2(CM?quG4=%ioSh{UapS;vjoXN63z>>Fr23m~kosDMmip%$Mk zS@J|AIpzL4H#WIV*q^uISk71vyRUH4&}qWPQB8*+VXNmSEtU!NYGIff>5aH;S3G!Z z6tG;eId?A3p1YbgZL*1jKsgx;parYt{I^Pr>Y~9GWp1){q7uOY& zQ$#B&NZ#dTvDY_rz#`0fabh=D zQ3?vnYZRe*40twnUz?>zFusq9^B(8=MH^|!67@tw79sn_GVizek|{3Ncoj-X54Vma zev!QhZ)5k?e|*!c>W*9|Q&QkD*BT+bDMUvQah8a*Cv6mIulv>i^rqLFGi@DSkb&po zkW2sWn_gES7i@%XKqtf_z7FA6grs#ktOe4Z^f+Bwr_WgrYF3^WD-(@s$WS;=yKhof z%S1qx&U5vJ>l&OhYip`yst?jJ*V`^rDOEv@czgm_=(vhdbu-2lHZ;0ly%pm><)PBf zZdhF8;6p>jnZCZ(ef{^TJ4furgRc9(yy>;gdu4qkQ#>E=2xF6w%6;Dyy6Rm^n!M!+ zdQ^496Cji35nkr=a>U>CyyN+YR8rS)U zZ+h^U;hMPbe(_%={O4B%Iyo&84e=SV-ZOsWj@4Z4-9}F~_| z=mq!hx!lsM4a-vW?GGrpZGw1(8lqm&&HP%z?+<|Zw0@u0=C@~81ZPt84};9ASQR-G z2w4?{HBB9X`O1O7>J)+77eZ|)jJLD`M^*{^tZq%NOL2Z`R;XvaNc1jV4wR{tiU|x= zrh#D_PdT3e7IlK8cR?HRbG^f;@IkwaZ_>obRU0(Mg+NzxlCUo{SmbM-aJys!4xZ?y zve|ktytCPwbgmlAO*B_^HTgmb7%#Y^Y)3^d)wOOfOj2QEO(iNRG-#;M=A}l<9YwEY zNSt*bfmhaN8d8<*g(?iltvS?W6kb(@{)*IJjj2r4%2XYiwha2Pit1(fnJSe>4s$K31Iy#GbN<2kKUrjB;N5v@0L?;OU_t4npHE?>`* zz;8#ph=>pz69ah6-T%OgepAw1HH{H<+dufCe<+|H60tFkgfYlkSGX3EmsK-CD&5_9 z)Zs$M2lU;Gw$th81yX&Bm`eGwitJ#|Ad1uzo5kE=+XNzl+hcL}Eqp*5GZF(bbtjFp z>2YgI$Na9H$wdcHu{cJ`am3==w%u0ZVreLBx~bY=T*Id&tlH~de8SDY@0h==&bF!X zRcZ?eT+B=v%}(WFZW-R9jq}lwV6!#SxF%i>g2{NOm=zrzR6kB8JWWQOF9&d%U4ve{ z##wD709_ET*RdMbYqoe%P6WZcjYnd4!*gxipoWFrB?h(FFJRq~XptHncMm>r%x?vJ zXo@8w={-=);mtoGxqkg2v(4I>h&8ei+NJo-#Gyu?8Z@IW>u80Ha zmw)V--|3+*xyJ#hJdtttMUEOPAk%bfW19R7fsnVyo%-=({&Vw@Yjb!s86!YU9814N zbtFS90g5zJUC}ubNj`OX4dl^ro1bQC=`mshuvMK(IyKxtIMHOc@wgyGN?0f7Wd0X|6QsNAd3Xpo`B#FATOsw%i6 zi{7)QIweq&BqMBcBEf{|&8T4UZo6InKl*-yl2RfhYF9dvQUT~H5QFWLLtI>oZ;@nt z8+guF`sGhOaBXew7neU6VBg33qC9gU8AehW@h*!9{J_}I6Dm-f&CXCCH5zlj^SeIb z04ASm*04#k7Ef}thuBB)Ce{qnq?*%Xu&`?7OJiLuxoX_xpf;J4CRO-`xCf7E^ntTs z?Q5@!16e;J-epw0%T&}eST9ZVJybbMJLOvwXs$Y3`S1IF`%6}hOkBNEuUCgF`B`UP z!`6jEOsFxTewtoui0MzVI9m;RWpz1E9}t6C>Jle$tQUcP5eGKV{qCT0%v~MeZxJIbLHTIXcB4 zY;3tkpXM<8MvQ=wTo1I{qG6}*bzl3M@7M3}x zQYf+HK!X=u4XAGvn+zA89hkX-0%Tc%M{lKH|^vYRv zD2q+byhJTX2DkYuiHJ@!$IAx7ZF9bFYBTN|^H_U-3I>VYtM7pDB z;Q-4|BU6H%y*OjRN&N@#-H@y`=>FwLGX9o% zO>*(K8sxoNy!-UZl%^1i!6tz^Y(k75pcK5RA#59uGPB8bB^oY4EE0w2;%I2lU)4g@ zG3?L7+#+TkaEhQ2O+hfC_>~LM$i?EM`^rbb&@Vge(m#^%Pb)?q8Wz-a{US47ve6|i z>7?arG>VE}hc+82{q`sZiiD=Nb?O5cm0x8LmvuLSsB4Z8a(AkUl(8r11&|<_B!@IC zgmzvt_#d_LZq~+fYoI5Z;mTE8PxZD~)XIZy_{TGTeRE7c{j4Q*oY?bCjr{Bn$;wgp zEgovFw6~1o0&vUFVP@SMKhf`hbUv|)NT>GGDCme)%H{KQ6~rbLGEJ2*kGWa^Gz(;) z!+S0VXhuF=_rAlJVyn|#Fp?G30N0bGhO~01@UQ@9(hY@Nz5}RGp-N<%JM!t4hE#Uh zTFk?>ik3A+6)QHrh(gw^{MoA;+jd=YVBPKSJz|nH4(?jBJ`mnaN)@Hh6 z9uQnIy&L_rVO-v(aK$=odqzC<(R-S(?J*593y@lAzl=a_NW^8cAQ#1O7ifZWF`xLM zKu3p`j3nB`zcJHoMKzQs14L&@bT^mt(-AWazM~I+=U@6OHeh#QX=$$k3h){vP7|dv zt~@ofOfxar_zCIE>Z=D|efTH81c!`fXomg6H1xY4cKx#7)}^o+Wo&1gm9B3-ST3T> zGignXRjzHg2qmM=c&ASU+bY<#>%QcA#;?pgEIXiw=-% zJb6Zv;Y*2!@z43Y8vVom+fF3DnXbwsx1${`#FDux3K?V|L6Ua-on9$zxa87 zOZgl`#OTJu!WU5D0--Gptk~vKgM8lT6Itr;R7UHg2esAbn)#{LXWL*o=$%(Mza}Tv z06nRj)78Q96a8BeZui=ahmn#Q64N%X#?_5RXe(?F!XYX(Tmzhs6!>{nbS(4mhh{L# zqew*EabERWhj-+Z9GZ>O&!Q+`b1qut^x;lOn1PT@a$;epTSx>Ce=ZL@wPngr-no8b zG2|q`lGgb>r!hQlC=YFgb()q%-|iiJSh(#scne1#?z-)R(;6#IJzR6gZ=io^-@wDMJO2Jo z)|u5-RPLml>}T1ISzh|u8vFqSwYUFa{awGOMbuY2+&z|$h(#h9$KfL{# zzfunClBrA>ARR6lscGgAMbs0HK&DF0L@Hj36>~I`cz{myl6n8^)}w^MD?KwG=j;N3 z;ml~63$EdwAnak)36O?6`j~WBO*kc?*$%ckeI4Z`83oQxnBCo3=z9zA-7WyvoEY&t``x%V-<`B@rYo%?2*iY6_f-Xq7ID;FTVL z@Q9~g6^T!bi%LKovkB-~Y+)do2gd#AZEW)1O#rXt42JmwC5F3R5bzm*b0) zKB|KFZ=FwNDeQ&jaMwKPhCcOuuM?x}b^g|2(fx7#JsySWk$F$eg49t5@ocR=^p$|l zz%ldCdNmKMc~wzly2a9KRGOntfFHYI5tneE``D+y?^SR9f600iz_`+@&ewHsm8w+x zrqaG|wq?tbcUzM8rS108?$y1-wk*lAyhygZwC!|SU2zjKfdn!@oS~Ec5)YU)13ZRd zSdvbF3=GYX4g&;2nBbmygv>m`3lo+AY2NRD?k#sSPn}%fy6bnpO+)gm)htT+sw|wn)udeBT)0=on4xBY3&A6rW|kf$oqg#WcEcs#;T8+YUU-a;q+j zbtVN7d6YM61%O3jVL<$pNQDlLr-dhJgf}SlQGGAQR|p?#G-=d;GBlYNs7=DOJmt1L zdCc$M;HR%lUc^j@Zf)h5E1$5Y2JYhGsC|BQ+E+l8V3 zcu$f_%Oagx<=acDgKENIDvqRGYTG#gKp>P$OJZG=BuF_I)EkdP>(I1pMwx%L&$#!L z`qyg0!NqWt}_cd8{C-t;^8xzT`Tw1g{axfU$8tN?~7 zusZ;<0iENd2C9kkN6jDanUzUWNi|{s5&EQ?T4pPDl8EZ6hg zF@G&cW#9y1Y_hTEzV}Ev4w$~Rr%&?qLHz=t!1bRv=3jQ7U|WXnTHQPK`KG8$-6pKSig~Mv zU{n=l81%wTN@ANtLejJ+k}Gf($uLkIDrq}rT?3Pvzc9%Y?&bS=88G_t({D{f$fJqN=Wnui+E~m?o)p&9QE~K5=s% zy$ldLW-Uk}a%h?&QK;b}i@u*+Lm_ zzRslu4p7SFiza7kcK;pPiNiEoy3&~1(Z9dxo z@LMLIE-xoGAcF$1vXa6soiFCl4pc507&l=5c@3Cusbr>ws+Dc6nQS><&cAxg>gS|YCt_3o!0 zjZmn@X7ouqs}z)%&_mWMh8Z$(#r?n&5&u&PLsioz z+{ce|;gXk_ya3ZMbwS*4-ngO6ts|>RL$MK7%ZeQ^Y#eR#!a5LB?xYxnabz(ViZ$Z_ zY7?K|tS?;+k3s&jVgwe`Kop+NDu>GeaoClDV9A@T@P26!Rbi0r3iuf&5Rc7o=4Buy+BW9Zc)O-&6 z$DEX~oxJEeiH#V67GQZh-IsPp{KZF1C7Bn|T#QO2c{Ujr39~{f)h&2+P$J zGPXzK$PNLVjucr-{zM#LrcJqHdl>`9O}N>TimdGvRD+|@!edNKTTY_?a@fQ~nl^$lF zsOB*Il}CvQbp!n+M7u@yXH>mQrcpDgcu{OHs>dB#F~=WFn>M%V5M#D=Rxj0ptd8Iz z=2~?Z&pB=4owa70*>*?k5b)$nzsgxaIcD5HACCByRpB&fmmE+L*hyQwr>-F$tZSPg zYk)7Z6?@Bl*O3V2v_8#t6C5AnB#LJC)y;%6pQ+iG>w{V#QYtP}T8+ge_6myPg~@3& zhd=^K`1K3(57bOC>wcA}H))L1@(3K3OGgr%hN8z{@J_fL8|a&Xy7*jJnZUd( zTRlDi-J0nv(KC@(bf#S=!0vxo&WzB;#XM%i2n-lRm#dC>tP`>9HZPA=sX*RvRCPbX$cay#8 zAx+F3&LmqL1eh%dx7_KzxH;kvEorWt6tSF7b{ECvRwtTJk2ueOq!EbpJxhU9EckDnsm5+g2LNyBJQjp{VUhsJq#rzIGkT zVQ+zE@8;>%EIeRxu^+;cMkTfx9c;ucXJ(0w zfs!K9vbTdxo4O_uQ#tbof%3aJG?=i6c*%tQ3Se%^PKvR-37K*O`$`JY~ENcaU1Ij@TBh!-Z!bqr|#{D6i5o_40f)d1mGv zUJVW%qH_ap+#%Y9^Eh#i`5iFtV|?WRQJD4fL{9?2i&`flWJUMZ82=XCA1o9}{?4_l zTve*nl;xNo8u34qZ9!P4Hb}mU zY%NmLli-i79;E6PLVK|h%Q%V!m9;W?K%X(5gSwn=X=o@Fn=@40$}7?~mu^6SPj?aR z+oZ&;Qm)jXD3DPT+e0Ac+)!x*5l%T`SHZSbsu=j^!GswT^aCUFZukB#NBu`o<4%kA zXjqGc1Jq0eVh7n?HY=>ggH0}cwp#7tGONXI*C9wT0L)6Ug=r%&ATUdwfK`ZuJdf?y zWK|K;VJJ$O9Ek&1}#v)JWP zh`C9`vLZ+1;=&w1_qk7hHcoLQyP;Yqv7%c6a93RVb8){X{oRTqtL_%HJ?5U%q0yRs z`w+*T2GpNmjL=p>Wxg82+sSR&!K5Un!|t2hH;dzD`q$$A0grh8&R>uFKUtTQHFD1V zH-3!N*|gi@e&;vh{{NM!O9WUzT2TkxfBk&if0E4KL;or6--H5~4d9ZSCatj~j0T`~$wQgam`Y7KiT)ZPAd}*K z7cZHuNvp0o`nD%Re#q)NFM=MTbyOYf;(~Px*egjA2+VSu0TsZ@iWl-7IJ%{zRC}?q z(Fpe?hTVsLJMOP{n_fq|t9Xg)*y;kgTHLB6k7AQc{Z8EP_Gz3OWp6bS4}-_A-{KdZ zXq$^}^uNUYivWGo$&b6=`duEk&5(aDrJ_XwZO@HvUcWw+AOT&3%g#{!@kPHbLHX&Z zx1J9%d72lVw(j5WPQMZN*AY!Wx^eADcy^~3L@P?n$00PkC{>p3R2QVBGt8co^&n?a zh&$akzetth9nlNt&muFLgvZpouu!9x$4Eh=(?w&{za=DHoEB$wdQnd#coAXe5%-zj zW2zad!jnG7>sFZ^+%8!`uFECbei+hKmyDx_usj(3NuKv^EdQqoL=AOg@^Y`yId&T< za?>-C*sM`VbF(7Lc4`y4*#aI*`?1|3(rtHXAH0y`b_af&Yg1Dagw@VN(ZtQSLyE=2 zhOtT;r_y(wGHpdG{vnt#-DRTthzu_4%r07~B-kHIV~2Y@78|a_R2+kkIIM@Sw2ytU zZnxbok<@%T%c7cl_WDOWg`cQh^C?fa#4K=B#=6l{qA?p~>Stoi6JG7Q6K0*5{Y{tAsSSt24w62&>xe~ zMfFHDT`qdYo%u4;XGy@uTeHU+`?!?Cd#ZacX(Er!!9-aRwKGMvIw4X6dc=jsbzh2wb(#zJ0T_gQKE#n55??UDsE@H)>IN2&R(A z=@{bw6)Q!io4VWuE@-119o|x{Ty@13KfdVN{}gkKdp}$7d;pLQ4B3RhJ#Q07V|Xs9 zCLgV51EShZE0KPQABVhpK4G48GpQM7V#tXeGkdAMjP_?nM7_Spvb!JQ+-Z@6rytg3 zgl^8G0ZMSOCAntFTyqkR-W^M5Bn~uclJ(X{>u{D^hLZ`hO@5M?EF$cKjJBJGRhUz^ z^h{XiEQ_Y*6!I(ZrXW#`hh_B6vs#ycEiy|2X`^57*%QeU@R4`_?yuv1VIoQ#{Ni~n z6w$~TpmOBdfhyn9r&#z%?+&VAA$g_I#T7be?q{*ZM)#3#v50+?OZVQtWzXW*r9kX+ zBY#KY8`1Cb_}X`LbnAiJ2?ekuR9QE0g#{{-5uy>7`<&(7i85>{oJyS*H zENwL9If^0&)UXl~%ti$FUErO^+&8}+_gh+&0!uGzkuvcXk(BtQg<5g@{~=CjN=#fy zg59G*RB$I9?zz`31P*6SZK&9e3rmk!RusE*9Wq@5oHSbr^w?j zSB5%Ejp;@ezi34s;*T(c#&lDrso0Qj%6GS{&b1ekO+>ej6f?aTKl2ryl3$+u%qO1m zqa%GAmi^~t>Bo_G-bj5Q_v@*B$+wc9OMX{!WBs@4KU06Zet&&F@ntvs##8^2U;WBcexLV|Ix@gl{m9Lf`|!FyjNEgd`|?x%z@3r5 z_oJ`<kqt+CHLeJ*IZc;qxSU@8CNfXdY zRdK&|Ifc{8yOB5&G)Z$B(R1Mf(o#U#4iN(?k)Nii8~a4n5Jd5wuKwGozhPC9@1DE{ z-O!3RGuN1vA5lMK`mq3`+3~17+&1K1J-`tw1tfEa?8SrexP%}Xtg{J| zw5<3ft=;J^|6SBye*~N*9;I%Z5#5Tn%Op|K3<2eYuzH4C?^*4$fmmOdBscPW*efdJ zfegjd)Gyn-*jYFG?Wn&z6Gm!J@|4qA_a8W>8tydEIC`UAByY_mB4ptECTy1|EqH>F zl5(7S2&Scbo4qJF6o^<<2Fl-mao3c^u*$}PPW^;@Qp>%(!9a7h6pPZ4M`0RX14AWkOfFlE6s z8#GWEp8`_~gbs#B40B6hCR77)hjROiOoi#j7`Y)BM|Qfu{JE(A!AXV5-J*`2y#L~k zebEE~FT7k!Lw&qE%jOyiNf2Z#p`yCiUfjmy2#`iJUnZ2hZn!TJZh>yRIwK>;ZujYb zANBh)IIwA2VA|jA4*WvYpT^2VtE9oMwR95=*GWkQbhDmO`&3)<*ipotwP^Z~y^I#v z3f%6eF1b(sQq*sBzs0tvDY2jwQ%f}xn*wUweCk(R+pk3ZuP*s@K=YY#RuiGRE$&IA zI>?oe+YBfhz3DL9$?iInPwi}<+ag?#hCa#2dzG9- z;{Jn0F5M)Tv?E37efvnZf8(=J|I5U}QpwQli2C+3?$IFi8xm!SCP~A2SxLVZW3cnfkD{dXz$NK7!*KLU_ zlsruwx^Fr0mixXoFzbNQ$ffN7Q)0%vUKMZYO)2i59&$`8*Go5qQd7 z`0c2_0zLc83=3AhbyZPrTkW@=n>5WBinmD2CSe(NlaKgLlnpx|03CcdAb4!Gi?0R17W59jkccOk% zhZ0q>14x3H_3KFpoCy;%&U2*V4t*i&w`L{5K1t5)O@(UibPvA~_50is+t%K|+NNpS z7*#$y5+(hq79S5CzPFtJdkoq^t41a_VAIG7i6hxE8{?r*)Jb8`H_O3S&9-tPrODe5 ztSocWGz-%kta{1~_dk9=>i4?BAJB}YC3&-Lx1`H}#=JO5uSiBJ7=TL5qk)HxkgCm!ct)-96%wz2h$(J3oMGdO3e+?}H~FO~ zm#*sjGF0XL!zSzbovxfgcyO=k&2xs0VtQw7ful1cYfTuGckKJ< zOYYI{eTlz9blGdmmql~K)q88{qk>VUg2uTNWpkx&girv@#NhJZu(;pdY zj;jXTyFUD;*G4rEU8MV-&a=7R3|m=BChOcAoG$y(*md_$?5$ZV1L@tt;1!1wvam|l zmNm4{Wws!TS7?{b3Rf!c+~)r3U%%y*j=Qr_fN5mZLP@7Mxk5X zmww<)uVe4MdM-I}K<*J7F`PAkgS-8~dnu7=KzrSsIZal{X)#@qo01p30@O`$TV^SfD^u9fcG+ytE1+GsdxMCyy*?PSJ-X_*`B6h6sAjL zWvWsF1>$Zd%&M4P@P_(L40u z)m}YvlgiBC1iV`gu3jhckTGKJ-E9mG;d4P05gn7`VxFgC)nLZl7N7IlR&kJ82Z66n zSCmLA4+J8O&G|_5`N`=!e|Gxy_6A0ej#ZCY;(wRO?B+Wcr(T~!I66z7EwjyhHc|yF z07i3f?9M+-zut3aaOU*^;vr~PDXJm*#vD_mT1Jd-YvF!0|mTcRn=pdMl{N zOxhl%<5<_$J8#XrPDwTY^qu#edA);DchiBH!)9XFM`m9?O1aVt^j!a)56`~7naEHq zGjxm>xxH{_%h}f-z4OG}>-_~Uh!j!NUJ#AhbLZd9ac=dw*LV6v6W&RlfBoxszH;I9 z-a9{e@%4W48JHR}SWVuUo`1c63rMKaNW_5pVy0?sVfP#WL?EiT~^0+b3Sh z{B`7K;)ch5xAMx5e=D*9%)tfW-2UaSD%=okZu#yOK!!=oE#$mRPQI04V{9-&Fn*Wi7Gon61c$~`;e@gD7*!^vl=(9< z-Cc>eO`o9heN!xP{>m)noHRh@L5xR{CGM8*6z=-%cRn%msf2g?o^@*ajicy?spzxg3eIqk_D{!R_)Lj zFRB9LnS6R}Sy+qeJRPn~_BNyKC3Xv19?cv`^5Y3?Wi0lYU zwD>vGevLm#HkxD{oAdxo3A3aX>r+J9a4Vd@37InyrC){zV9#O~5S-{qef}^lbKm*g zo8B3B_SZmn7{`ql=-wiJyop{$elfXbS&l<5N;*c#mL+2@D4=Hqo}W>-^Vi?>rdOQT zu-%pxez;F>TnRLm43eUa4~3Z*6YL*%{%^eL^-ht1VN#LJ$(uy4@Xn@SwjHZOQ)2Sf zy0<{chv}ud|A5b?(c*OV=vr|=rq?wcuSKKt z%KCdSj5%~nW2qV{Dp5R7o4Ho4Jn7E7{-*bc@A)@f@^{|!wrnxKh+em7Vg+Ua8-NE7 zt26vGxP}jn33!IM#>)}+C*0q9Dmq!LzWCjbFZMSS%lV<6hG&n0Hc;ISkAMH?w{`gIHmnVe z|E-j~-VpBRy~t*)0(Y7|{Q0gZ8s3dNAN%m`S;sR-Dv4_AfZo?=4YOuMxtMn!;}UW= zw`}A-U4eAN?j%QXjL>9RDXQtMWL>S}m#!|-{!O9%5pa+Vyzw~>clq8%UTF`>@IcyR zCd#DeZyKq6FVtiMkFgU_&CTo^q3Ve8x%QYIZsm!x4B<0UTVzQ)3iiWheWn@)hv0cK zN(|8yzQMW@GR@H|YHk#38#hjI1s?4090o+F^cHB`tdA{RKBw>KadL6x7 zP62Oy8hapWhcCJ1MYaU)tcb{i;Wp7k{BxA@a_hXM7@%Odahe)??SrgR|9Mj7l z>e2R5*Lm!S|40*0Q{(4@F4fIfMDGu|kLtAh2HS3?oNIgZh`&0fOZ(jk_FMDn{-=7_ zP*t4%dc?iT;h{n6rh^>5ZdSpaB3&^)fKRd4gU-meEV}x~j`(}s<7{`hf5W!R^ESE9 zvvb__KF%r9LFqP|9Yqm`0ke&#+`r=FySg{n>{Ls4n)t?;>1uw17|p95bvvIp;#bCk zW0y<h41DDtkMqS5~M|=sveB6HbF@6m87);OO z>OVY3BMhH9tkrrS-mMwuKK8C76hZ$i+m^_@yU)MnG2c@PncloYis{j)7Mi(jS4GLe zvN4X?=+AQcW?nC#S9#uJ?$n7R{($>lwyjwWJ?eEeT|stV>wcGm?bG%!4Mx8v%|b93 zdcvSS5ceA|cs!4js*qoGJfmyqA|{%egZRWtG&hG#66Flt_%41AXwBQ16`r@wElrR4 zU1x0_Kc;8LhO{l)`n2xa#qjYW-MTs;OS)j(rt9MzobdIg)9hjC;~hG7!87bLIRvIx zu%SryI*sd9_sqF5fI_UdAJf=Gx+IfOAE36tFrU^2s?D?Bm0_C)uGLgz7d!99fP(Sk zlILyai*@{(8Aq(idpr}X^!mAox1JHQ!)edkNCQtLPVnL^pT!R|J4HQPvHHX_7U^M^ zx1e;|izEgdh$GExP;F(CAx9$|yJ4SUQ6Y4tD2_cX=6?TwPY}l7$<%&|>(-$01m-gw z_*^BU8f9c^UrcNZ9XQXyi&&3?4m_mOGVKj=__F7(9j#qmVa;-pIY3AGdiL$D&4J(Y zlm>?-=6T}CnHca-l>@|Vk55=48X+tEf1dm0*|S61s@%r(1V5oo@8sa-v<9h z?tX-ICQIJ?WZ?d(OJn{QBip$U)o_lpC6CCF#lYTwS^fyK`RQqBu-66Wp|Aj)_z?`K zvUp-ZJ?-va9rHU~c7;C%QWNSNzgb^^sGCnl!t9877YS{^a`RP z-QbNe5IV_seBj8GA3T~|NgfH1NXdz{7$!+u$#$kejHGNP0cZGbg+9cd{sUc{)E4qb z@Ciw$DGFPai8XGu*?GuRc1|TVyQWzaGg+c|0 z$~gE#2;Dw69oP~d znDFp)5cZCL&~#k7@J1lncSTI`JKqR%UGeZi*53(Iingc*;RlSSs$^aw$ z5Zlcyby##zxJq@%P3 zg7>ZfJ1oX^0Q8N@K6|M%sw7lay;*CwtmU?@7>6|5q#8^j^(rNxW-J{hF(a;4j%V4H{6xexhB6|xrMr>nR6?L?=CC8`uBY7b z{Qz4KNEQUOhxW4-iC9=-Mb--tXHoDhv3`ub8}9eHXH{2Pwy4ky*=*rVHM7NgFx;M< zabJ3f%ZR5@J|+Fq7xc?R?pF_F{DJ+%*;!mvhnfsXsliF969NnfjVtEt%VA#uRs%!_ zOW1mDrvdKhl4Bo)O5F??a2>pYb4@8WPnox$YgI$F_UuO=j#hCmm)JQ~FktQm)`#O`gy;v9VribwlK~#N6I?>*sE3d`#cb zr%91oAB%y&rIw}5NVXF_p70tsy@4Jf=*7&Zx8)0Kv7YbNe7`1Lt25L?WgWlJ!)7P- zSme-=@V65IB<##KW0;B{J*-SjO+VefL$tI(GSOVLjwA`iT=FsXk(Z@)Usb1$yStk* z{z})43$T<+o5@nve4hV&*1eCTLLkEV7-*^bsE)drkSX4Ago3ppx=u}HP2;ManlX=t z87r!dAVy!o(l1AzbuE<%<@IJPZcEC`b?VW`Yi4<5RoS03$jF_O^vz8}p7Cc-MZqZ(L`uyBfWs~Pp?g-~ z&7UDii|BJTs3myR#v^sH`GxC~90`fdlM<3LmZ+|GH3KU~30KaS-3PbPPi0lS!$4!! zr<9k_G@ ze128{pw?Hqzuo-?2UjfN9-u|G7*=_~`jv~c%Y^#vfp<&u;avxi3(n5VfoqN{%gypd zstA*3&S=6utm%9}&pPsqUw4MJF7t33ZQ5EbSh$BiE*`BD2D(Bnw$o(PQo#Lt;tmR%Ot`KFPM?euM4)qP3}Jv)ci2ns;NX`9Ak^Y{6BfFoeow$dW0$ z$#GTLvYx8ZgdyL*an*fmSo9{|Sa>{(Ad$)BN0UvNVsqg{Yrb5f{9K{XSnffDC^uzt zUHQTQyg!vq_JD&^ZKzVxBws0&@t@|`W{bPB1pPOVtXs&fYAqpDtFBdg=BsMKsz0PLGt+W z^6ZLoq1Z2*@s!z&vt}%b<@ysLRrNFo&y?9*6gJc&4TJF!QZ?oTrXf;%hOkJ=3Tq*B zg{yFlvfeBh(X7b*qG!)(GvaEDVFHI^VcxJ7Q#Vl7T76pVghVHSR+vrzwp1g z!2K!Pi9D+~aCDHFN4jCVd+}Qt5{iG0ZG-!-Y*%LeoBGJD+uq4EdWb{ z_*dv%wWH61x3of%Aod`)oBfm%;o2;i|G@m+YKg7eG%)FC z-87F?pmdT?da83BSu`|KOozGyiX&8;J5`ej>VMUh|B2qn+RCeqP}EK9;1Dna1nhEk z!0uQt6947yJK)7}76!uF4t{6dL*HTTjRGUdVn>2g`%21Vr5+trK`kqb-#?}4MO3Lp z!K!OQ&xHHppMM~-)_v#ezu;|kJ9cONSKPrJSt=S>IFvg7S+jh^1YT(}9}-|>dcZ@Z zY#E#>>#<3@qSLYzEnZ5Ez=683cu9$)#xXeZWHfd)m=5}q4heJvGD9O^=s*zxLoz@! zy>}_&n)he@qwXiz4xa&;TG7m~Cv&-95yx&96{nzqc~?WP#%19bDTGrq17MCIxGiSi93i9ZpUYqi+0NZ*6dk_qiP>B%dlth@8nq_c@L=!!sp{$x$TXYU4G&u~ z+YK|F+b9jWpZxC`e|OHxYSmi%!bVy4N8Rv;vo~+%h&Q=tx1(rUc7dvLRN(^5cz~ zs>ju+sA1GHnQjKjZ>td^0E%QbNVv>j02}9auzk|~JGMiZ)+H5j{X=>87Dq6rd*|JA zUx&bgZ4aeaNQp_4M+vUIWV5uJcLAtkCFdV-m0e!+;-p*sKQsPT_ixztEX5Vz_&~&3 zZVoNHIr@lIk}x(tq2BFdWlC2J+||n|)nEmoWVURwywGjzohP+W(m;{@lH{c4hSZ3Y zhFmY*Zb(F=q|G@a;rPDe1l*Iman-%>ml=OKs6n#|goV7@+%c+y7-2$ogZnnu>|)){ zG2M35b%5jyj7Cd7-%=SMp2?9V~E{C0=(AChKPm`M0f~BF_+0c;90bG~Lk79_( z_Y-188Cx>{n%_H{@5vQQ=@sjSTktxk3NNI}z;zV!ofYsp2!n5J%Cx466)-z86%a(y z<&7CK2wM=v53IADlmhA);i;UtmxWC}%4mX*e@S8kL123{O z=8BmKzjqkQH#3QSNupo1kcue@2E|a~7|sho6O0-$5`d&e7u;`VC*Z8v+yo(aI6fg( z3Ix#UnCYvb7w`FK9l;3}aLoussyje9MSQh{G#i$OplvWJn^n-lwUsp$#bhIGgn|hu zqZlf%j~QXM^-T-+ya0&_>Coeigw_KR8m#aDmX_LPNK^LYR!GvzHlg=uCBaL1d>cAY zU}I?39J&yfEv_cbwqWXUJNl4tu%00&s}FV>YZnvQ7mH7+Zh>qWef(al9J>Ij_kof$ ztR=cjT`G(elZcA$Z+K#7K|m=AI%Soa7BJ#=_Cv6TiRcMbJ1vA0A_9+*=PFQ|paI=z zHx>jXVv=`X$rAGLdy4X9nHAfh@t0*V(RjUt@~}$Ku_LSa!P&gPg9Y?<@$- z3$FJtgzU6NaN`<#|DSWd|0tCEG#{b`X(pZP z(I_G+S64vBzkP$lr=;M`r*vl{?XZyz=1Gs)n~NcUnAEKsE;5t_8(E1Anr-4G)ls#q zPMd2%y767~Qjy1ws#Q~MC(g-2y)|*0s|Ao1<#27&z2#{AnIHk0+3~>4)GJC{1U^l( zR?&UBv?HoKP>IA%?(nLtzZI(jeKe+X(P&f|#t;gvjc5WiDR+N0gXwa^i~{Y2q)S`o zxs>S=0HvmMcw~2!`N1Gb9MiN=ZMz`cNY9?ItPOS2=n$K_Fr``t5}@cVX#Q;H$B0Kk z!3$>b-O7EPSb(pco|(S|_i-yqSv0L@*)~&DNv)=xt<>ZCEQjdMAWhApxCSkTDWLBU zMeDAF0yV8b&nGrQvVW-45f89(?b?v_2ChL}+H_%AR0dZbGF|*g680rptv$Jv{Y7Xk-mzEc=L5Mp1zz+hpBiK`QFi zbM91Q)?d*b#@6f5M38W#Vdf+C{u_QNNF)mj^(?wF@YeKFXhfmKZ+mG11Mw`WytE9}Yv!-bK6dOns!O;B>Y ztB+*;R4XVebhs$nh)Cgq08LMww$gnsSM>G0a{}QMV{vvrAfLMsKqFU^eQwCh`rVC0 z`BOoL#akD7S<8%Ib6T_2&HI|7A7DF#y+d=v{Wd=ix_vPyj$2^cKoWo%X)JEF&V7Yr zeF<_VH9BRNugm(o-1o5UXi~vDO(a{$0knq*!~yp=oZi|_Ft93(F}JnmBu;Ech70ZL z?!9rIOT}xO1MLJ>ysWso4H*6+Ga0pZ1xDq0J_H>@y)Yf{hDNdsUpA#>ovz>J<`R5x zKa(82i%$*>_BqCV*50eDP#c8Q=0@w8mF^nbp%xzuwm|1vgQOp_ZJ7cV+?pi4v}EHs zAW><1lq@l_D;Q%l#^#KU4x9ehW)YWaZ$+1q22H{aS3d}iIs*$Nd`lA#TdHXBqbleS zsc&udM8`J9bGx&diHFKNdvlrG%03VY3dM3Mxm0Rt$Ts0#X(nKf%3fJOgv+_+e6q1M zO<*|ojcmTZnOM0(J9S%gO_f}xHQ(Kv%9V2MnWCTxh-xo1r-`1+12k4FW+{J>1cf-= zu(sHf@5yxJR^@XzVp6%@Lb_5QQcu-qG0&9qsY*7pqOq81t_(d=NjHGRaIizL30GiS>(v2?gL*Zv@Wvbewu$rd|V)I`TyjIJHfWnNu{Y7 zII`)0yNw7)k6NV^9l9Cc&r{nlM%?^g-W8F`K1vy!ox3)5_8p4y<3w*k ztOLerB*1e&^UZO85PvMR(83KL#Fe>qe?9L1zwY0DYaAO%@866Q)v&~NyZd#v>kowy z_maIWvo_D1CY?8Aa<-r`5?lPSS%tXnxp;s@Vlv&KI3+ED#aDL4zaRHk-+9j)pU)RV zIfTm-q8e%F!pyhF{grKTPtu!o!_!)Zj|b_FX5g&2Kj)IwD}acTbSlc<>ZQoceH+JF zq65G#7W#%zd-5N_!(O4GQ7rikC(l`{hRqRIkEcusC^b)2uex!#?yE?tdAH_pn>=rd{rKHiSK1>z?Z(oUHSz4E9@RX@zK`4;Rz8v>=ED@z>Gv&VLeIzJPNp41J zzdg^1F^|pOZhgZBBW0>>ki|d7Yp_12F}u(qt@okQhPbesD>A zv-`kzlj7bOlvCEMS#hJNdwq%Li>~|qRBa_x@`@6@L;}{jvm6>CkAvPZ9zKeJ+P%TS zZj>2CHESa15tv#iwm`aUz-&mCfFEOEClt;G^M--YFAg4c&g}~U;X0eSGxQMg$+OxbvB=93NDhemQ{&;voICm<>dF>^#U$$XtbJRn`+1IURA{;dhiaL-uUriKcWIWdP@i!*?=5_HIVSiy=gv}L1xt6%6Ph)*tbjq>@ zR@IvvC4rDbYh0f<;SW4cK7R-#CPha4w9ayFt(z*k`JC{gOrp_yA2PQ|Xc;<3C5-?J z#SGG1jKT2c759bs1UXhlB_52_Zo4sbAr{5qI*6&|7AoJMBLNSD6Gv}YPO81x(KQwJ zs0JNN30o8jivrhzeEg17-Fp|X0%Z4R8c^7))2W-;VrgBum}`1(dpi5<-tFsWLAcLs z&KJ`iB*ha>P_CAm^KIEmsdZ;&6$qiQLV$i+bL6pSTT;bjX9sy)xzvoCK>f2`b0S=C|#pG`b zNzW~+sX>>-e>E|-yN>tW_c{i>#NyQCxtZ%qz3Jt61NM5!Dxs^8!09>yVlF!GyYG8j z1}S>Rb)xh;%~3H}hart&Bii@{Uc9Q&l-aHBm$;go)0!P@rCa&_``*|#H8Sw^HP|P} znaQ)L4RO`-a%#f+IzMsq%GA`g(*pUBYVlY^2pl)R_rAA0a^C$2|891JAH47NjT$YK z*yj6e)&%6$CfEjmXGLl`{34!qgloyEkGbgg-S^hFSX0avve%@^RdTsNPZ+1!Hz;zkC=qs7uPzp`# zP!yjuN8>P=>pWkN+Y}d33YXgRmIoZvQ#89oA{r<8RZ!#spXnE8rWA&>Gkx|gIsjNP z87c^kMt5d-C054Lh~KkkL5L-@A1w=;u)6wTCA*R^A}Sy{Sx5=l5 z=06CoIaR2^~kz#=Vkg6ts9sRJpKgg>I-FJIh0a-fh!}7 zW~h$1>C%M1Yq?EoF(UjmAaO}9ZHVMZ5>dxe+l1bfj(*d9q+!C}OPcKsn^rn|2*oFu zh5S0x<+e0V_@8strV0Ne?o9K94=%VwN%uPYZ4EMS)cnZj>v5VeLgVga3+DnD_?ldI z&J@oe`*c84Kp8XAkLm@?!AQFolfLGK5>l@tFwAtE_S!R^U; z_v#NH_6MK96BMp7JtBd1fhB9=V?MA2GdTjsO920AfRx^2u)o4*R=F>-SMGcePN!z;MNku@C@p}qP$T!^#}50ez)Kd_5s8|q6a0gWS)#?4 zUFXLS`^~Fjw!(Y3|J;yr#cRG;E;))Z!mQN#z*RV|-S$@x`z;MIPrOl&Tpq&`Vz#*s z_x+q}8x-g?hjyqv0e_Hg7{I^q2suZ}k=vJD$Fcj~H?h0uVl^i#e%-Dvuw+WyHvjy@ zeXpfxLRwhy$wav>ci<^_&tB9F4H+JJ5vmR?yvIqKrk2=+=jk&M$mcN9%j}NeWU)YV zaxhn$6UHak5q&h{&K$q*t@R<4?pN3w+-wdyJ!_vD1;D_<#f8AMs^4b==RKU>_)At7 zKB^N#?$Xouy{0LHx4;WvGj6|TTpuL~3|_yLq zvKNu%IW5)HevBCPRk4D;a!Vc~^bQq;kI#ZoB9~`iPwtM!73^jCyJE!SME)s1FQBW8 z)BaeOkuP*>4 zmROqNSLaRAHHO@a=|ht!0XX)#c%XwHPpJyIdnoD-fzB z3~Y5fXYPAzSfGRM27BvacT#Ry31NF@#>2V!G@8vJAdxJw~CY>CIuE{ zdR7U$z8P^yUHs7b``(T*L$S~@UoG0R!dUDc&sRwxNNO5ag{Z-9Qw4)mX(_Qf7ICqQ zOi%_|Q3~!DKPuqRhk#P{Am9XvpJATZccmgP+pO@k>hRo8&$+M7vmRXc!hNsgwy|x= z)EhXY{39uVQ_fz3Ty&~nveNMG*2G-TLQv}Iw#U}S6Yi%k-}gG#8=KVxFk3}|@Dsh8 z^`})yxE~SG`lwpm$$G#3%7VMLc;7q38Z(X9q}r5dW2w#uog@(c^sPh0j}hM`J9(J6 zX;xsf9_f4wq49WPYbS>j0hF7G!CfX?$Y*dy-1=S;6?$`^LQ^0>xM=%D)CMe%b-P_` zK8kumbG76|Y{=D?;HgeMnDpyz;E`0Qj27RmIz<3!1UuZ^4V0IdpPpJ=aQ}_{Q8#`Q z8VMNs^t7~mS^Wlv)%_*+A34*x+y{1GX8tU3%=DAKq>FjXgl*%Rvo=L-1+8~;x9)pA z1%bBI0+e-io%=5wZ|n=|R?D2TJ}M@tnSVXzUj&JuMmt|{hu;mAUQdXGx-n$eIBD=i zs%>W3Nuw}dnY(m}M_5epI*+&X9Cb@C-1nMWJZM<0i@S-wn$(-rj6?1ZxuA=c{PrZt z^u<(bW5(Tj52uEy%}69qVAXptk1&s-Vgy8j7{4>MeI()+Ap%jr6&Bp_m!J%I+G%xQ zikir#qm7iID5RPwK9Nro;-72Cw-%FYQrYHoKGU8;4bE5J-OyERBwD|HkY-Ljxl$qD+%=HO^#R_C^?KD-!RfYAA2~&|-ejhutK78esRoMMwH|KE zwdP8tWFBCXVg}V4M}1?3v<0lw8PXTXARw8%tC><6*(}mrF_r2mR7fW;5(7{n2R+k8 zYC7qXnL?$b;WLkrlKYa2eU<{m?e&OVt3WzgQN1_Hu=(QSZS^B_^HbOmUDy8&QebZ| zHwJ8FVRmB9ia*Y+Q0EgGO0T!L$v+1a5LdlX<%;`FejbiS(+d~f($}c4QN%YkVqulqX805hgtlmWnA zjUbvaag+JG#oE&f1|`FvsaB)&;N@1!xi&D)FKnNDZgB>I_^W9gxuq{b|3$L zF#dJ=@w1bs13Ahl;3|U2EK$Hzj4t=+Ujo*<6h|6i@z=hK*j!^bq7-T*QLI;{h$)vE zzU;h>`V84AJz{%H1T|SlvXS1fC@k_Az(- z6NmhAl<9uW{S>={F8#?v{+bc-ilDryDBz_Kpv1`G;~;Cxi!awyXohU5b3=Cz`McL6 zM?xvpaoEzH=g#+-h)c9@0E7h}N0A%CQ$&R2}4kytfy1u25) zMhH3=-0$gvEwV-uIR<5|`K`;8cb~2mE|iYdB0h8|8K_3)MqPpI8!ehZ-p zHQZv1GRA^WyYi18@|VMj<%TmpxK1tH?Y@uW10^$FD5{iW&4QzTJHqg__MbT9Q{=>t zPP$W{I^=gQg+ZY*AdUpurW(+r`F=J>XXQ7h5DOVnU9k&e!xY$EvMAIX)THt9hT5-P z%;kWX1xqs`JJ<{(BW`h-k%wE!!k!}gB9g>uBia4VP9PiH_aFW#FX}!u@-^=li@pyO zTS(T%r72|G*xIjoYdjzt7TCG%o?7=cuXhiI|69g!j2rYtV&^6)^ovOf^I0T$d~Zi2 z$xbFiy1aB06KghN7T|jnJhJ^s;5OWkZTy+kqq&CMPAmSk}R%I1-cFx6!ZLgw3iK$%IATqkiZu@ zN&yU!aG~LP0XrPlJf5Q%A`SrQ%PD<%wM}t|7v>lly?hv0+6&0uSIyChYI9cC>{`Jo zNJ}V0*XY$sD%cnpiyrxm^@0{MCYIm$Fq}%wT4^k?lfe8ym3mI3?+Fj_6WfQ0U`ZkH zTTGmWcdf`L;s#5V3HMlWM|~glwEY zPZ^YuV-Dbd#;6BTdb}I>NlVI5O-8t;{9x&NK#y+)Y&~lWuyDiEZ zk><;65SC>3>AV1=N2?{%ME9DbW+F(1?BV)_j63_$!+zJ2q~e;W+z%-ET7N<}gyv#rHUGF{GOs|gD2QfVuT1wWT74yN0RsSH_%?McG^Qhn(hpl;dE zU|x#mlabuLWx0EipN;&iE1YWg%dTg~)Bfj{zOUg2U*Zptg;$4{EsGZoqF@)@e-!so zm~qP}vWH?)-2y_q{c z*irkMAKtNSS=~BsgqB}s7F0VEUW%Ni|1))U$rI+2Vf&LxM+@v?)`Qw`8MUQ8yWyB$ zKX=7|G9}qxruCzi)S|s{(xmwU-8GxfinUlyZ0-co@;l20kQNa({IVCf)I8mt@|P0G zL}9_+%X|PZ`2bppi`lQ`k^0k%Gn3~DkJce>*)7X~on+3Fnj6$kvWxfsA9ZZrS>uH= zJ2>rwIK|-66#XV|YDr~C!bem3hvKh_KGWl#OPG_?UP{*Q6>5c&++*>Tm(h#-;+9mR zuigqHs$Cu=CoCPSpZ$?28HT7Qmmx6<@@y%1^)nK#sM3NbP}fX*vALyplzcQiOZyU} zeKA;Fv?UTFv_xs(cBanrFNkm1k2PKjc-tu|X-W>V>pd9x%p%y_!4-SGxFX;z1Y5T} zveHZ3fFA}`DS7@9;0_9^3=e1ownk!SfCLR+@+2=O4nGF|!D=nAsO~=v*q8qvWW^RwUX|ONnSt zbCR-I|6+b4hJ>?VE75c3F(`#tmTLc|2oX+;qWAih!B0)#5o|K}-9aV}@-ZAB_=GB4 z-1a^Gu3)LLepwYEqFYOU$$m!hj#-$M&6XmwC5IRifXZnR_6%afj4n(|Y|=|tiUrtS zb0ocRnoz&%p=4wDk5R(Dy*tjc$+3Dc>^r;!k+7r!8YksxV1WC2 zOV>M^QY~%pmi##t%d!^@L}I`DD^t^2wOqL(3Nn2fv{OLYaHVHquvD2ROpIEZM3fN{ zmMIgRRv~k?e6C#1XZwIkt$@0k zTM`67{E>jue!L8C`fcM)m*|Js^05HxLqGOB0lW}>eu<_%6fl=dtbl!ovh75|26Iy9 z{C6_LOOol+RPtg%USb5N5)tFHx)8rR#TJ%eXZm#rJu0XTpkKS+<{QHlW>n!? zKL7(^YH06hzyP%SE>Ef;1W`W@M(T_k=;fNJyP4j>(zTzxUILWk*&yg&*FRC?5KAG8 z;GpMw1Td0M4GFNjk{;!l4J2E)to2einCTeLXgBLdgHiREw$=$~vMs*o!tq;&YRiX0FQLWhZk;BG%!wDdop8j4a_1*9&-N zBL-KQrtSN=;HF=X?rq9>_!+1((#N@+(;%LNkBu$>_@ewZd+EwZ;@mY;%4$dUMNsI@ zhb^ye4e0(Q#k0X@GZ!bxqQ6?x-0jgPAK1u)N22#lHIvjZMZU0evDIBN+2Bxg9SR$7+@LcN`89WQ86=<&~@|z+e;vv$1)PL>O zUN0#D*NT6I*RZ-Y3EN;J@zS0|V{NFzL1SBg)y6UGu&79R-VMiKAkOibu$;q0j{;YOtA3G+iPeujw`G7 zt*aXfFFtq`hF#+s_PK#S(RM-XT!4jz6X7&y9CPza$b5FPIUbA-&)VAn0I+(O{flY* zYTQFoxZTK?+=9w1s-x)LXA_M8hSvpEQaEIsjY&GG-skom*Xsg)X788)YL6w%DXqF) zh_z>yEQ-;7lY4g4^5^aJ&RfCv@Q^Cz2l8la{qp|hAq&y_H*Dx4%}f03QWr*&mik0C=8`B0t)cR0kZz{aEtYklJ&OHEfYR=MQu4zo z=h4ANTJ#yi0dZvhw`O;p0iGEtHn`(hg!K^sXxbCTm|_&@2~Lg%{Bz0XHt=GRde6V~ zU}=p+qHxiWFjNnK)@yZ;)zV8@3<`uv*(1*dE0e=V@-#}~xY~-Sd=vewHnuHMlvIq` zAmwCL_&JTq8=JSV$CnCl!wOhAgc%Td4fY?2%irI990(PamBEIv5QUm$!VCrPJ zHA(tgp1imWEEo`Sb_wlP%y%O?FZuS$n?pCIz6fWyRUzyDni?^hh)j&}|ul z<&Sf}b=LDcNPgt|p_a1noKius+MB5ogl-h1LJ*qD%qnonVW}lVX@wT0R(I;0=MU^O zDPEt_w2z<&!Z0paIAB2yAa@w?cy8z=VsN;yaN2cW z^!!E&D_pVAve3fou5ok+Jr!h>)~rUG0=`0WL+E{PMhlpncCT@Nllw=u zqn&~INyb6Efvn%aXB(>rk3rUQckK_}^d{UNvF%v0AqmH4o6vK3uB?VnYxtW`G76ay41|XPe z)n$ZjP~!zNHq$JGDKEe5dO(i`4=+7qn$H8h6 zXXK0$Lb>fQP9QAIjlOq_Wma=HW#ql*qtr$F-0`1JfG1RcVa}GWY}B=gqYcD%;!mx4 zt#I5TFzbm&T6b6;QHENMbG7(oEfKw~CmE)Bo2P0&COW=RYP;4`Us8VPi$Ww&@P&G# zi={K=zWN^$e$pj=F+q+zr6owJpF9iiGUx4XKXGej@p;%Zgi#Zy-AfW}tIQuuq1FgA zyI=c{3G%GEektKM9%O{LSramAF6wU0lR9F87We{NXWPvrECc-V5f!{8l+yC3z=Su? zNYLC=%KhjsC;UG5RkovU@mCW5uBRx-%z6tb|HiO&FqKIGeOdDLP5k%a^v>ZP7BDI$nUBhb$e`u2} z4V$LREzC1Sld7)LMCWbP&7!x=J=P%7e$IlL4!g&QQ0XR~)!vYHzr@d0V%=$c=%~6H z_0jX;K>D~C4({p28OwR(Ar-|B_Q9p5srpu%xE|ruxqLAS3!_icpgJP(WU-7pTP&Z{@OS5QbpG;LENtR<7w{4M7sag&et zC&>hXmA$Eizq*1>dPemK?Rk_Mzi^FGU6bw$oIH#YOiPuPe%)j?wV zXkaI?_0a78@qdu;u~dhfzpXb{2G9pV1wp5=+`?=Dv-uc8#3AULZQ?H zJR$*_xxUeCV=mK3BL7+{su1s)0@l76+Srg%OUUs!B65hRH3*%`-z3M~=!cvL~z_3k|{0pUSz zxcfPFdRAz$J?Q&l*mMgvA^SdHi{@cn>pH4Hi4718J|D(0gkJlGXmW89Gz9}G2&n!_ z_pjf}#qM|5w!3ez1y9?%$#B+qW-qp=fMa?Tj8S&Y-J1MC03UtY1Sh_ILBrQ;+-8^M zJ_rfM{F~~RTL{s7xY#Zw3WY<42BTlgt?ocTtXl$waz_uxefYTyp%U|-5;rS>1|(~X z<^D(A$?pP;tSK;f=sD$>EOFX{2VZk7@5}gWMlJY8vVv7`A?8E2nFs)`x{mDLMbI0= zcWji*w$A-5_jL>?()7w4qo{?1Zg)+^0n8zK(il#w1djz5d4Gn~(Gj+-CFzoeAOH>o zQPM1uviksMIsyh0`o)_q;<+F6l4~<_;vy!+ttXC}+ijwQ+AWc=2XZ{oHO_>wG(m~V zK<4Nj>;Wy$Jdxa0)(q42>f;VW+S3J(M7>G6O1m$(U->}BPr0wN?QuW+Jzzt%NUykk znUgs&#v=z!5LZIzHTMlJ*t{7CB0ZKzm`VcL%FK;`I9vF0g-BmX#`Xg|5`BnB^+9*) zgBibZ$!a;G#E>ej?^5I&`4i70X4oCn#JO18A44l3Nyye8ml0nSc-JH0& zdW9QJBOm@@IOC7h-T(gmEW-i z-3lE?xc5=Qla4U9ejPLDdHC8ZT)U38vErhqY9leZ!3OANkOFV5VMP%JZ% z61A8p&}FHRAm6M zRmB;GM2u99C4FbX;tDnySCj0qFPfNkpMG`RZ*kvY+o5boqw3uZCW~M5d!NaG8!QBh z#7>KDt}%^A@gy_J+ybz2U8uIuN7p#%fsB9XvNi~5Bly1e2(v|Eh<}W0WXMU zg*20fesT*lZKYD7DW9Q6W1&sOYXA~zN`cA@zHzbyHc@6J4v&FS{xM`3Ad#`n^rRa) zS_&CT{H7`mdU{iNS0?}7Isy~2>7K^6JXwcHq9du-n=f=0)6}EOVAXjq8T!r1_H4c@ zKQNZsevryMpLqmXg)z@uU6vv0kkSyZb^q)${`thxzdBX(_W!`1Wy_);GLMP|Wf&Xq z6oz)~kFA%>m?dtbMeP$9I%F_XZ~EjCex}|;-RPR0z}I3IdGwn+Esz{tNoIDqw?mQ0 zQ-s`^Sg^FjVrWIw3D<`1-5k`LxBH$j)nKWMN5qqHe(lRC-FLCUXnIujuD6thMR$|Lr;>4@Q_IM_V z6DvNk6I+t!`)^fKa%Ol~g{rQqx8C>OeRuiqh;*u2K9q3#xfn)u7Ta34o#%?ml0a8N z@ldCiA+1IdW^1HgE37tB=Q1B!bS@0G$~dNkCiGB!c7_~$8OQ*sY2&hH1k+{gI3zC9 z0;)GQl~Vo;zx)k$H&Ih3Ut^|yc_%GaGtS%c z`C;SgbX6r(0j4xv$DJ~vOBH*JW?s6!A9XkSjv2!{SCv}NnIgg@Df;M|-{CwdU2Qrw z{YY4$z?4pRr&ucTvW3&lkx+yHI5VO#?(UKrL_(Q7T9}YfMExp~cXa_2$g&GSw9uwn z?A2S%`w2WIw{LwsiQ}cM@4C5FT8>M;t%2@uLFtT{mjC81A!xD+; zrHN2va!PnF`Rk9KDGtE54V9FH4n+Hg@y47f%xj~IbVK9LuB()pUD>d+t48MfV3^r` zk`OkmG1I)Kxi=P%#$acYaMW*_c<99&G?_P|oX-eqB%03ogl9=*L%>Lg2J8-N1|>?G zr9s!sXZS7TG^=CgwX{@6LUGVG%maeq!E^S95owvwWN0I3pQo)==QC+*)d=krpBe-1 zLri~=Lq{kU#B%2odb~j@`0!YeKxHTnK$DM?d(}^~2`$5T@Nrloe#}{?^#3AD4e@T{z(txHen_UWNE~&TaU&Q2!pt zX=;L7^Ewo-!>qWEm+oR~U%0-Dt5y2uf=+j9_pm%1VZSUU>KJ$1B%xw7@0g4K40VMO z@`1Ux|18wC1X?u7|ERu{FsV!OmqI<}_h<)p@WVzpZ6X!See~xccw=XH?pr?(Eh`J6 zx$*n{*Fp_3i)0XOn)}deq26jgtU*@NsN2lv?GRUI=W1RLHMfL6|M9~0^W0iQey z*0Mfqj=bb=y%BC%Yi#@$%67mO6;V{-CfP8ag8i0A*<5>5PE6o1nkt{ILHzRAn0MDx zZ{TtDYn=D2a^y6KWG1j{6xVS$CtpF|IH_o{y57vm)nCWG^S2y<=l|f*BTjp#zgI=f z70AOP2h=I`W{Vs+q1Sp<$BsBy<>IjP2v=20kzD(%w01d@kthgk%uN1<@mB34tvo!d z_I}C-d#VX8t7TDj>oeOgZHd~vO}8IGL^H#=U4U;?&-Q+0#@?x6?)AFwIO6nq4|3kn zqMZbGX0Xx`_(g*=KcE`*+Fq^8`**#S*Phg02a9rnO%cp$u$D7^O3~pA`DsWMjY(Y~ z$u@}wN{qX^d_Z>MsrxW!@>^g*f*X`YXnc`)?cG3`kQ{ZA1PZJ(IW)=wd5d?)i6c&< z_fgIb)lPH-b3W}FO;WbeP_|>D zoq;bxuo*jyUQn_IHCDt8$#Rz=T_}sNHqas3Qtd!A=^HOg63h>^s9^~F;C=q&5vLnB z%&B2n35p5LVkko~jIqYDlGOA*F(XJyqw9(!HKTHo7#1688>=cL#Qr)75h)0%sCc(k zce^)SI3aIp^DM0@VzqRrR7s*Qd#8uj7dmPS>umBa`YI;)8t->IU1#6M#WT;6Wp; zXZVOOvKHHn!9g*myq1lf-m$`vv%>oVXGHj=XT8{?L(Y~e7#YK*mvuO=om#?a%KHtT zE%*MKb2C~k7DQjyF5OCtl6|#(vUDr*h$R{ zf$D3S_weIGPA!|rOC#u5H2F)s^N{xnKR5J8PY3or`f&y|jBWh6%pFdtH}R`OP6Daf*>SJuowzkYcVlBFwe6Ufr22a1QVhv{BK6V)1B(EMih8Ym*of<<(A^S<` zx6r54O&XW2VH7dg^Z46as&lox+D)LCf71fj$P~v+BCiGDWpm9kUr$w3EhoTuWx7c!e>REr864X( zt1$#<&OUl3Rk0`841@t#YL)5AiiSi@rj;n*naU>Y1kwpfwX5S5RTM8BfBpptr3sUB z*cr%{r2mZ;OhFqYSQPaCDo%^rPLej#|fSy|d89`JG?W(!Id)8^5 zbDwkCnj&RWW0?0?$O>P+fc>I$!Y=aKxo4hp>gQf~&S{wY&T~%HxD$uJ6i;T8f(G)P z2_LJlJ`{M9TroZJA)sm`MGuygbd;FVDn@YMh#+W~_GuAqwz_!r`U`1M+*~`i`~&29 z-~&$6+&j3+mR@9{0tSjDOM-@tbA8vHs`|3&F|13BD~HVtV1cg#@0QA9X6q5b#)NmioD`f0XuX{T-)avv{LoyH{u;+!9vW>|Jgs+)pDkGYE2? z?jh>Yj5dVo$L8|6)O}9Z+}it`HFe?pS)WbgQ4;OK3Pk=snhU4qnx~wujBzuX!Zv8J zsGs}5l+&}6DO2X~nhvXIr;+h#_!-l_{8i7IZDe66EnZs?lRGBW`?#S5i#J_*)N$6S9}6tOR1cT(h`SE4qUnz$;~L8JU+G^$xgax~*; z_j~{2*9k%Gd;E)oUE5&WR}?$U8#i?DSH0A4ko9eWJYOXzu@P(-nJrY5u^V#VX>@bw zqBY+J?722evI0?K@oK$B3oOZ-t=H*I{3hE+MDXSTYMaCX*X$!()pcEx4WJ-W1-ikO z8^*cBB>uq`uTW`acFG!ix{%zismY~lGudUB($%G^nseFO7LZUYYLMyzt;#kS`}L|^ zMW=A&Qw^-?Rk=ht-{djZYa=XrrY@IFbYi-fO4f8X)FzYZu5=^8X8;4jR4s~Ckq#$8Ty3jC z*vl8$bfO|&6HhO0!Z=U@=PF{K=aQL3ygXA540#dTUp0b}dP!fNTLEn9IXgc>@c;5`AU+(5q6L=fhD%m1CD+4g+6r zf@!F98U~f#E5GMD>*#W5pJ2uR-F0ekq-C^%RTWy@8jYiv3Uznyu3^$(%vLL?x`y>v|7yC z@f{duE@&qk6kxpzX3#h-qx#+D z^?%iM+E^d4>x5;{DBXiP-uo~=cOrQ7e$2%!-d%r9E2LS)EZ&rrW6=8uKX$g_m?YRB zx?ToyxkXy)WY430z)U21#=H16*IA5#&;tnL1vhGCYLcY*EyQ~HZ(S#g5D&`!<&_P? zwj$l%j8c)spn-&2A||)tYMmSkE}RxmrCGfzAscv^zw&Hz1mqNdl@`C1^CrLTI_)?p ziLS(fR=0{|5;`411+GmrgaDOfGBcVVM9a zG4*Jyx|&^JJW-j#h4~m$JmyAd`zo@JZo#mdSR$FWn)LJ86KvJup%R5_5B-X}(aXK? zj&MbenC&)Q2Qk|-iP=?8zSuu|?~^aCTtTGd{u^d^2&LBE*qRsC%1s+~nfXz*)+id8 z-TST=Z*EYqUmiSmiFPUMBNAL_bs;C?tE=ta8wXw?+`6IYTEp(Pc)(3s%`;^^r{MMP zTe&(A>GZt$+K58}_4SSdcZ<+F!l8kH$yg$Ir=^9Q>NI2l$u*6kwpX%TZSj*bW~@o#wj+e6$LU(r z=k!~iwdmRQ70L&1)HQ?Tq|aOR3i&J1<-{MRr4(YsWTKmlGuTQP^)-I6G236)PuiNe znu#99&tfaq5avCo7ywhNe0br06}VA4>SO3Z_(;lgLcH^hwlY^NNV%>$Ls3GgVu!1s z^i~aGX7iRx2axnSuDs6>YW%pjoe1G~q^vgsambLDCH!~S-Il9uPS#uGZM7kcI&G*c za7n1GJ;n@Afx=~x)N$i^oAtQ@a;)>)xv7ok#1xkTPVKnD+jn|{Q=hlE+6Dv=u@16s z?YH@9i#59Hh`a3?k*H5@t+H;v$wD^kA;`)U%4&(*4|UUHWX0?gHgjd9iM$h#&rw>g zKc(CsM&T=JtoMcp+Fj&nE z%|#6f%@%b7#0%wZDG2INf%MbCToNgxmEzvO9e z<>xjy9ezY{b=||FRhR_fjdOdmmWi1T<*`=t=diW8sIJq9S{v^51Q#b4)tMmTlukbq zhn!Le8wd(TWyIwyu_o2`3~$;|6FYd*!5T=~;gEB4kKJ=4K&N58Q^oqo| zs^rcke7wvb#$4@H?kAZUj4}|@vH#F(^}?<>oDtu!(^^FJ7`#z8q{Hjhu7!Aw=rDbi zTFh3}og!A-YhN*;z>eAGPrMWb41z_mkh8KFlty2f*Yo-&r>4S&cEE#;(Eik>$WP5K z{lrUmcprIVlk@8A*6?T7d6UEvUw_OGC9a`D!1iHQH(i!HT5EO1Yz5)zig@!36kRQM z{K(?EUKw^ypANplzKeIYa9#5@5KSCKlT^IG&OFZDoy*Llq3C2nEWD|4DZIoE-?ug5 zTp12B+QN$HJ#+sC4Eoq8`TIUPC9sdbS)FT^qMJ1L++w3jCE4dh@e{YuMC(ZMmMC#X z0}uz6%V*Un>WfS<;<$|j;6o=yN44DQ+4@NA0(RxbcS**VKOBiD-XS7CRi z_Z-5y!W=-YvL4<)nH!LAmd?a zP|er4s7vY<#Yx4cdH<+Zw?nQ4-PHUt<*oav>#U82r2=a7Ugc&GR8Ac8`9M{@0>FQ< z+WTE|$5WidTUuf)e6WHT@LeIDo3u_WY1O1sY1>L>Hd&Gf)OXm4QwDq_4PM({BHV=7 zY|Y|T_$Wh;K&J?QtWQMn>f0q(}AM(?5qJ&SQ`%0Uq3->frXTOsB^h zs&Rr#Ag0G|oCvb8c;SXO%D%s@Bc27Z zE?b|jzzsfL$7Vglp1&QxgnVCx#NMh5|J4e)!ZX6(+1Uz`^ zWXmEimGJ-7l5f3hTjgx~*7bj!e>74wB6&QGR{mcieZ&9x<{}sQp2Zk;4mw7>Sf^tIb=D;=M_xOKIwOA`_{S3%v&7Of)i zCF5DI65t3D$?I}$$UQwVfyb7Lz35CRhK10`uqINgM+o5?@G<^IRlhhB^1|e6dt55u z7c_fHmxntroVkIZXgTFFn!}Y*jokGy6f*MC%h5c8%1Bq^K)*B`6?V&w#1jafq&{aV z&{MSLzig7DWD#peN8hUT(`GfuF&zf^&G#p;G$;h2kj|JWP9@4`3_)PRe95eg*h!eh zmV|YBV=JgCNPuk~)IAVopyg_}qyn{2+;d~+nHhBl@*H>&*N5{#;jJlP_9q`sc>nC6Zg1VFfV5Dp{Wjkd>JFhC)dF`vl z{UvY=R08Wm2~eIVhHns-)|yz-WH($*=v^U-TK-)Cfk{eb)vY2B0EQ263rgo)$Sk?4 z3s1yhN`ql(2niL(0rjq=VjWb=)3KDrOxE(6?nljZv9tR z%FXincHR$5<-a`~9_ESetK9JE;L;&xsg}~berKD?0N71>`x1inwE!-bJh9>kEJn8v z@!DqF!yM*{T>~HJ)Ahtn7U}4EOW;81m#k5vV25!hhtyF_kg#cbkEqoe?+3WNFB|4; z@ft9pf{{#^O^Df?!B&*Eu74#u-_Nc-YP9kudoHAXP3N{sunMb5%MJsl@TI(*` z7q2mgO3U|x7WHyvcn3E6qM+>>-TgqnO`RTxN7QY!vJ}&aJdz?95w-jo>3FJ{YDVrg z93IO6(-1**=y|==KO19Z>;2AArjs!rQd^bna6mE>?&C1&?cxW*hLE$0P0S~PFZvB% zfc+8M$f*-9oUQ(lYTLtVF#Z4mS@gA%J1rKL_;q0f$JY<>1HnK<(z?7Kyp_Nc(8wnT z%N;rz569&TI5IqSTJz{0UTlxz#?7^=GSe!_)J&Mm8e_+9laJqSv+6TU=oRXg9S{+X zyMs$8XL1tq({g-BpHtjvael<4mi=xSSbyi)ida|h^b7$7g_)xwt3}#= z3EuVkO{!HhKog=5yNQHTpsAeIG>+B5*mOFeWh5?i#Wrv9LkFDRowoC_5lu`Uv(OGI zU14U}mXg1>vCBmoh3nY2(W+b-W$yGo*AEWr4n@x+<(+gvQ}a>V<8^@BFnuqY7kgVI zD;|3%EfjAk0|EwKLSzkai-9U^_x@@?0H+ziP!SObc}4xPcQFxKXiVjJ3tX6BsdWv< zpb1Qu!^FAP+gzRl0|>v}^K^x73Em^4aZM3pwpHy{oKd|?DKc9KQ5#q>+S^CN;mP2` zJTL~+XM?P+VC(Herz%Z^d>7#yjjqayIH}hUQ1Q|V3tNqRPP~OC+)QKGxvU#|n^*Wy zMD?I%g@Os{v6utSEqJ5K=5$_e1*Mm?XU49o$@t=4Fk>m(VSQJJm6kWU;RoTxd9zRS zQ|}EMr)xP0GWDz>r0UyR%0F%ZE$W^^6BK@d0NP@>?Cr&vg)lyO7IsQCh{`J}Y!Fx} zw}j)qQ5_Q~UugOyPNgR9Xvlm2yAL{PgniJZ9v}lAJA)y-u0iByOk5PJq@f>mOwX<- z>s=QIGyTrZMl^<}wOh0K0ZavB%=BbC4Xtui@%;-!Jxn|{t;J1QX7%<<|bR(3Y}porEH;udYOOJR4d%@IcPn#>0EY!ezA>+aS5RnlK$;NcEhOH?maU6O1Oa# z1&WVhd0kbx8Y(Rsh7EcUP|wpX*0m*(a6h|KyT-HrVlmDI-|kiE%qDT48nwaJQL7Rv zMwVIormPt4!X99W!H4^VXgTTEP+y`5#pb{-jObCcW*?&gpfQajNZ6>VVsX{{rKfu? ztFziI6qW%$@~UORXs{)~y31((q!x_DI;|A-PdZNCe0waDUMF&8T#*HA5d? zgmkBcZt_Ne3(dBTDjkO4qvI-$(Jq+Bbfps7!LxO+WH-Rc^gUtf@wyE$rDaA>qTF_+i84X>wDw*gWo7_mzqH^2uJ(Qj}dsaFfY#jGB(;E z==wJ>1={M(Tg&#asX>G?T9_AI9#v$0rSq5kYpm<80v$VV3<=Vq3;xgh!lme; z|D#hFOVWIp32vwt*f3~F0O4}auvBkj7Y5c?P^ea$BJ#X73G1E@ZB~7{ZDg0Q?;l~= zD9ooomJK=arHO~#(u^j6c_q7%LCyT-*A=dh22#s`8#z7A_IF z$94j66sAIk#k^+0?N}=al1w-GP^YZU=F{dz#fAV+EbU11b;ZF!Paw_%B5Z6{WJV5F)z_~$jK#*1-l=B57H?~4+w;vlu3JhSyU9N%8@@Gu~e3h_Yg6uY`Q3@L&F=SW}gZA^)P6Yc~%owbZ?#7~i40$vU z}2$Y!s>F_EdO#kPTNVpJ;Q6aV5GTS_D z0SiH8AK3@I0zTI#U|cYQs9G3=<^azXaA`O$#vj z4AC3!o!;)Z6Flr&{VBzw*q74=dRAX1E$+2?R%wimts4snqynEyul4UXI<+YYZLM4n zIb|2Tf8n?GB}O)=*Z4@~yF=BwS%utYBd{I*Qci@|^WM2{5h(j8jr0~@O(V}k1|whz z-GiZ$MK&}Fv@Kb$66*p9L(_=5zbOO?Fk48;as82-^0pC8u=4J*OA>GT&8NZuz^Vlk z($L+Q5;734J<-?%{4nt81tU%@sxapg;*ei)6o;eqkcpC(>#OmwkT>$)Z+&m0^Q9KY zMW{!IX?DQj_CLCndf)xWjm{t&I@Ow2E^A5wiSaC`$qXfZH3=_7-fAmmNFojw=1aK7 z91MOlbTBN+hEpyYEIEaGPAr<_fG>s6;u{*?X$~ zkWKwD3lDDXu}3d8>$F1!nGhKfri(_%r+-} zehg8MFZ;KSYR9*Q-3mHUrZ&xqmrw&TDQdVIJi}nts4g3GO=@Z_vQ{(wQk_|S!wIbArmvm{%3s8z-!=y^sIBGh3`=!#Oii~7Ss81oW*ce; z1fZp;7Hbbj&fqF6n&R#hqFa#^m(6%4;dgKE^&Qeti9i6A30KBL{$BSoxKn=^>4%`k|##x?p=_S&#w#E!_9 z(VxcpK)9b7osh%43So;Ag}{X#X!#<=KA>ph?AEPkt{|l`V``(6sA1HVdQWtxo$4;d zR38ECR_&@L3A1UE1)iTdV4rwTGm?%iNjtsAi}fn2P`x&^MPsN!a1U3}C^%tQ0EA<0 z;a>gMt`=`}V`qd>r5r?FYZ8vXHgk=wo7oA^$GpE?;4zAar!}OUqryLhHO^uPR7=e=)!HJZ(qnG;rqUtrjk;;4Pl{C>%%O0DKiHB& zA+G8xf&KcZO{ZNNzm>K)tGO9m<3wGXdcZF{OJ<<`mtTCg&<4IPOpL`ZtrpQP#x&3v zJiguLlwtWh0z9;eoyhQ0y$k~dm`A^Pf0Rgra`Xo0nq_nc@?hgfl`TOw&oQ^tkU=vd zu^mTNdx>H0{qv6i`SCvXFDU>&!tsfbdvQW%(PflrmcAgS$wFM=vAA4i=H+7Oqdz*d^FP>dQ^tQ@OO%0LZDr?ZzB#6J3YbOkDt`fht z>Rh@%N2r!$2Fv*@DsDo@WfN5xQ`Y1*WgFs|_5=}El3>8S5Rixolu z2$+w?&YFQQu0{Gu-QdI&1?Zgj^q<6>>Yb>uEoj1x$BSho76U5sEuZX+5-Sh2Bs)_X zUsw?DbXge&vXI5IHQvYm6bqmFgyhY#Yio#W4cFC0->Jz=kGxHvi8=3dqKQe*dokv$ z#*&2e)_F_+EatS;xN-r7@_eiKW(jXGmWa&0`pGX;gde-xOMW)yyuCRxJYwF*8yQIj zx<5L3X^cqiz8Uyc?}fQEI4CmAjaqe&tj}Chu_MJqO+r~Ms zMY1>zps#P}whpBwpLKdK@@P5IIMqW=eVHzDzt7~6MYDWuV8Iu248mH)>hXT(t1)K~ z$PU_0r8w!8{xzM2!J~>r0^_B|XqtU{%DbJ1E3sLx@?QSHm{Uct4{S0|dmrZKtF73R zX*UP?7~cr!tq4K3WrbEJLNvo2UyC{Wy{~hg1lt$z7^vSw_50NMtj1@(cl}+=sqj9| z8S~@F_&s6}tQ>8iU+8)(Z?0se0KOP$lL!RW5T;*RdSpuafEy)Dfj)aSuo9b$uoWqq zY(6ArX}POW6WDn>;AZ$;8Tel0giw8HW@e?V+<5yK_6pE`;Ms7KmhlIZZ@~k-TXHv8 zY@Fz;zXe;>U{N6`jvT|lw;q=nykFE#?}xl`ySM#EF{g5?!;TdqSBZukL{Arq^#$Q+ zJ^t0J+1P5|L}Z;;Hg-GCp$pV<`SH+HXSJeB)qH$JTxCGtRcbF#Z8 zB`33`Z^y@L2z{o#kN+gb7A(RfSM(9Q*^B%%<}6L3|7I04i@vP)BtL=Qhd0RIa5Wf} zPy>U-mH!rV4pXeNfVyC-YJILHzgDLT?{9d#LI8)=|4tOl2AV_5(pWXaeJq!3HJQ16 z6!9MA4bW63yqCFX?STOw9UH!M#V1c7A#Xs<&9IdwFLe=P5u*-@@r|FwoZhsHuN|zl z-?T@)lRsz7fWKCpH0!*V`K3L@4&78t>VVt4bFal5R5%yC_i?c_=^L*Z@pgHuUT3~s z4!D3HE{cR?t9Ox3!nDut+A&N#OfO&~rP2E#pX|z~IvOe~Gs(Ji)s=X>u%W80J5%V) zW)>4uo`tVATNf{{i+8mp!Cc2fAfCu17pGY2QgxU(B+`JgH&@27@LHYY1^l^?JtAeq za4cD<&!i4loUEt@VGOS?+`clE$*B}UQp;(?Ev#VjIAfK)P# zci=BJkWPc&g3K|I?IE>n4!eu=^G{<&Hff$=J|K(BGArcLWNF{&sd4Y@8+2km;gsH@6Hx9K+DM=GL|)oJOPWX^H2|sBniH9z{8=F1jD5U$N#k!}hrlNMF5Xqc(Bo zTWwSoZgRC#GnZfy&_)HP5Zpe4LIb^<@ZcluFpP#KrCvLMicb)X*b<&sT8s4AHgD)i z2w$eFoST=Tla?sjCm#X|JP?fP%QEK~rf}vOm;?Z2j z9Y?yxlu_e#-V$;~h#2{RK2;I!637@sKP3DNe?A=cK7VV-`3z7Ogo`9^YONO7$u2iA za&Hi=cP7O_;QruXgX6zKu)a~=(F{=Tee8~qGmtlnSO%YJ)~n^E-uJ{bJ8S(|3i{{i zz=2&e_!KTU6JXCUG?dOk*OB&{+0OB?AS={WJ({6cn6!()<`?K)i;lRNx<<+v(-c`O z^+2RKETfFj>FB8@;D^)Rhm*;zj9f#VwAh%zE57k%!=i zRZ()>UuCn1`eX#3GA2)J_0_Skn!?PLSz}?INK3VM*!7%)wswhD6p1a6zA=Uia!{U!+!*jiKKO=s$pLTaF4}@c_7ZD9(w(BS z^^gGIZLL#rJD=Je!uDe|=Qi&Y=bODxa;~5K^mktB^4e|+IZMM(>kt>WxvU~H-aqXL zIS0K{dqYmOm*>2B_UbDyb$G9HnXR{#L{oKNMJ4n2s%WY#l}0=cTl|iFjFw%Ll7K`8 zlp!W84oE2ck+oc+h&-?;^w<>7hO7?&U6~#h)QGh@F_X>>k9*(T4+ZRUqmtZdA(y#7 z%PO$kw1$Z9ByP#nQf}(pT{hQz5onD;d10lTbwjB%+uklYfH?xP8syv&%AImH+VKihsc|A2$z#2f*Q@GWA^ctBP&Jb#AE?9L znPAbMSQT=%V99bx+u7?a7?CWm$&~?J<~XnX(Z~Gn8)NVmQzK)vx3TY=z1LQUoW(sd z=YwN)!NW9)&~Pl&MoTZS$aBp?yLM+eXOKFBp83&%kkh+6u)F2w9Z?a>(%73uvf`b^1DL1Q67|_GvzRrY zCbOXsURP+vrdIFPH54CY0l1BsiOcZaHo-n*28YEixEe)(=)-!LE8k31lXTHyy&0ZU zYC&y2FwM9WU`O5K{pQ+`GiW@NJsU6>DvkAxjyT^f6ul5b96f5wmF^sa`}8*mYrXfa z4>^nOOwfFWIV9H1rixqXPx-V5tm7V_Z1hMId%t#qZk)ebv)lxwLuHj1+E zAwY$MP2S+f5I9KZId|VClcM6LV>E)YNPJ-_bi8_PUB4SG8X0TEEfxbE9aqwcummQh z@X{1PaU3o-RBL<~5e~@7^VFu0Q`7IVBr%0{`_M`cE>U4wdWD*;iHr}!^+XmjOz^;M zw&N*aVL-kiw4m1Z^>MeU2H*5VC!UQsm}8m=7s4(-ks41HMu;MVR#V|pvzfMXS;-IM z@(4Fm1tNO_8%`pyW9kVqDKdssIo|7o%_t+YNn*sMtFq}GxWp$2VpBPMq&nN1jn`E- zCU~{_h&3C0N8dRJtQQebC95Sn$a%gF5Q+4QG!EbL^m21WsKCMzE6NB(gSlA~j z!FiV>zCpjY$zUJEo`&aJ?*stVbD#W7c+tWVpijS!ndsC1yy%G~lXp6tPU>_@r@M5z zTc=^2PU|$H)2OqsWOB^;#)KDn@=wE^3rkv$J9}cYpWGW7nSEQRzh>bde*d^rSGwT- zXv}#nlgA8S|K43v(*MnplHP6(?C^V+a1dRmx2L3J#ScnKR=-qI()VSKuW)>oxt;P?{9=SioIqn4wFqne|NgV1=r`3g?u9663GM}`C6 zfL>7hdI3J{O>o3H$~a0nVjK|;m&2jZuaUv$$nm(bzcn!weF)3ebl;-O7&5h6@OonFX^E< z2k+uzny!cD>QOTTvDtS&$CZ+jCHM08FvtHQ;ct=AeO$Nj9yQMXkZU;N{-5ys8Lq#< zv6=gS*SbH}vfQ&7qh2-{9bb{-1Num;L`9B>DVlx4Z+h#3KjeBr{r@>W_#`*#mtWzaqAg6W6z4rf_F?c75MM0|@)G@9bOH1@k>vc>m1o_LU0H z!{EYivD+Q|`SH->TSHGZ%~q~ixGx9GI$n6{0?P#QsWpX1>SteBv+&^TGiw*F&F)^e zaF8HxtNLEAo&EByS$OK`?D_QzCuhIEexYx6^@fE`3=aB#@o?xVIJwz-HY{{- zKk&K}dL|cYoBh;=h1SC=`BT?eO?uaNl213D->VDWeOzL|*}uxaoOEJ?g9Cl52dSA# zbEj?HJ@FK)bGP!t1vz{^RY{`r8yEJ>wrpCc&S{PJj%uCSEN|VX?wP%|XX^oyHNm6QGjJy<>afu~>Gk#V9cR}J>9)USMaeD=gMFP`D8wS}jR>x#|Bo_%o; z`}Dqnf@iE2mRHnmOiApVeeT&8J1Z^}JPF%2tmJfwdKTV4J=_1>i{*&k5WZxHo&WlHvUdx1JzKUU Ql4~+&5`#EPVEyxd0V#=Y(*OVf diff --git a/data/en.wikipedia.org/wiki/Bibliography_of_biology-0.md b/data/en.wikipedia.org/wiki/Bibliography_of_biology-0.md new file mode 100644 index 000000000..1db580823 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Bibliography_of_biology-0.md @@ -0,0 +1,55 @@ +--- +title: "Bibliography of biology" +chunk: 1/3 +source: "https://en.wikipedia.org/wiki/Bibliography_of_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:42.724301+00:00" +instance: "kb-cron" +--- + +This bibliography of biology is a list of notable works, organized by subdiscipline, on the subject of biology. +Biology is a natural science concerned with the study of life and living organisms, including their structure, function, growth, origin, evolution, distribution, and taxonomy. Biology is a vast subject containing many subdivisions, topics, and disciplines. Subdisciplines of biology are recognized on the basis of the scale at which organisms are studied and the methods used to study them. + +== Anatomy == + +This section contains a list of works in anatomy, the study of the structure of living things. + +Ibn Sīnā (Avicenna) (1025). The Canon of Medicine. +Vesalius, Andreas (1543). De humani corporis fabrica libri septem (On the fabric of the human body in seven books). +A landmark publication in anatomy and medicine. +It is the 400th birthyear of the beautiful book which graces the lectern in front of me, the most artistic book and one of the most illuminating in the history of medicine. As Osier remarked, 1543 is a starred year in the history of science. In it appeared the two great works which inaugurated modern science, Copernicus' Revolutions of the heavenly bodies, which gave us a rational and abiding explanation of the workings of the macrocosm, the great universe, and Vesalius' Fabrica, which for the first time fully, and for the first time accurately, portrayed not only the structure but to some extent also the workings of the body of man, that mysterious spiritual animal which the Middle Ages called the microcosm or little universe. +Gray, Henry (1858). Henry Gray's Anatomy of the Human Body. +First published under the title Gray's Anatomy: Descriptive and Surgical in Great Britain in 1858, and the following year in the United States. Gray died after the publication of the 1860 second edition, at the age of 34, but his book was continued by others. In 2008, for the 150th anniversary of the first edition, the 40th edition was released. + +== Biophysics == + +This section is a list of works on biophysics, an interdisciplinary science that uses the methods of physical science to study biological systems. + +Galvani, Luigi (1791). De viribus electricitatis in motu musculari commentarius. Bologna: Accademia delle Scienze. English translation: — (1955). "Commentary on the Effects of Electricity on Muscular Motion". Isis. 46 (3). Translated by Margaret Glover Foley: 305–309. doi:10.1086/348425. +Galvani's researches into stimulating muscles with electricity. His theory of an "animal electric fluid" was later disproved by Alessandro Volta, but stimulated research into bioelectricity. + +== Botany == + +This section is a list of works on botany, the scientific study of plant life. + +Elpel, Thomas (2004). Botany in a Day: The Patterns Method of Plant Identification. Pony, Montana: HOPS Press, LLC. ISBN 978-1-892784-15-5.: Emphasizes plant family characteristics to facilitate plant identification. Used as a text at many universities and herbal schools. + +== Cell biology == + +This section contains a list of works on cell biology, the study of cells – their physiological properties, their structure, the organelles they contain, interactions with their environment, their life cycle, division and death. + +Hooke, Robert (1665). Micrographia: or, Some physiological descriptions of minute bodies made by magnifying glasses (first ed.). J. Martyn and J. Allestry. + +== Ecology == + +This section contains a list of works in ecology, the scientific study of the relations that living organisms have with respect to each other and their natural environment. + +Warming, Eugenius. Plantesamfund – Grundtræk af den økologiske Plantegeografi (in Danish). 335 pp. Copenhagen: P.G. Philipsens Forlag. Published in English as — (1909). Oecology of Plants: An Introduction to the Study of Plant Communities. (English edition). Oxford: Clarendon Press. +Turned descriptive faunistic/floristic biogeography into a new discipline, ecology. Based on his botanical investigations from Tropics to tundra, Warmings aimed to explain how similar environmental challenges (drought, flooding, cold, salt, herbivory etc.) were solved by plants in similar ways everywhere in the World, despite the different descent of species on different continents. +Gause, Georgii Frantsevich (1936). The struggle for existence. Baltimore: Williams and Wilkins. +Gause formulated his Competitive exclusion principle, through experiments involving paramecia. The principle holds that no two species can co-exist for long if they have to compete for highly similar resources. This outcome has two preconditions: 1) panmixis of individuals of competing species, 2) the environment is homogeneous in time and space. These conditions may be met by aquatic microorganisms grown under laboratory conditions. However, in most real-world biotic communities, both conditions are likely to be violated from moderately to strongly. Due to its simplicity and intuitiveness, Gause's Competitive exclusion principle has had a great impact on subsequent ecological thinking. + +== Evolutionary biology == + +This section contains a list of works on evolution, the change across successive generations in the heritable characteristics of biological populations. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Bibliography_of_biology-1.md b/data/en.wikipedia.org/wiki/Bibliography_of_biology-1.md new file mode 100644 index 000000000..980b4eb0c --- /dev/null +++ b/data/en.wikipedia.org/wiki/Bibliography_of_biology-1.md @@ -0,0 +1,34 @@ +--- +title: "Bibliography of biology" +chunk: 2/3 +source: "https://en.wikipedia.org/wiki/Bibliography_of_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:42.724301+00:00" +instance: "kb-cron" +--- + +Georges-Louis Leclerc, Comte de Buffon (1749–1788). Histoire Naturelle. +Until the publication of this encyclopedia much of the European scientific community thought that all animals were created by God about 6,000 years ago. Not only did this 44-volume encyclopedia contain all descriptive biological knowledge of its time, it offered a new theory. One hundred years before Darwin, Buffon claimed that man and ape might have a common ancestor. His work also had a significant impact on ecology. +It is no exaggeration to claim that virtually all the well-known writers of the Enlightenment, and even of later generations, in France as well as in other European countries were Buffonians, either directly or indirectly. +Lamarck, Jean-Baptiste (1809). Philosophie zoologique ou exposition des considérations relatives à l'histoire naturelle des animaux. Dentu and The Author. English translation: Lamarck, Jean Baptiste Pierre Antoine de Monet (2001). Zoological philosophy: an exposition with regard to the natural history of animals. Nabu Press. ISBN 978-1-178-26555-2. +Darwin, Charles; Wallace, Alfred Russel (1858). "On the Tendency of Species to form Varieties; and on the Perpetuation of Varieties and Species by Natural Means of Selection". Zoological Journal of the Linnean Society. 3 (9): 46–50. doi:10.1111/j.1096-3642.1858.tb02500.x. +In September 1838 Charles Darwin conceived his theory of natural selection as the cause of evolution, then as well as developing his career as a naturalist worked privately on finding evidence and answering possible objections, circulating essays written in 1842 and 1844 to his friends. Wallace, who was corresponding with Darwin from Borneo, arrived independently at the same theory. He wrote his paper On The Tendency of Varieties to Depart Indefinitely from the Original Type in February 1858 and sent it to Darwin, who received it on 18 June 1858 and passed it to Lyell and Hooker. They arranged for a joint publication of Wallace's paper and an extract from Darwin's 1844 essay; this was read to the Linnean Society of London on 1 July 1858, and printed in the Zoological Journal of the Linnean Society 3: 46-50. It had little impact at the time, but spurred Darwin to write an "abstract" of the "big book" Natural Selection he was then working on; this condensed version was published in November 1859 as On the Origin of Species. +Darwin, Charles (1859). On the Origin of Species. London: John Murray.(Online: 6th Edition (text)) +The Origin of Species is one of the hallmark works of biology. In this shortened abstract of his intended "big book" on Natural Selection, Darwin details his theory that organisms gradually evolve through a process of natural selection, and this process leads to the formation of new species. It was first published on November 24, 1859 and the initial print run was oversubscribed by booksellers at Murray's Autumn sale the day before. +Darwin presents a theory of natural selection that is in most aspects identical to the theories now accepted by scientists. He carefully argues out this theory by presenting accumulated scientific evidence from his voyage on the Beagle in the 1830s, and from his continuing studies up to the date of publication. His studies continued with the book being revised accordingly; the most extensive revisions were the 6th and final edition. +Darwin's theory of evolution by natural selection, with its tree-like model of branching common descent, has become the unifying theory of the life sciences. The theory explains the diversity of living organisms and their adaptation to the environment. It makes sense of the geologic record, biogeography, parallels in embryonic development, biological homologies, vestigiality, cladistics, phylogenetics and other fields, with unrivalled explanatory power; it has also become essential to applied sciences such as medicine and agriculture. +Darwin, Charles (1871). The Descent of Man, and Selection in Relation to Sex. John Murray. +Fisher, Ronald (1930). The Genetical Theory of Natural Selection. Oxford University Press. +In the preface, Fisher considers some general points, including that there must be an understanding of natural selection distinct from that of evolution, and that the then-recent advances in the field of genetics (see history of genetics) now allowed this. In the first chapter, Fisher considers the nature of inheritance, rejecting blending inheritance in favour of particulate inheritance. The second chapter introduces Fisher's fundamental theorem of natural selection. The third considers the evolution of dominance, which Fisher believed was strongly influenced by modifiers. The last five chapters (8-12) include Fisher's more idiosyncratic views on eugenics. One of the founding works of population genetics. +Dobzhansky, Theodosius (1937). Genetics and the origin of species. With an introduction by Stephen Jay Gould (1982 Reprint ed.). New York: Columbia University Press. ISBN 978-0-231-05475-1. {{cite book}}: ISBN / Date incompatibility (help) +Wilson, E. O. (1975). Sociobiology: The New Synthesis. Cambridge, MA: Belknap Press. +Wilson introduced the term sociobiology as an attempt to explain the evolutionary mechanics behind social behaviors such as altruism, aggression, and nurturance. Wilson's book sparked one of the great scientific controversies in biology of the 20th century. +Gould, Stephen Jay (1977). Ontogeny and Phylogeny. Harvard University Press. ISBN 978-0-674-63940-9. +Critically revisits Haeckel's idea that ontogeny recapitulates phylogeny. Gould presents heterochrony as a concept that allows us to describe the majority of developmental processes in evolution. This book played a significant role at the time by bringing the evolutionary biology community back to examine developmental biology, ignored for many years. +Pinker, Steven (1999). How the mind works. Vol. 882. New York: Norton. pp. 119–27, discussion 128–34. doi:10.1111/j.1749-6632.1999.tb08538.x. ISBN 978-0-393-31848-7. PMID 10415890. S2CID 38521835. {{cite book}}: |journal= ignored (help) +A synthesis of many of the ideas of Evolutionary Psychology. This field posits that there are insights into the way that the mind works if you view our cognitive capabilities as the adaptive result of evolution. Synthesizes the work of many Evolutionary Psychologists and provides a comprehensive starting point for inquiries into (exactly as the title states) how the mind works. + +== Genetics == + +This section contains a list of works on genetics, the science of genes, heredity, and variation in living organisms. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Bibliography_of_biology-2.md b/data/en.wikipedia.org/wiki/Bibliography_of_biology-2.md new file mode 100644 index 000000000..34a7f8921 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Bibliography_of_biology-2.md @@ -0,0 +1,58 @@ +--- +title: "Bibliography of biology" +chunk: 3/3 +source: "https://en.wikipedia.org/wiki/Bibliography_of_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:42.724301+00:00" +instance: "kb-cron" +--- + +Mendel, Gregor (1866). "Versuche über Pflanzen-Hybriden". Verhandlungen des naturforschenden Vereins Brünn. Published in English as "Experiments on Plant Hybridization". Journal of the Royal Horticultural Society. 26: 1–30. 1901. (Online version) +The result of years spent studying genetic traits in pea plants. Mendel compared seven discrete traits. Through experimentation, Mendel discovered that one inheritable trait would invariably be dominant to its recessive alternative. This model, later known as Mendelian inheritance or Mendelian genetics, provided an alternative to blending inheritance, which was the prevailing theory at the time. +Fisher, Ronald (1918). "The Correlation Between Relatives on the Supposition of Mendelian Inheritance". Transactions of the Royal Society of Edinburgh. 52 (2): 399–433. doi:10.1017/s0080456800012163. S2CID 181213898. +Schrödinger, Erwin (1944). What is life? the physical aspects of the living cell (2001 reprint ed.). Cambridge: Cambridge Univ. Press. ISBN 978-0-521-42708-1. {{cite book}}: ISBN / Date incompatibility (help) +Based on a series of public lectures delivered at Trinity College, Dublin. Schrödinger's lecture focused on one important question: "how can the events in space and time which take place within the spatial boundary of a living organism be accounted for by physics and chemistry?" He introduced the idea of an "aperiodic crystal" that contained genetic information in its configuration of covalent chemical bonds. In the 1950s, Schrödinger's idea of an aperiodic crystal stimulated enthusiasm for discovering the genetic molecule. Francis Crick, co-discoverer of the structure of DNA, credited Schrödinger's book with presenting an early theoretical description of how the storage of genetic information would work, and acknowledged the book as a source of inspiration for his initial research. +Pauling, Linus; Harvey A. Itano; S. J. Singer; Ibert C. Wells (1949). "Sickle Cell Anemia, a Molecular Disease". Science. 110 (2865): 543–548. Bibcode:1949Sci...110..543P. doi:10.1126/science.110.2865.543. PMID 15395398. S2CID 31674765. +Crick, Francis; Watson, James D. (1953). "Molecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic Acid". Nature. 171 (4356): 737–738. Bibcode:1953Natur.171..737W. doi:10.1038/171737a0. PMID 13054692. S2CID 4253007. (Online version (Original text)) + +== Microbiology == +This section contains a list of publications on microbiology. Microbiology is the study of microorganisms, which are defined as any microscopic organism that comprises either a single cell (unicellular), cell clusters or no cell at all (acellular). + +== Molecular biology == + +This section contains a list of works on molecular biology, the study of the molecular basis of biological activity. + +Crick, Francis; Watson, James D. (1953). "Molecular Structure of Nucleic Acids: A Structure for Deoxyribose Nucleic Acid". Nature. 171 (4356): 737–738. Bibcode:1953Natur.171..737W. doi:10.1038/171737a0. PMID 13054692. S2CID 4253007. (Online version (Original text)) +Described a molecular structure for DNA that was consistent with X-ray diffraction data and had implications for the nature of ineritance. + +== Physiology == +This section contains a list of works on physiology, the science of the function of living systems. This includes how organisms, organ systems, organs, cells and bio-molecules carry out the chemical or physical functions that exist in a living system. + +Harvey, William (1628). Exercitatio Anatomica de Motu Cordis et Sanguinis in Animalibus. English translation: Harvey, William (1993). On the motion of the heart and blood in animals. Translated by Robert Willis. Buffalo, N.Y.: Prometheus Books. ISBN 978-0-87975-854-7. + +== Taxonomy == + +This section contains a list of works on taxonomy, the practice and science of classification or the result of it. + +Linnaeus, Carolus (1758–1759). Systema naturæ per regna tria naturæ, secundum classes, ordines, genera, species, cum characteribus, differentiis, synonymis, locis (two volumes) (in Latin) (10th ed.). Stockholm: Laurentius Salvius. Online access +Classified animals using a hierarchical system with 5 levels: Kingdom, class, order, genus and species. The official starting point of zoological nomenclature. +Linnaeus, Carolus (1753). Species Plantarum (The Species of Plants). +A two-volume work, going through many editions (ever expanding), listing all plants then known, made accessible by an ordering in (artificial) classes and orders, and giving every listed species a two-part name. With this book anybody, by counting the male and female parts present in a flower, could get to a listing of the genera the plant in question belongs to. The system of binomial nomenclature that bears his name effectively began with this work. + +== Zoology == + +This section contains a list of works on zoology, the study of the animal kingdom, including the structure, embryology, evolution, classification, habits, and distribution of all animals, both living and extinct. + +Pliny. Naturalis Historia. (c. 77 – 79) +Encyclopedia of nature. It included many areas that are not considered to be part of nature sciences today - from geography, botany, zoology to painting. The encyclopedia was also novel with respect to its structure. It was the first to use references, table of contents and tables of animal characteristics. +White, Gilbert (1813). The Natural History and Antiquities of Selborne. +Observations on birds and many other aspects of the natural world that White observed near where he lived. + +== See also == +List of zoology journals +Outline of biology + +== References == + +== Further reading == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Index_of_anatomy_articles-0.md b/data/en.wikipedia.org/wiki/Index_of_anatomy_articles-0.md index 9554aac2b..2fcdc049d 100644 --- a/data/en.wikipedia.org/wiki/Index_of_anatomy_articles-0.md +++ b/data/en.wikipedia.org/wiki/Index_of_anatomy_articles-0.md @@ -4,7 +4,7 @@ chunk: 1/1 source: "https://en.wikipedia.org/wiki/Index_of_anatomy_articles" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T07:49:03.783525+00:00" +date_saved: "2026-05-05T07:55:04.348567+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/Index_of_evolutionary_biology_articles-0.md b/data/en.wikipedia.org/wiki/Index_of_evolutionary_biology_articles-0.md new file mode 100644 index 000000000..3754bbb14 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Index_of_evolutionary_biology_articles-0.md @@ -0,0 +1,110 @@ +--- +title: "Index of evolutionary biology articles" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/Index_of_evolutionary_biology_articles" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:17.405760+00:00" +instance: "kb-cron" +--- + +This is a list of topics in evolutionary biology. + + +== A == +abiogenesis – adaptation – adaptive mutation – adaptive radiation – allele – allele frequency – allochronic speciation – allopatric speciation – altruism – anagenesis – anti-predator adaptation – applications of evolution – apomorphy – aposematism – Archaeopteryx – aquatic adaptation – artificial selection – atavism + + +== B == +Henry Walter Bates – biological organisation – Black Queen hypothesis – Brassica oleracea – breed + + +== C == +Cambrian explosion – camouflage – Sean B. Carroll – catagenesis – gene-centered view of evolution – cephalization – Sergei Chetverikov – chronobiology – chronospecies – clade – cladistics – climatic adaptation – coalescent theory – co-evolution – co-operation – coefficient of relationship – common descent – convergent evolution – creation–evolution controversy – cultivar – conspecific song preference + + +== D == +Darwin (unit) – Charles Darwin – Darwinism – Darwin's finches – Richard Dawkins – directed mutagenesis – Directed evolution – directional selection – disruptive selection – Theodosius Dobzhansky – dog breeding – domestication – domestication of the horse + + +== E == +E. coli long-term evolution experiment – ecological genetics – ecological selection – ecological speciation – Endless Forms Most Beautiful – endosymbiosis – error threshold (evolution) – evidence of common descent – evolution – evolutionary arms race – evolutionary capacitance +Evolution: of ageing – of the brain – of cetaceans – of complexity – of dinosaurs – of the eye – of fish – of the horse – of insects – of human intelligence – of mammalian auditory ossicles – of mammals – of monogamy – of sex – of sirenians – of tetrapods – of the wolf +evolutionary developmental biology – evolutionary dynamics – evolutionary game theory – evolutionary history of life – evolutionary history of plants – evolutionary invasion analysis - evolutionary medicine – evolutionary neuroscience – evolutionary psychology – evolutionary radiation – evolutionarily stable strategy – evolutionary taxonomy – evolutionary tree – evolvability – experimental evolution – exaptation – extinction + + +== F == +Joe Felsenstein – R.A. Fisher – Fisher's reproductive value – fitness – fitness landscape – fixation index (FST) – fluctuating selection – E.B. Ford – fossil – frequency-dependent selection + + +== G == +Galápagos Islands – gene – gene-centric view of evolution – gene duplication – gene flow – gene pool – genetic drift – genetic hitchhiking – genetic recombination – genetic variation – genotype – gene–environment correlation – gene–environment interaction – genotype–phenotype distinction – Stephen Jay Gould – gradualism – Peter and Rosemary Grant – group selection + + +== H == +J. B. S. Haldane – W. D. Hamilton – Hardy–Weinberg principle – heredity – hierarchy of life – history of evolutionary thought – history of speciation – homologous chromosomes – homology (biology) – horizontal gene transfer – human evolution – human evolutionary genetics – human vestigiality – Julian Huxley – Thomas Henry Huxley + + +== I == +inclusive fitness – insect evolution – Invertebrate paleontology (a.k.a. invertebrate paleobiology or paleozoology) + + +== K == +karyotype – kin selection – Motoo Kimura – koinophilia + + +== L == +Jean-Baptiste Lamarck – Lamarckism – landrace – language – last universal common ancestor – level of support for evolution – Richard Lewontin – list of gene families – list of human evolution fossils – life-history theory – Wen-Hsiung Li – living fossils – Charles Lyell + + +== M == +macroevolution – macromutation – The Major Transitions in Evolution – maladaptation – The Malay Archipelago – mass extinctions – mating systems – John Maynard Smith – Ernst Mayr – Gregor Mendel – memetics – Mendelian inheritance – Mesozoic–Cenozoic radiation – microevolution – micropaleontology (a.k.a. micropaleobiology) – Miller–Urey experiment – mimicry – Mitochondrial Eve – modern evolutionary synthesis – molecular clock – molecular evolution – molecular phylogeny – molecular systematics – mosaic evolution – most recent common ancestor – Hermann Joseph Muller – Muller's ratchet – mutation – mutational meltdown + + +== N == +natural selection – natural genetic engineering – nature versus nurture – negative selection – Neo-Darwinism – neutral theory of molecular evolution – Baron Franz Nopcsa – "Nothing in Biology Makes Sense Except in the Light of Evolution" + + +== O == +Susumu Ohno – Aleksandr Oparin – On The Origin of Species – Ordovician radiation – origin of birds – origin of language – orthologous genes (orthologs) + + +== P == +paleoanthropology – paleobiology – paleobotany – paleontology – paleozoology (of vertebrates – of invertebrates) – parallel evolution – paralogous genes (paralogs) – parapatric speciation – paraphyletic – particulate inheritance – peppered moth – peppered moth evolution – peripatric speciation – phenotype – phylogenetics – phylogeny – phylogenetic tree – Pikaia – Plant evolution – polymorphism (biology) – population – population bottleneck – population dynamics – population genetics – preadaptation – prehistoric archaeology – Principles of Geology – George R. Price – Price equation – punctuated equilibrium + + +== Q == +quantitative genetics - quantum evolution – quasispecies model + + +== R == +race (biology) – Red Queen hypothesis – recapitulation theory – recent African origin of modern humans – recombination – Bernhard Rensch – reinforcement (speciation) – reproductive coevolution in Ficus – reproductive isolation – r/K selection theory + + +== S == +selection – selective breeding – selfish DNA – The Selfish Gene – sexual selection – signalling theory – sociobiology – social effects of evolutionary theory – species – speciation – species flock – sperm competition – stabilizing selection – strain (biology) – subspecies – survival of the fittest – symbiogenesis – sympatric speciation – synapomorphy – systematics – George Gaylord Simpson – G. Ledyard Stebbins + + +== T == +Tiktaalik – timeline of evolution – trait (biological) – transgressive phenotype – transitional fossil – transposon – tree of life – triangle of U + + +== U == +unit of selection + + +== V == +variety (botany) – vertebrate paleontology (a.k.a. vertebrate paleobiology or paleozoology) – viral evolution – The Voyage of the Beagle – vestigiality + + +== W == +Alfred Russel Wallace – Wallace effect – Wallace Line – Wallacea – George C. Williams (biologist) – Edward O. Wilson – Sewall Wright + + +== Y == +Y-chromosomal Adam – Y-DNA haplogroups by ethnic groups + + +== See also == +List of biology topics +List of biochemistry topics \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-0.md b/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-0.md index e331c8779..aa3477da0 100644 --- a/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-0.md +++ b/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-0.md @@ -4,7 +4,7 @@ chunk: 1/3 source: "https://en.wikipedia.org/wiki/Index_of_molecular_biology_articles" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T07:49:35.327157+00:00" +date_saved: "2026-05-05T07:57:24.969272+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-1.md b/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-1.md index 131105854..2cdbc3593 100644 --- a/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-1.md +++ b/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-1.md @@ -4,7 +4,7 @@ chunk: 2/3 source: "https://en.wikipedia.org/wiki/Index_of_molecular_biology_articles" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T07:49:35.327157+00:00" +date_saved: "2026-05-05T07:57:24.969272+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-2.md b/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-2.md index 5db179245..e780a2881 100644 --- a/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-2.md +++ b/data/en.wikipedia.org/wiki/Index_of_molecular_biology_articles-2.md @@ -4,7 +4,7 @@ chunk: 3/3 source: "https://en.wikipedia.org/wiki/Index_of_molecular_biology_articles" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T07:49:35.327157+00:00" +date_saved: "2026-05-05T07:57:24.969272+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/List_of_Accipitriformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Accipitriformes_by_population-0.md new file mode 100644 index 000000000..7458dd21a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Accipitriformes_by_population-0.md @@ -0,0 +1,32 @@ +--- +title: "List of Accipitriformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Accipitriformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:16.119972+00:00" +instance: "kb-cron" +--- + +This is a list of Accipitriformes species by global population. This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and species classifications are noted. +While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. While not all of these species have had their populations quantified, species without estimates are also listed below in a separate table. +The order Cathartiformes (containing family Cathartidae, the New World vultures) has been folded into Accipitriformes by the International Ornithological Congress. Other authorities, such as the American Ornithological Society, maintain Cathartiformes and Accipitriformes as two distinct orders. Because Cathartidae has only seven species, they are included in this list for simplicity. +Version 15.1 of the IOC World Bird List describes 266 members of Accipitriformes when including Cathartidae (259 without). As of December 2025, IUCN/BirdLife International have evaluated 259 of these species, excepting 7 being maintained as subspecies of other birds in this list. +There is one species listed as a member of Accipitriformes which is extinct: + +Bermuda hawk (Bermuteo avivorous) - last observed in 1603. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Anseriformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Anseriformes_by_population-0.md new file mode 100644 index 000000000..1747d1183 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Anseriformes_by_population-0.md @@ -0,0 +1,39 @@ +--- +title: "List of Anseriformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Anseriformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:17.440289+00:00" +instance: "kb-cron" +--- + +This is a list of Anseriformes species by global population. Where possible, estimates are given for both the population of mature individuals, and the total global population. This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and species classifications are noted. +Anseriformes (Anser being Latin for "goose") is the taxonomic order to which the ducks, geese, swans, and screamers belong. Version 15.1 (2025) of the IOC World Bird List describes 178 species belonging to Anseriformes, six of which are extinct. As of December 2025, BirdLife International has assessed 176 species (excepting Mexican Duck and the split of Taiga/Tundra bean goose); 168 (95% of assessed species) have had total or breeding population estimated. A variety of methods are used for counting waterfowl. For example, in North America, national and sub-national agencies use planes and helicopters to make aerial transects of breeding populations, and extrapolate these counts over the species' known ranges. Methodologies are continuously being refined; thus estimates can be expected to become more accurate over time. Forecasts can be made by studying habitat condition trends and by interviewing local experts. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The first two birds in this list, the pink-headed duck and crested shelduck, retain a status of Critically Endangered on the IUCN Red List but may be extinct. The last sighting of the former occurred in 1948-1949, but some dispute this date and argue the species was last reliably documented in the 1930s, 1923, or 1910. The last pink-headed ducks in captivity died in the 1940s. Unconfirmed reports from Myanmar provide some hope this species is still extant. +The last confirmed reporting of the crested shelduck was in 1964 near Vladivostok. A disputed record from North Korea was claimed in March 1971. Unconfirmed reports from Northeast China are the best chance this species is still extant. +To be assessed as Critically Endangered, a species must have experienced a decline of at least 80% in the past ten years or three generations, or be projected to decline that much in the future ten years or three generations. Some species included in this list are rapidly approaching their minimum viable population (MVP), at which point the species would become functionally extinct. + + +== Extinct species == +Réunion shelduck or Réunion sheldgoose; Alopochen kervazoi: known only from fossils; extinct by 1710. +Mauritius shelduck or Mauritius sheldgoose; Alopochen mauritania: described by Johannes Pretorius (as sheldgoose) in 1669; extinct by 1698. +Amsterdam duck or Amsterdam wigeon; Mareca marecula: known from fossils, extinct by 1793 due to hunting and introduced rats. +Mauritius duck or Mascarene teal; Anas theodori: early explorers described "a great number of grey teal" on Mauritius in 1681, which may have referred to this bird. Last reported in 1696. +Mariana mallard; Anas oustaleti: considered by some taxonomists to be a subspecies of the mallard or American black duck. Last known individual died in captivity in 1981. +Finsch's duck; Chenonetta finschi: once very abundant, went extinct between 1250-1860. +Labrador duck; Camptorhynchus labradorius: hunted to extinction; last seen in 1875. +New Zealand merganser or Auckland Island merganser; Mergus australis: hunted to extinction; last recorded in 1902. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population +List of duck breeds + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Apodiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Apodiformes_by_population-0.md new file mode 100644 index 000000000..f5c1c497e --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Apodiformes_by_population-0.md @@ -0,0 +1,32 @@ +--- +title: "List of Apodiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Apodiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:20.899567+00:00" +instance: "kb-cron" +--- + +This is a list of Apodiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +Members of Apodiformes include the swifts, treeswifts, and hummingbirds. Note that some ornithological authorities (e.g., IUCN/BirdLife International) no longer recognize Apodiformes, and place all members within Caprimulgiformes. However, Apodiformes is maintained as a separate order here to match IOC taxonomy (IOC World Bird List version 15.1). For more discussion of this taxonomic complex, see Strisores. +This list is not comprehensive, as not all Apodiformes have had their numbers quantified. +The IOC World Bird List (version 15.1) recognizes 480 species of Apodiformes, one of which is extinct. +One member of Apodiformes is extinct: + +Brace's emerald (Riccordia bracei) - went extinct circa 1877. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Bucerotiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Bucerotiformes_by_population-0.md new file mode 100644 index 000000000..dacb190da --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Bucerotiformes_by_population-0.md @@ -0,0 +1,29 @@ +--- +title: "List of Bucerotiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Bucerotiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:23.644325+00:00" +instance: "kb-cron" +--- + +This is a list of Bucerotiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is incomprehensive, as not all Bucerotiformes have had their numbers quantified. +The IOC World Bird List (version 15.1) recognizes 75 species of Bucerotiformes. +This list follows IUCN classifications for species names. Where IUCN classifications differ from other ornithological authorities, alternative names are noted. +Some species listed as members of Bucerotiformes are extinct: + +St. Helena hoopoe (Upupa antaios) - went extinct by end of 17th century. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Charadriiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Charadriiformes_by_population-0.md new file mode 100644 index 000000000..b7143a3cf --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Charadriiformes_by_population-0.md @@ -0,0 +1,41 @@ +--- +title: "List of Charadriiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Charadriiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:25.429069+00:00" +instance: "kb-cron" +--- + +This is a list of Charadriiformes species by global population. Charadriiformes (Charadrius being Latin for "plover") is the taxonomic order to which the waders, gulls, and auks belong. While numbers are estimates, they have been made by the experts in their fields. +Not all Charadriiformes have had their numbers quantified, but species without population estimates are included in a secondary table below. +The Charadriiformes were sometimes grouped with the Ciconiiformes in older taxonomic systems (e.g., Sibley-Ahlquist taxonomy). However, the American Ornithological Society, International Ornithologists' Union (IOC) and BirdLife International, which informs IUCN taxonomy, now agree on it being a separate order following more recent genetic analyses. +A variety of methods are used for counting Charadriiformes. For example, the piping plover is subject to the quinquennial Piping Plover International Census, which is carried out in 9 Canadian provinces, 32 US states, Mexico, Central America, and the Caribbean. In the 2006 survey, Saskatchewan alone had 159 volunteers scour 294 waterbodies. The mountain plover has had its nests counted through the drive transect method. Once density has been calculated, the numbers are extrapolated over a bird's range. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The IOC World Bird List (version 15.1) recognizes 392 species of Charadriiformes, eight of which are extinct. There are several disagreements about the species status of taxa within Charadriiformes. As of January 2026, IOC lists ten species which are considered subspecies by IUCN/BirdLife International. Similarly, IUCN/BirdLife International list three species which still have subspecies status in IOC taxonomies. See 'Notes' column of included tables for more information on these taxonomic disputes. +This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +Some members of Charadriiformes are extinct: + +Christmas sandpiper, or Kiritimati sandpiper (Prosobonia cancellata) - likely extinct by 1860. +Tahiti sandpiper (Prosobonia leucoptera) - last seen in 1777, when only specimen was collected. +Moorea sandpiper (Prosobonia ellisi) - last seen in 1777, when only specimen was collected. +Canarian oystercatcher, or Canary Islands oystercatcher (Haematopus meadewaldoi) - last specimen collected in 1913; last observations occurred in 1940s. +Great auk (Pinguinus impennis) - extinct from being hunted; last observed in 1852. +Slender-billed curlew (Numenius tenuirostris) - last observed in 1995; declared extinct in 2025. +North Island snipe (Coenocorypha barrierensis) - last recorded in 1870. +South Island snipe (Coenocorypha iredalei) - last recorded in 1964. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Ciconiiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Ciconiiformes_by_population-0.md new file mode 100644 index 000000000..471a6d14f --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Ciconiiformes_by_population-0.md @@ -0,0 +1,24 @@ +--- +title: "List of Ciconiiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Ciconiiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:26.760685+00:00" +instance: "kb-cron" +--- + +This is a list of Ciconiiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The IOC World Bird List (version 15.1) recognizes 20 species of Ciconiiformes. As of December 2025, IUCN/BirdLife International have assessed the populations of all members of this order. This list follows IUCN classifications for species names. Where IUCN classifications differ from other ornithological authorities, alternative names are noted. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Columbiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Columbiformes_by_population-0.md new file mode 100644 index 000000000..35a7947e4 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Columbiformes_by_population-0.md @@ -0,0 +1,43 @@ +--- +title: "List of Columbiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Columbiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:28.306796+00:00" +instance: "kb-cron" +--- + +This is a list of Columbiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is not comprehensive, as not all Columbiformes have had their populations quantified. +The IOC World Bird List (version 15.1) recognizes 352 species of Columbiformes, 13 of which are extinct. This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +Some members of Columbiformes are extinct: + +Bonin wood pigeon (Columba versicolor) - last observed in 1889; extinct due to deforestation. +Ryukyu wood pigeon (Columba jouyi) - last observed in 1936. +Passenger pigeon (Ectopistes migratorius) - last wild bird was shot in 1900; last captive individual died in 1914. +Rodrigues pigeon or Rodrigues turtle dove (Nesoenas rodericanus) - went extinct during the 18th century. +Spotted green pigeon or Liverpool pigeon (Caloenas maculata) - known from one specimen, and not seen since 1928. +Norfolk ground dove (Pampusana norfolkensis) - poorly described species, known only from subfossils. Extinct sometime after 1790. Not recognized by IUCN/BirdLife International. +Tanna ground dove (Pampusana ferruginea) - last observed (only record for species) in 1774. +Thick-billed ground dove (Pampusana salamonis) - last observed in 1927. +Choiseul pigeon (Microgoura meeki) - last observed in 1904. +Dodo (Raphus cucullatus) - extinct circa 1662. +Rodrigues solitaire (Pezophaps solitaria) - extinct by end of 1760s. +Red-moustached fruit dove (Ptilinopus mercierii) - last observed in 1922. +Mauritius blue pigeon (Alectroenas nitidissimus) - extinct between 1832 - 1837. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Coraciiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Coraciiformes_by_population-0.md new file mode 100644 index 000000000..4dc5dccb0 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Coraciiformes_by_population-0.md @@ -0,0 +1,28 @@ +--- +title: "List of Coraciiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Coraciiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:29.674747+00:00" +instance: "kb-cron" +--- + +This is a list of Coraciiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is incomprehensive, as not all Coraciiformes have had their numbers quantified. +The IOC World Bird List (version 15.1) recognizes 186 species of Coraciiformes. This list follows IUCN classifications for species names. Where IUCN classifications differ from other ornithological authorities, alternative names are noted. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Cuculiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Cuculiformes_by_population-0.md new file mode 100644 index 000000000..590cc6229 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Cuculiformes_by_population-0.md @@ -0,0 +1,32 @@ +--- +title: "List of Cuculiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Cuculiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:31.015528+00:00" +instance: "kb-cron" +--- + +This is a list of Cuculiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is incomprehensive, as not all Cuculiformes have had their numbers quantified. +The IOC World Bird List (version 15.1) recognizes 156 species of Cuculiformes, two of which are extinct. This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +Some species included as members of Cuculiformes are extinct: + +Snail-eating coua, or Delalande's coua (Coua delalandei) - last seen in 1834. +St. Helena cuckoo (Nannococcyx psix) - last seen in 1550. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-0.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-0.md new file mode 100644 index 000000000..1e658cf5b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-0.md @@ -0,0 +1,13 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 1/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +This list contains a list of EC numbers for the first group, EC 1, oxidoreductases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. + +== EC 1.1 Acting on the CH-OH group of donors == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-1.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-1.md new file mode 100644 index 000000000..e3a03b106 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-1.md @@ -0,0 +1,257 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 2/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.1.1 With Nicotinamide adenine dinucleotide or NADP as acceptor === +EC 1.1.1.1: alcohol dehydrogenase +EC 1.1.1.2: alcohol dehydrogenase (NADP+) +EC 1.1.1.3: homoserine dehydrogenase +EC 1.1.1.4: (R,R)-butanediol dehydrogenase +EC 1.1.1.5: acetoin dehydrogenase. Now EC 1.1.1.303, diacetyl reductase [(R)-acetoin forming] and EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming] +EC 1.1.1.6: glycerol dehydrogenase +EC 1.1.1.7: propanediol-phosphate dehydrogenase +EC 1.1.1.8: glycerol-3-phosphate dehydrogenase (NAD+) +EC 1.1.1.9: D-xylulose reductase +EC 1.1.1.10: L-xylulose reductase +EC 1.1.1.11: D-arabinitol 4-dehydrogenase +EC 1.1.1.12: L-arabinitol 4-dehydrogenase +EC 1.1.1.13: L-arabinitol 2-dehydrogenase +EC 1.1.1.14: L-iditol 2-dehydrogenase +EC 1.1.1.15: D-iditol 2-dehydrogenase +EC 1.1.1.16: galactitol 2-dehydrogenase +EC 1.1.1.17: mannitol-1-phosphate 5-dehydrogenase +EC 1.1.1.18: inositol 2-dehydrogenase +EC 1.1.1.19: glucuronate reductase +EC 1.1.1.20: glucuronolactone reductase +EC 1.1.1.207: (-)-menthol dehydrogenase +EC 1.1.1.208: (+)-neomenthol dehydrogenase +EC 1.1.1.21: aldose reductase +EC 1.1.1.22: UDP-glucose 6-dehydrogenase +EC 1.1.1.222: (R)-4-hydroxyphenyllactate dehydrogenase +EC 1.1.1.23: histidinol dehydrogenase| +EC 1.1.1.24: quinate/shikimate dehydrogenase (NAD+) +EC 1.1.1.25: shikimate dehydrogenase (NADP+) +EC 1.1.1.26: glyoxylate reductase +EC 1.1.1.27: L-lactate dehydrogenase +EC 1.1.1.28: D-lactate dehydrogenase +EC 1.1.1.29: glycerate dehydrogenase +EC 1.1.1.30: 3-hydroxybutyrate dehydrogenase +EC 1.1.1.31: 3-hydroxyisobutyrate dehydrogenase +EC 1.1.1.32: mevaldate reductase +EC 1.1.1.33: mevaldate reductase (NADPH) +EC 1.1.1.34: hydroxymethylglutaryl-CoA reductase (NADPH) +EC 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase +EC 1.1.1.36: acetoacetyl-CoA reductase +EC 1.1.1.37: malate dehydrogenase +EC 1.1.1.38: malate dehydrogenase (oxaloacetate-decarboxylating) +EC 1.1.1.39: malate dehydrogenase (decarboxylating) +EC 1.1.1.40: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) +EC 1.1.1.41: isocitrate dehydrogenase (NAD+) +EC 1.1.1.42: isocitrate dehydrogenase (NADP+) +EC 1.1.1.43: phosphogluconate 2-dehydrogenase +EC 1.1.1.44: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) +EC 1.1.1.45: L-gulonate 3-dehydrogenase +EC 1.1.1.46: L-arabinose 1-dehydrogenase +EC 1.1.1.47: glucose 1-dehydrogenase [NAD(P)+)] +EC 1.1.1.48: D-galactose 1-dehydrogenase +EC 1.1.1.49: glucose-6-phosphate dehydrogenase (NADP+) +EC 1.1.1.50: 3α-hydroxysteroid 3-dehydrogenase (Si-specific) +EC 1.1.1.51: 3(or 17)β-hydroxysteroid dehydrogenase +EC 1.1.1.52: 3α-hydroxycholanate dehydrogenase (NAD+) +EC 1.1.1.53: 3α(or 20β)-hydroxysteroid dehydrogenase +EC 1.1.1.54: allyl-alcohol dehydrogenase +EC 1.1.1.55: lactaldehyde reductase (NADPH) +EC 1.1.1.56: ribitol 2-dehydrogenase +EC 1.1.1.57: fructuronate reductase +EC 1.1.1.58: tagaturonate reductase +EC 1.1.1.59: 3-hydroxypropionate dehydrogenase +EC 1.1.1.60: 2-hydroxy-3-oxopropionate reductase +EC 1.1.1.61: 4-hydroxybutyrate dehydrogenase +EC 1.1.1.62: 17β-estradiol 17-dehydrogenase +EC 1.1.1.63: testosterone 17β-dehydrogenase. Now EC 1.1.1.239, 3α(17β)-hydroxysteroid dehydrogenase (NAD+) +EC 1.1.1.64: testosterone 17β-dehydrogenase (NADP+) +EC 1.1.1.65: pyridoxine 4-dehydrogenase +EC 1.1.1.66: ω-hydroxydecanoate dehydrogenase +EC 1.1.1.67: mannitol 2-dehydrogenase +EC 1.1.1.68: 5,10-methylenetetrahydrofolate reductase. Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H] +EC 1.1.1.69: gluconate 5-dehydrogenase +EC 1.1.1.70: D-glucuronolactone dehydrogenase. Now included with EC 1.2.1.3 aldehyde dehydrogenase (NAD+) +EC 1.1.1.71: alcohol dehydrogenase [NAD(P)+] +EC 1.1.1.72: glycerol dehydrogenase (NADP+) +EC 1.1.1.73: octanol dehydrogenase +EC 1.1.1.74: D-aminopropanol dehydrogenase (reaction due to EC 1.1.1.4 (R,R)-butanediol dehydrogenase) +EC 1.1.1.75: (R)-aminopropanol dehydrogenase +EC 1.1.1.76: (S,S)-butanediol dehydrogenase +EC 1.1.1.77: lactaldehyde reductase +EC 1.1.1.78: methylglyoxal reductase (NADH-dependent) +EC 1.1.1.79: glyoxylate reductase (NADP+) +EC 1.1.1.80: isopropanol dehydrogenase (NADP+) +EC 1.1.1.81: hydroxypyruvate reductase +EC 1.1.1.82: malate dehydrogenase (NADP+) +EC 1.1.1.83: D-malate dehydrogenase (decarboxylating) +EC 1.1.1.84: dimethylmalate dehydrogenase +EC 1.1.1.85: 3-isopropylmalate dehydrogenase +EC 1.1.1.86: ketol-acid reductoisomerase (NADP+) +EC 1.1.1.87: homoisocitrate dehydrogenase +EC 1.1.1.88: hydroxymethylglutaryl-CoA reductase +EC 1.1.1.89: dihydroxyisovalerate dehydrogenase (isomerizing). Now included with EC 1.1.1.86 ketol-acid reductoisomerase +EC 1.1.1.90: aryl-alcohol dehydrogenase +EC 1.1.1.91: aryl-alcohol dehydrogenase (NADP+) +EC 1.1.1.92: oxaloglycolate reductase (decarboxylating) +EC 1.1.1.93: tartrate dehydrogenase +EC 1.1.1.94: glycerol-3-phosphate dehydrogenase [NAD(P)+] +EC 1.1.1.95: phosphoglycerate dehydrogenase +EC 1.1.1.96: diiodophenylpyruvate reductase +EC 1.1.1.97: 3-hydroxybenzyl-alcohol dehydrogenase +EC 1.1.1.98: (R)-2-hydroxy-fatty-acid dehydrogenase +EC 1.1.1.99: (S)-2-hydroxy-fatty-acid dehydrogenase +EC 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase +EC 1.1.1.101: acylglycerone-phosphate reductase +EC 1.1.1.102: 3-dehydrosphinganine reductase +EC 1.1.1.103: L-threonine 3-dehydrogenase +EC 1.1.1.104: 4-oxoproline reductase +EC 1.1.1.105: all-trans-retinol dehydrogenase (NAD+) +EC 1.1.1.106: pantoate 4-dehydrogenase +EC 1.1.1.107: pyridoxal 4-dehydrogenase +EC 1.1.1.108: carnitine 3-dehydrogenase +EC 1.1.1.109: Now EC 1.3.1.28, 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase +EC 1.1.1.110: aromatic 2-oxoacid reductase +EC 1.1.1.111: 3-(imidazol-5-yl)lactate dehydrogenase +EC 1.1.1.112: indanol dehydrogenase +EC 1.1.1.113: L-xylose 1-dehydrogenase +EC 1.1.1.114: apiose 1-reductase +EC 1.1.1.115: ribose 1-dehydrogenase (NADP+) +EC 1.1.1.116: D-arabinose 1-dehydrogenase (NAD+) +EC 1.1.1.117: D-arabinose 1-dehydrogenase [NAD(P)+] +EC 1.1.1.118: glucose 1-dehydrogenase (NAD+) +EC 1.1.1.119: glucose 1-dehydrogenase (NADP+) +EC 1.1.1.120: galactose 1-dehydrogenase (NADP+) +EC 1.1.1.121: aldose 1-dehydrogenase (NAD+) +EC 1.1.1.122: D-threo-aldose 1-dehydrogenase +EC 1.1.1.123: sorbose 5-dehydrogenase (NADP+) +EC 1.1.1.124: fructose 5-dehydrogenase (NADP+) +EC 1.1.1.125: 2-deoxy-D-gluconate 3-dehydrogenase +EC 1.1.1.126: 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase +EC 1.1.1.127: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase +EC 1.1.1.128: The reaction described is covered by EC 1.1.1.264, L-idonate 5-dehydrogenase. EC 1.1.1.129: L-threonate 3-dehydrogenase +EC 1.1.1.130: 3-dehydro-L-gulonate 2-dehydrogenase +EC 1.1.1.131: mannuronate reductase +EC 1.1.1.132: GDP-mannose 6-dehydrogenase +EC 1.1.1.133: dTDP-4-dehydrorhamnose reductase +EC 1.1.1.134: dTDP-6-deoxy-L-talose 4-dehydrogenase (NADP+) +EC 1.1.1.135: GDP-6-deoxy-D-talose 4-dehydrogenase +EC 1.1.1.136: UDP-N-acetylglucosamine 6-dehydrogenase +EC 1.1.1.137: ribitol-5-phosphate 2-dehydrogenase +EC 1.1.1.138: mannitol 2-dehydrogenase (NADP+) +EC 1.1.1.139: polyol dehydrogenase (NADP+). Now included with EC 1.1.1.21 aldehyde reductase +EC 1.1.1.140: sorbitol-6-phosphate 2-dehydrogenase +EC 1.1.1.141: 15-hydroxyprostaglandin dehydrogenase (NAD+) +EC 1.1.1.142: D-pinitol dehydrogenase +EC 1.1.1.143: sequoyitol dehydrogenase +EC 1.1.1.144: perillyl-alcohol dehydrogenase +EC 1.1.1.145: 3β-hydroxy-Δ5-steroid dehydrogenase +EC 1.1.1.146: 11β-hydroxysteroid dehydrogenase +EC 1.1.1.147: 16α-hydroxysteroid dehydrogenase +EC 1.1.1.148: estradiol 17α-dehydrogenase +EC 1.1.1.149: 20α-hydroxysteroid dehydrogenase +EC 1.1.1.150: 21-hydroxysteroid dehydrogenase (NAD+) +EC 1.1.1.151: 21-hydroxysteroid dehydrogenase (NADP+) +EC 1.1.1.152: 3α-hydroxy-5β-androstane-17-one 3α-dehydrogenase +EC 1.1.1.153: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) +EC 1.1.1.154: ureidoglycolate dehydrogenase +EC 1.1.1.155: homoisocitrate dehydrogenase. The enzyme is identical to EC 1.1.1.87, homoisocitrate dehydrogenase +EC 1.1.1.156: glycerol 2-dehydrogenase (NADP+) +EC 1.1.1.157: 3-hydroxybutyryl-CoA dehydrogenase +EC 1.1.1.158: Now EC 1.3.1.98, UDP-N-acetylmuramate dehydrogenase +EC 1.1.1.159: 7α-hydroxysteroid dehydrogenase +EC 1.1.1.160: dihydrobunolol dehydrogenase +EC 1.1.1.161: The activity is part of EC 1.14.13.15, cholestanetriol 26-monooxygenase +EC 1.1.1.162: erythrulose reductase +EC 1.1.1.163: cyclopentanol dehydrogenase +EC 1.1.1.164: hexadecanol dehydrogenase +EC 1.1.1.165: 2-alkyn-1-ol dehydrogenase +EC 1.1.1.166: hydroxycyclohexanecarboxylate dehydrogenase +EC 1.1.1.167: hydroxymalonate dehydrogenase +EC 1.1.1.168: 2-dehydropantolactone reductase (Re-specific) +EC 1.1.1.169: 2-dehydropantoate 2-reductase +EC 1.1.1.170: 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating) +EC 1.1.1.171: Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H] +EC 1.1.1.172: 2-oxoadipate reductase +EC 1.1.1.173: L-rhamnose 1-dehydrogenase +EC 1.1.1.174: cyclohexane-1,2-diol dehydrogenase +EC 1.1.1.175: D-xylose 1-dehydrogenase +EC 1.1.1.176: 12α-hydroxysteroid dehydrogenase +EC 1.1.1.177: glycerol-3-phosphate 1-dehydrogenase (NADP+) +EC 1.1.1.178: 3-hydroxy-2-methylbutyryl-CoA dehydrogenase +EC 1.1.1.179: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming) +EC 1.1.1.180: Now included with EC 1.1.1.131 mannuronate reductase +EC 1.1.1.181: cholest-5-ene-3β,7α-diol 3β-dehydrogenase +EC 1.1.1.182: Now included with EC 1.1.1.198 (+)-borneol dehydrogenase, EC 1.1.1.227 (-)-borneol dehydrogenase and EC 1.1.1.228 (+)-sabinol dehydrogenase +EC 1.1.1.183: geraniol dehydrogenase (NADP+) +EC 1.1.1.184: carbonyl reductase (NADPH) +EC 1.1.1.185: L-glycol dehydrogenase +EC 1.1.1.186: dTDP-galactose 6-dehydrogenase +EC 1.1.1.187: GDP-4-dehydro-D-rhamnose reductase +EC 1.1.1.188: prostaglandin-F synthase +EC 1.1.1.189: prostaglandin-E2 9-reductase +EC 1.1.1.190: indole-3-acetaldehyde reductase (NADH) +EC 1.1.1.191: indole-3-acetaldehyde reductase (NADPH) +EC 1.1.1.192: long-chain-alcohol dehydrogenase +EC 1.1.1.193: 5-amino-6-(5-phosphoribosylamino)uracil reductase +EC 1.1.1.194: coniferyl-alcohol dehydrogenase +EC 1.1.1.195: cinnamyl-alcohol dehydrogenase +EC 1.1.1.196: 15-hydroxyprostaglandin-D dehydrogenase (NADP+) +EC 1.1.1.197: 15-hydroxyprostaglandin dehydrogenase (NADP+) +EC 1.1.1.198: (+)-borneol dehydrogenase +EC 1.1.1.199: (S)-usnate reductase +EC 1.1.1.200: aldose-6-phosphate reductase (NADPH) +EC 1.1.1.228: (+)-sabinol dehydrogenase +EC 1.1.1.251: galactitol-1-phosphate 5-dehydrogenase +EC 1.1.1.252: tetrahydroxynaphthalene reductase +EC 1.1.1.253: Now EC 1.5.1.33, pteridine reductase +EC 1.1.1.254: (S)-carnitine 3-dehydrogenase +EC 1.1.1.255: mannitol dehydrogenase +EC 1.1.1.256: fluoren-9-ol dehydrogenase +EC 1.1.1.257: 4-(hydroxymethyl)benzenesulfonate dehydrogenase +EC 1.1.1.258: 6-hydroxyhexanoate dehydrogenase +EC 1.1.1.259: 3-hydroxypimeloyl-CoA dehydrogenase +EC 1.1.1.260: sulcatone reductase +EC 1.1.1.261: sn-glycerol-1-phosphate dehydrogenase +EC 1.1.1.262: 4-hydroxythreonine-4-phosphate dehydrogenase +EC 1.1.1.263: 1,5-anhydro-D-fructose reductase +EC 1.1.1.264: L-idonate 5-dehydrogenase +EC 1.1.1.265: 3-methylbutanal reductase +EC 1.1.1.266: dTDP-4-dehydro-6-deoxyglucose reductase +EC 1.1.1.267: 1-deoxy-D-xylulose-5-phosphate reductoisomerase +EC 1.1.1.268: 2-(R)-hydroxypropyl-CoM dehydrogenase +EC 1.1.1.269: 2-(S)-hydroxypropyl-CoM dehydrogenase +EC 1.1.1.270: 3β-hydroxysteroid 3-dehydrogenase +EC 1.1.1.271: GDP-L-fucose synthase +EC 1.1.1.272: D-2-hydroxyacid dehydrogenase (NADP+) +EC 1.1.1.273: vellosimine dehydrogenase +EC 1.1.1.274: 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming) +EC 1.1.1.275: (+)-trans-carveol dehydrogenase +EC 1.1.1.276: serine 3-dehydrogenase (NADP+) +EC 1.1.1.277: 3β-hydroxy-5β-steroid dehydrogenase +EC 1.1.1.278: 3β-hydroxy-5α-steroid dehydrogenase +EC 1.1.1.279: (R)-3-hydroxyacid-ester dehydrogenase +EC 1.1.1.280: (S)-3-hydroxyacid-ester dehydrogenase +EC 1.1.1.281: GDP-4-dehydro-6-deoxy-D-mannose reductase +EC 1.1.1.282: Quinate/shikimate dehydrogenase +EC 1.1.1.283: methylglyoxal reductase (NADPH-dependent) +EC 1.1.1.284: S-(hydroxymethyl)glutathione dehydrogenase +EC 1.1.1.285: 3′′-deamino-3′′-oxonicotianamine reductase +EC 1.1.1.286: isocitrate—homoisocitrate dehydrogenase +EC 1.1.1.287: D-arabinitol dehydrogenase (NADP+) +EC 1.1.1.288: xanthoxin dehydrogenase +EC 1.1.1.289: sorbose reductase +EC 1.1.1.290: 4-phosphoerythronate dehydrogenase +EC 1.1.1.291: 2-hydroxymethylglutarate dehydrogenase +EC 1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming) +EC 1.1.1.293: tropinone reductase I. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-10.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-10.md new file mode 100644 index 000000000..b618ef97b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-10.md @@ -0,0 +1,158 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 11/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.13.11 With incorporation of two atoms of oxygen === +EC 1.13.11.1: catechol 1,2-dioxygenase +EC 1.13.11.2: catechol 2,3-dioxygenase +EC 1.13.11.3: protocatechuate 3,4-dioxygenase +EC 1.13.11.4: gentisate 1,2-dioxygenase +EC 1.13.11.5: homogentisate 1,2-dioxygenase +EC 1.13.11.6: 3-hydroxyanthranilate 3,4-dioxygenase +EC 1.13.11.7: deleted +EC 1.13.11.8: protocatechuate 4,5-dioxygenase +EC 1.13.11.9: 2,5-dihydroxypyridine 5,6-dioxygenase +EC 1.13.11.10: 7,8-dihydroxykynurenate 8,8a-dioxygenase +EC 1.13.11.11: tryptophan 2,3-dioxygenase +EC 1.13.11.12: linoleate 13S-lipoxygenas +EC 1.13.11.13: The activity is the sum of several enzymatic and spontaneous reactions +EC 1.13.11.14: 2,3-dihydroxybenzoate 3,4-dioxygenase +EC 1.13.11.15: 3,4-dihydroxyphenylacetate 2,3-dioxygenase +EC 1.13.11.16: 3-carboxyethylcatechol 2,3-dioxygenase +EC 1.13.11.17: indole 2,3-dioxygenase +EC 1.13.11.18: persulfide dioxygenase +EC 1.13.11.19: cysteamine dioxygenase +EC 1.13.11.20: cysteine dioxygenase +EC 1.13.11.21: Now EC 1.14.99.36, β-carotene 15,15′-monooxygenase +EC 1.13.11.22: caffeate 3,4-dioxygenase +EC 1.13.11.23: 2,3-dihydroxyindole 2,3-dioxygenase +EC 1.13.11.24: quercetin 2,3-dioxygenase +EC 1.13.11.25: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase +EC 1.13.11.26: peptide-tryptophan 2,3-dioxygenase +EC 1.13.11.27: 4-hydroxyphenylpyruvate dioxygenase +EC 1.13.11.28: 2,3-dihydroxybenzoate 2,3-dioxygenase +EC 1.13.11.29: stizolobate synthase +EC 1.13.11.30: stizolobinate synthase +EC 1.13.11.31: arachidonate 12-lipoxygenase +EC 1.13.11.32: Now EC 1.13.12.16, nitronate monooxygenase +EC 1.13.11.33: arachidonate 15-lipoxygenase +EC 1.13.11.34: arachidonate 5-lipoxygenase +EC 1.13.11.35: pyrogallol 1,2-oxygenase +EC 1.13.11.36: chloridazon-catechol dioxygenase +EC 1.13.11.37: hydroxyquinol 1,2-dioxygenase +EC 1.13.11.38: 1-hydroxy-2-naphthoate 1,2-dioxygenase +EC 1.13.11.39: biphenyl-2,3-diol 1,2-dioxygenase +EC 1.13.11.40: arachidonate 8-lipoxygenase +EC 1.13.11.41: 2,4′-dihydroxyacetophenone dioxygenase +EC 1.13.11.42: identical to EC 1.13.11.11, tryptophan 2,3-dioxygenase +EC 1.13.11.43: lignostilbene αβ-dioxygenase +EC 1.13.11.44: Activity is covered by EC 1.13.11.60, linoleate 8R-lipoxygenase and EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase +EC 1.13.11.45: linoleate 11-lipoxygenase +EC 1.13.11.46: 4-hydroxymandelate synthase +EC 1.13.11.47: 3-hydroxy-4-oxoquinoline 2,4-dioxygenase +EC 1.13.11.48: 3-hydroxy-2-methyl-quinolin-4-one 2,4-dioxygenase +EC 1.13.11.49: chlorite O2-lyase +EC 1.13.11.50: acetylacetone-cleaving enzyme +EC 1.13.11.51: 9-cis-epoxycarotenoid dioxygenase +EC 1.13.11.52: indoleamine 2,3-dioxygenase +EC 1.13.11.53: acireductone dioxygenase (Ni2+-requiring) +EC 1.13.11.54: acireductone dioxygenase [iron(II)-requiring] +EC 1.13.11.55: sulfur oxygenase/reductase +EC 1.13.11.56: 1,2-dihydroxynaphthalene dioxygenase +EC 1.13.11.57: gallate dioxygenase +EC 1.13.11.58: linoleate 9S-lipoxygenase +EC 1.13.11.59: torulene dioxygenase +EC 1.13.11.60: inoleate 8R-lipoxygenase +EC 1.13.11.61: linolenate 9R-lipoxygenase +EC 1.13.11.62: linoleate 10R-lipoxygenase +EC 1.13.11.63: β-carotene 15,15′-dioxygenase +EC 1.13.11.64: 5-nitrosalicylate dioxygenase +EC 1.13.11.65: carotenoid isomerooxygenase +EC 1.13.11.66: hydroquinone 1,2-dioxygenase +EC 1.13.11.67: 8′-apo-β-carotenoid 14′,13′-cleaving dioxygenase +EC 1.13.11.68: 9-cis-β-carotene 9′,10′-cleaving dioxygenase +EC 1.13.11.69: carlactone synthase +EC 1.13.11.70: all-trans-10′-apo-β-carotenal 13,14-cleaving dioxygenase +EC 1.13.11.71: carotenoid-9′,10′-cleaving dioxygenase +EC 1.13.11.72: 2-hydroxyethylphosphonate dioxygenase +EC 1.13.11.73: methylphosphonate synthase +EC 1.13.11.74: 2-aminophenol 1,6-dioxygenase +EC 1.13.11.75: all-trans-8′-apo-β-carotenal 15,15′-oxygenase +EC 1.13.11.76: 2-amino-5-chlorophenol 1,6-dioxygenase +EC 1.13.11.77: oleate 10S-lipoxygenase +EC 1.13.11.78: 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming) +EC 1.13.11.79: aerobic 5,6-dimethylbenzimidazole synthase +EC 1.13.11.80: (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase +EC 1.13.11.81: 7,8-dihydroneopterin oxygenase +EC 1.13.11.82: 8′-apo-carotenoid 13,14-cleaving dioxygenase +EC 1.13.11.83: 4-hydroxy-3-prenylphenylpyruvate oxygenase +EC 1.13.11.84: crocetin dialdehyde synthase +EC 1.13.11.85: exo-cleaving rubber dioxygenase +EC 1.13.11.86: 5-aminosalicylate 1,2-dioxygenase +EC 1.13.11.87: endo-cleaving rubber dioxygenase +EC 1.13.11.88: isoeugenol monooxygenase +EC 1.13.11.89: (hydroxymethyl)phosphonate dioxygenase +EC 1.13.11.90: [1-hydroxy-2-(trimethylamino)ethyl]phosphonate dioxygenase (glycine-betaine-forming) +EC 1.13.11.91: 3-mercaptopropionate dioxygenase +EC 1.13.11.92: fatty acid α-dioxygenase + +=== EC 1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases) === +EC 1.13.12.1: arginine 2-monooxygenase +EC 1.13.12.2: lysine 2-monooxygenase +EC 1.13.12.3: tryptophan 2-monooxygenase +EC 1.13.12.4: lactate 2-monooxygenase +EC 1.13.12.5: Renilla-type luciferase +EC 1.13.12.6: Cypridina-luciferin 2-monooxygenase +EC 1.13.12.7: firefly luciferase +EC 1.13.12.8: Watasenia-luciferin 2-monooxygenase +EC 1.13.12.9: phenylalanine 2-monooxygenase +EC 1.13.12.10: Reaction covered by EC 1.14.13.59, L-lysine 6-monooxygenase (NADPH) +EC n1.13.12.11: The activity is due to EC 1.14.13.8, flavin-containing monooxygenase +EC 1.13.12.12: transferred to EC 1.13.11.67, 8-apo-β-carotenoid 14′,13′-cleaving dioxygenase +EC 1.13.12.13: Oplophorus-luciferin 2-monooxygenase +EC 1.13.12.14: Now EC 1.14.13.122, chlorophyllide-a oxygenase +EC 1.13.12.15: 3,4-dihydroxyphenylalanine oxidative deaminase +EC 1.13.12.16: nitronate monooxygenase +EC 1.13.12.17: dichloroarcyriaflavin A synthase +EC 1.13.12.18: dinoflagellate luciferase +EC 1.13.12.19: 2-oxoglutarate dioxygenase (ethene-forming) +EC 1.13.12.20: noranthrone monooxygenase +EC 1.13.12.21: tetracenomycin-F1 monooxygenase +EC 1.13.12.22: deoxynogalonate monooxygenase +EC 1.13.12.23: 4-hydroxy-3-prenylbenzoate synthase +EC 1.13.12.24: calcium-regulated photoprotein + +=== EC 1.13.99 Miscellaneous === +EC 1.13.99.1: inositol oxygenase +EC 1.13.99.2: Now EC 1.14.12.10, benzoate 1,2-dioxygenase +EC 1.13.99.3: tryptophan 2′-dioxygenase +EC 1.13.99.4: Now EC 1.14.12.9, 4-chlorophenylacetate 3,4-dioxygenase +EC 1.13.99.5: now EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase + +== EC 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen == + +=== EC 1.14.1 With NADH or NADPH as one donor (deleted sub-subclass) === +EC 1.14.1.1: now EC 1.14.14.1, unspecific monooxygenase +EC 1.14.1.2: now EC 1.14.13.9, kynurenine 3-monooxygenase +EC 1.14.1.3: deleted, covered by EC 1.14.99.7, squalene monooxygenase and EC 5.4.99.7, lanosterol synthase +EC 1.14.1.4: now EC 1.14.99.2, kynurenine 7,8-hydroxylase +EC 1.14.1.5: now EC 1.14.13.5; imidazoleacetate 4-monooxygenase +EC 1.14.1.6: now EC 1.14.15.4, steroid 11β-monooxygenase +EC 1.14.1.7: now EC 1.14.99.9, steroid 17α-monooxygenase +EC 1.14.1.8: now EC 1.14.99.10, steroid 21-monooxygenase +EC 1.14.1.9: deleted +EC 1.14.1.10: now EC 1.14.99.11 estradiol 6β-monooxygenase +EC 1.14.1.11: deleted + +=== EC 1.14.2 With ascorbate as one donor (deleted sub-subclass) === +EC 1.14.2.1: now EC 1.14.17.1, dopamine β-monooxygenase +EC 1.14.2.2: now EC 1.13.11.27, 4-hydroxyphenylpyruvate dioxygenase + +=== EC 1.14.3 With reduced pteridine as one donor (deleted sub-subclass) === +EC 1.14.3.1: now EC 1.14.16.1, phenylalanine 4-monooxygenase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-11.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-11.md new file mode 100644 index 000000000..c7ba092ef --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-11.md @@ -0,0 +1,117 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 12/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors === +EC 1.14.11.1: γ-butyrobetaine dioxygenase +EC 1.14.11.2: procollagen-proline dioxygenase +EC 1.14.11.3: pyrimidine-deoxynucleoside 2′-dioxygenase +EC 1.14.11.4: procollagen-lysine 5-dioxygenase +EC 1.14.11.5: Now included with EC 1.14.11.6 thymine dioxygenase +EC 1.14.11.6: thymine dioxygenase +EC 1.14.11.7: procollagen-proline 3-dioxygenase +EC 1.14.11.8: trimethyllysine dioxygenase +EC 1.14.11.9: flavanone 3-dioxygenase +EC 1.14.11.10: pyrimidine-deoxynucleoside 1′-dioxygenase +EC 1.14.11.11: hyoscyamine (6S)-dioxygenase +EC 1.14.11.12: gibberellin-44 dioxygenase +EC 1.14.11.13: gibberellin 2β-dioxygenase +EC 1.14.11.14: Now EC 1.14.20.13, 6β-hydroxyhyoscyamine epoxidase +EC 1.14.11.15: gibberellin 3β-dioxygenase +EC 1.14.11.16: peptide-aspartate β-dioxygenase +EC 1.14.11.17: taurine dioxygenase +EC 1.14.11.18: phytanoyl-CoA dioxygenase +EC 1.14.11.19: Now EC 1.14.20.4, anthocyanidin synthase +EC 1.14.11.20: deacetoxyvindoline 4-hydroxylase +EC 1.14.11.21: clavaminate synthase +EC 1.14.11.22: Now EC 1.14.20.5, flavone synthase +EC 1.14.11.23: Now EC 1.14.20.6, flavonol synthase +EC 1.14.11.24: 2′-deoxymugineic-acid 2′-dioxygenase +EC 1.14.11.25: mugineic-acid 3-dioxygenase +EC 1.14.11.26: deacetoxycephalosporin-C hydroxylase +EC 1.14.11.27: [histone H3]-dimethyl-L-lysine36 demethylase +EC 1.14.11.28: proline 3-hydroxylase +EC 1.14.11.29: hypoxia-inducible factor-proline dioxygenase +EC 1.14.11.30: hypoxia-inducible factor-asparagine dioxygenase +EC 1.14.11.31: thebaine 6-O-demethylase +EC 1.14.11.32: codeine 3-O-demethylase +EC 1.14.11.33: DNA oxidative demethylase +EC 1.14.11.34: Now EC 1.14.20.7, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming) +EC 1.14.11.35: 1-deoxypentalenic acid 11β-hydroxylase +EC 1.14.11.36: pentalenolactone F synthase +EC 1.14.11.36: pentalenolactone F synthase +EC 1.14.11.37: kanamycin B dioxygenase +EC 1.14.11.38: verruculogen synthase +EC 1.14.11.39: L-asparagine hydroxylase +EC 1.14.11.40: enduracididine β-hydroxylase +EC 1.14.11.41: L-arginine hydroxylase +EC 1.14.11.42: tRNAPhe (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase +EC 1.14.11.43: (S)-dichlorprop dioxygenase (2-oxoglutarate) +EC 1.14.11.44: (R)-dichlorprop dioxygenase (2-oxoglutarate) +EC 1.14.11.45: L-isoleucine 4-hydroxylase +EC 1.14.11.46: 2-aminoethylphosphonate dioxygenase +EC 1.14.11.47: [50S ribosomal protein L16]-arginine 3-hydroxylase +EC 1.14.11.48: xanthine dioxygenase +EC 1.14.11.49: uridine-5′-phosphate dioxygenase +EC|1.14.11.50: Now EC 1.14.20.8, (–)-deoxypodophyllotoxin synthase +EC 1.14.11.51: DNA N6-methyladenine demethylase +EC 1.14.11.52: validamycin A dioxygenase +EC 1.14.11.53: mRNA N6-methyladenine demethylase +EC 1.14.11.54: mRNA N1-methyladenine demethylase +EC 1.14.11.55: ectoine hydroxylase +EC 1.14.11.56: L-proline cis-4-hydroxylase +EC 1.14.11.57: L-proline trans-4-hydroxylase +EC 1.14.11.58: ornithine lipid ester-linked acyl 2-hydroxylase +EC 1.14.11.59: 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase +EC 1.14.11.60: scopoletin 8-hydroxylase +EC 1.14.11.61: feruloyl-CoA 6-hydroxylase +EC 1.14.11.62: trans-4-coumaroyl-CoA 2-hydroxylase +EC 1.14.11.63: peptidyl-lysine (3S)-dioxygenase +EC 1.14.11.64: glutarate dioxygenase +EC 1.14.11.65: [histone H3]-dimethyl-L-lysine9 demethylase +EC 1.14.11.66: [histone H3]-trimethylL-lysine9 demethylase +EC 1.14.11.67: [histone H3]-trimethyl-LL-lysine4 demethylase +EC 1.14.11.68: [histone H3]-trimethyl-L-lysine27 demethylase +EC 1.14.11.69: [histone H3]-trimethyl-L-lysine37 demethylase +EC 1.14.11.70: 7-deoxycylindrospermopsin hydroxylase +EC 1.14.11.71: methylphosphonate hydroxylase +EC 1.14.11.72: [2-(trimethylamino)ethyl]phosphonate dioxygenase +EC 1.14.11.73: [protein]-arginine 3-hydroxylase +EC 1.14.11.74: L-isoleucine 31-dioxygenase +EC 1.14.11.75: 31-hydroxy-L-isoleucine 4-dioxygenase +EC 1.14.11.76: L-glutamate 3(R)-hydroxylase +EC 1.14.11.77: alkyl sulfatase + +=== EC 1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor === +EC 1.14.12.1: anthranilate 1,2-dioxygenase (deaminating, decarboxylating) +EC 1.14.12.2: Now EC 1.14.13.35 anthranilate 3-monooxygenase (deaminating) +EC 1.14.12.3: benzene 1,2-dioxygenase +EC 1.14.12.4: EC 1.14.13.242, 3-hydroxy-2-methylpyridinecarboxylate monooxygenase +EC 1.14.12.5: Now EC .14.13.241, 5-pyridoxate monooxygenase +EC 1.14.12.6: Now EC 1.14.13.66, 2-hydroxycyclohexanone 2-monooxygenase +EC 1.14.12.7: phthalate 4,5-dioxygenase +EC 1.14.12.8: 4-sulfobenzoate 3,4-dioxygenase +EC 1.14.12.9: 4-chlorophenylacetate 3,4-dioxygenase +EC 1.14.12.10: benzoate 1,2-dioxygenase +EC 1.14.12.11: toluene dioxygenase +EC 1.14.12.12: naphthalene 1,2-dioxygenase +EC 1.14.12.13: 2-halobenzoate 1,2-dioxygenase +EC 1.14.12.14: 2-aminobenzenesulfonate 2,3-dioxygenase +EC 1.14.12.15: terephthalate 1,2-dioxygenase +EC 1.14.12.16: 2-hydroxyquinoline 5,6-dioxygenase +EC 1.14.12.17: nitric oxide dioxygenase +EC 1.14.12.18: biphenyl 2,3-dioxygenase +EC 1.14.12.19: 3-phenylpropionate dioxygenase +EC 1.14.12.20: Now classified as EC 1.14.15.17, pheophorbide a oxygenase. +EC 1.14.12.21: Now EC 1.14.13.208, benzoyl-CoA 2,3-epoxidase +EC 1.14.12.22: carbazole 1,9a-dioxygenase +EC 1.14.12.23: nitroarene dioxygenase +EC 1.14.12.24: 2,4-dinitrotoluene dioxygenase +EC 1.14.12.25: p-cumate 2,3-dioxygenase +EC 1.14.12.26: chlorobenzene dioxygenase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-12.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-12.md new file mode 100644 index 000000000..82d75b066 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-12.md @@ -0,0 +1,150 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 13/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor === +EC 1.14.13.1: salicylate 1-monooxygenase +EC 1.14.13.2: 4-hydroxybenzoate 3-monooxygenase +EC 1.14.13.3: Now EC 1.14.14.9, 4-hydroxyphenylacetate 3-monooxygenase +EC 1.14.13.4: melilotate 3-monooxygenase +EC 1.14.13.5: imidazoleacetate 4-monooxygenase +EC 1.14.13.6: orcinol 2-monooxygenase +EC 1.14.13.7: phenol 2-monooxygenase +EC 1.14.13.8: flavin-containing monooxygenase +EC 1.14.13.9: kynurenine 3-monooxygenase +EC 1.14.13.10: 2,6-dihydroxypyridine 3-monooxygenase +EC 1.14.13.11: Now EC 1.14.14.91, trans-cinnamate 4-monooxygenase +EC 1.14.13.12: Now EC 1.14.14.92, benzoate 4-monooxygenase +EC 1.14.13.13: Now classified as EC 1.14.15.18, calcidiol 1-monooxygenase +EC 1.14.13.14: trans-cinnamate 2-monooxygenase +EC 1.14.13.15: Now EC 1.14.15.15, cholestanetriol 26-monooxygenase +EC 1.14.13.16: cyclopentanone monooxygenase +EC 1.14.13.17: Now EC 1.14.14.23, cholesterol 7α-monooxygenase +EC 1.14.13.18: 4-hydroxyphenylacetate 1-monooxygenase +EC 1.14.13.19: taxifolin 8-monooxygenase +EC 1.14.13.20: 2,4-dichlorophenol 6-monooxygenase +EC 1.14.13.21: Now EC 1.14.14.82, flavonoid 3′-monooxygenase +EC 1.14.13.22: cyclohexanone monooxygenase +EC 1.14.13.23: 3-hydroxybenzoate 4-monooxygenase +EC 1.14.13.24: 3-hydroxybenzoate 6-monooxygenase +EC 1.14.13.25: methane monooxygenase (soluble) +EC 1.14.13.26: Now classified as EC 1.14.18.4, phosphatidylcholine 12-monooxygenase +EC 1.14.13.27: 4-aminobenzoate 1-monooxygenase +EC 1.14.13.28: Now EC 1.14.14.93, 3,9-dihydroxypterocarpan 6a-monooxygenase +EC 1.14.13.29: 4-nitrophenol 2-monooxygenase +EC 1.14.13.30: Now EC 1.14.14.94, leukotriene-B4 20-monooxygenase +EC 1.14.13.31: 2-nitrophenol 2-monooxygenase +EC 1.14.13.32: albendazole monooxygenase +EC 1.14.13.33: 4-hydroxybenzoate 3-monooxygenase (NAD(P)H) +EC 1.14.13.34: leukotriene-E4 20-monooxygenase +EC 1.14.13.35: anthranilate 3-monooxygenase (deaminating) +EC 1.14.13.36: Now EC 1.14.14.96, 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase +EC 1.14.13.37: Now EC 1.14.14.97, methyltetrahydroprotoberberine 14-monooxygenase +EC 1.14.13.38: anhydrotetracycline monooxygenase +EC 1.14.13.39: nitric-oxide synthase +EC 1.14.13.40: anthraniloyl-CoA monooxygenase +EC 1.14.13.41: Now EC 1.14.14.36, tyrosine N-monooxygenase +EC 1.14.13.42: The activity is covered by EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase +EC 1.14.13.43: questin monooxygenase +EC 1.14.13.44: 2-hydroxybiphenyl 3-monooxygenase +EC 1.14.13.45: Now EC 1.14.18.2, CMP-N-acetylneuraminate monooxygenase +EC 1.14.13.46: (-)-menthol monooxygenase +EC 1.14.13.47: Now EC 1.14.14.99, (S)-limonene 3-monooxygenase +EC 1.14.13.48: Now classified as EC 1.14.14.51, (S)-limonene 6-monooxygenase +EC 1.14.13.49: Now classified as EC 1.14.14.52, (S)-limonene 7-monooxygenase +EC 1.14.13.50: pentachlorophenol monooxygenase +EC 1.14.13.51: 6-oxocineole dehydrogenase +EC 1.14.13.52: Now EC 1.14.14.88, isoflavone 3′-hydroxylase +EC 1.14.13.53: Now EC 1.14.14.89, 4′-methoxyisoflavone 2′-hydroxylase +EC 1.14.13.54: ketosteroid monooxygenase +EC 1.14.13.55: Now EC 1.14.14.98, protopine 6-monooxygenase +EC 1.14.13.56: Now EC 1.14.14.100, dihydrosanguinarine 10-monooxygenase +EC 1.14.13.57: Now EC 1.14.14.101, dihydrochelirubine 12-monooxygenase +EC 1.14.13.58: benzoyl-CoA 3-monooxygenase +EC 1.14.13.59: L-lysine N6-monooxygenase (NADPH) +EC 1.14.13.60: Now included with EC 1.14.13.100, 25-hydroxycholesterol 7α-hydroxylase +EC 1.14.13.61: 2-hydroxyquinoline 8-monooxygenase +EC 1.14.13.62: 4-hydroxyquinoline 3-monooxygenase +EC 1.14.13.63: 3-hydroxyphenylacetate 6-hydroxylase +EC 1.14.13.64: 4-hydroxybenzoate 1-hydroxylase +EC 1.14.13.65: deleted +EC 1.14.13.66: 2-hydroxycyclohexanone 2-monooxygenase +EC 1.14.13.67: Now EC 1.14.14.55, quinine 3-monooxygenase +EC 1.14.13.68: Now EC 1.14.14.37, 4-hydroxyphenylacetaldehyde oxime monooxygenase +EC 1.14.13.69: alkene monooxygenase +EC 1.14.13.70: Now EC 1.14.14.154, sterol 14α-demethylase +EC 1.14.13.71: Now EC 1.14.14.102, N-methylcoclaurine 3′-monooxygenase +EC 1.14.13.72: Now classified as EC 1.14.18.9, methylsterol monooxygenase +EC 1.14.13.73: Now EC 1.14.14.103, tabersonine 16-hydroxylase +EC 1.14.13.74: Now EC 1.14.14.85, 7-deoxyloganin 7-hydroxylase +EC 1.14.13.75: Now EC 1.14.14.104, vinorine hydroxylase +EC 1.14.13.76: Now EC 1.14.14.105, taxane 10β-hydroxylase +EC 1.14.13.77: Now EC 1.14.14.106, taxane 13α-hydroxylase +EC 1.14.13.78: Now EC 1.14.14.86, ent-kaurene monooxygenase +EC 1.14.13.79: Now EC 1.14.14.107, ent-kaurenoic acid oxidase +EC 1.14.13.80: Now classified as EC 1.14.14.53, (R)-limonene 6-monooxygenase +EC 1.14.13.81: magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase +EC 1.14.13.82: vanillate monooxygenase +EC 1.14.13.83: precorrin-3B synthase +EC 1.14.13.84: 4-hydroxyacetophenone monooxygenase +EC 1.14.13.85: Now EC 1.14.14.135, glyceollin synthase +EC 1.14.13.86: The activity is covered by EC 1.14.14.87, 2-hydroxyisoflavanone synthase +EC 1.14.13.87: Now EC 1.14.14.140, licodione synthase] +EC 1.14.13.88: Now EC 1.14.14.81, flavanoid 3,5-hydroxylase +EC 1.14.13.89: Now EC 1.14.14.90, isoflavone 2-hydroxylase +EC 1.14.13.90: Now EC 1.14.15.21, zeaxanthin epoxidase +EC 1.14.13.91: Now EC 1.14.14.136, deoxysarpagine hydroxylase +EC 1.14.13.92: phenylacetone monooxygenase +EC 1.14.13.93: Now EC 1.14.14.137, (+)-abscisic acid 8-hydroxylase +EC 1.14.13.94: Now EC 1.14.14.138, lithocholate 6β-hydroxylase +EC 1.14.13.95: Now included with EC 1.14.14.139, 5β-cholestane-3α,7α-diol 12α-hydroxylase +EC 1.14.13.96: Now EC 1.14.14.139, 5β-cholestane-3α,7α-diol 12α-hydroxylase +EC 1.14.13.97: Now EC 1.14.14.57, taurochenodeoxycholate 6α-hydroxylase +EC 1.14.13.98: Now EC 1.14.14.25, cholesterol 24-hydroxylase +EC 1.14.13.99: Now EC 1.14.14.26, 24-hydroxycholesterol 7α-hydroxylase +EC 1.14.13.100: Now classified as EC 1.14.14.29, 25/26-hydroxycholesterol 7α-hydroxylase +EC 1.14.13.101: senecionine N-oxygenase +EC 1.14.13.102: Now EC 1.14.14.141, psoralen synthase +EC 1.14.13.103: Now EC 1.14.14.142, 8-dimethylallylnaringenin 2-hydroxylase +EC 1.14.13.104: Now EC 1.14.14.143, (+)-menthofuran synthase +EC 1.14.13.105: monocyclic monoterpene ketone monooxygenase +EC 1.14.13.106: now classified as EC 1.14.15.39, epi-isozizaene 5-monooxygenase. EC 1.14.13.107: limonene 1,2-monooxygenase +EC 1.14.13.108: Now EC 1.14.14.144, abieta-7,13-diene hydroxylase +EC 1.14.13.109: Now EC 1.14.14.145, abieta-7,13-dien-18-ol hydroxylase +EC 1.14.13.110: Now EC 1.14.14.146, geranylgeraniol 18-hydroxylase +EC 1.14.13.111: methanesulfonate monooxygenase +EC 1.14.13.112: Now EC 1.14.14.147, 3-epi-6-deoxocathasterone 23-monooxygenase +EC 1.14.13.113: FAD-dependent urate hydroxylase +EC 1.14.13.114: 6-hydroxynicotinate 3-monooxygenase +EC 1.14.13.115: Now EC 1.14.14.148, angelicin synthase +EC 1.14.13.116: Now EC 1.14.14.174, geranylhydroquinone 3-hydroxylase +EC 1.14.13.117: Now EC 1.14.14.39, isoleucine N-monooxygenase +EC 1.14.13.118: Now EC 1.14.14.38, valine N-monooxygenase +EC 1.14.13.119: Now EC 1.14.14.149, 5-epiaristolochene 1,3-dihydroxylase +EC 1.14.13.120: Now EC 1.14.14.150, costunolide synthase +EC 1.14.13.121: Now EC 1.14.14.151, premnaspirodiene oxygenase +EC 1.14.13.122: chlorophyllide-a oxygenase +EC 1.14.13.123: Now EC 1.14.14.95, germacrene A hydroxylase +EC 1.14.13.124: now classified as EC 1.14.14.40, phenylalanine N-monooxygenase +EC 1.14.13.125: Now EC 1.14.14.156, tryptophan N-monooxygenase +EC 1.14.13.126: Now EC 1.14.15.16, vitamin D3 24-hydroxylase +EC 1.14.13.127: 3-(3-hydroxyphenyl)propanoate hydroxylase +EC 1.14.13.128: 7-methylxanthine demethylase +EC 1.14.13.129: Now EC 1.14.15.24, β-carotene 3-hydroxylase +EC 1.14.13.130: pyrrole-2-carboxylate monooxygenase +EC 1.14.13.131: dimethyl-sulfide monooxygenase +EC 1.14.13.132: Now EC 1.14.14.17, squalene monooxygenase +EC 1.14.13.133: Now EC 1.14.15.32, pentalenene oxygenase +EC 1.14.13.134: Now EC 1.14.14.152, β-amyrin 11-oxidase +EC 1.14.13.135: 1-hydroxy-2-naphthoate hydroxylase +EC 1.14.13.136: Now EC 1.14.14.87, 2-hydroxyisoflavanone synthase +EC 1.14.13.137: Now EC 1.14.14.153, indole-2-monooxygenase +EC 1.14.13.138: Now EC 1.14.14.157, indolin-2-one monooxygenase +EC 1.14.13.139: Now EC 1.14.14.109, 3-hydroxyindolin-2-one monooxygenase +EC 1.14.13.140: Now EC 1.14.14.110, 2-hydroxy-1,4-benzoxazin-3-one monooxygenase. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-13.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-13.md new file mode 100644 index 000000000..273c79be4 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-13.md @@ -0,0 +1,117 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 14/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +EC 1.14.13.141: Now EC 1.14.15.29, cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] +EC 1.14.13.142: Now EC 1.14.15.30, 3-ketosteroid 9α-monooxygenase +EC 1.14.13.143: Now EC 1.14.14.76 ent-isokaurene C2/C3-hydroxylase +EC 1.14.13.144: Now EC 1.14.14.111, 9β-pimara-7,15-diene oxidase +EC 1.14.13.145: Now EC 1.14.14.112, ent-cassa-12,15-diene 11-hydroxylase +EC 1.14.13.146: taxoid 14β-hydroxylase +EC 1.14.13.147: Now EC 1.14.14.182, taxoid 7β-hydroxylase +EC 1.14.13.148: trimethylamine monooxygenase +EC 1.14.13.149: phenylacetyl-CoA 1,2-epoxidase +EC 1.14.13.150: Now EC 1.14.14.113, α-humulene 10-hydroxylase +EC 1.14.13.151: Now EC 1.14.14.84, linalool 8-monooxygenase +EC 1.14.13.152: Now EC 1.14.14.83, geraniol 8-hydroxylase +EC 1.14.13.153: (+)-sabinene 3-hydroxylase +EC 1.14.13.154: erythromycin 12-hydroxylase +EC 1.14.13.155: α-pinene monooxygenase +EC 1.14.13.156: Now EC 1.14.14.133, 1,8-cineole 2-endo-monooxygenase +EC 1.14.13.157: Now EC 1.14.14.56, 1,8-cineole 2-exo-monooxygenase +EC 1.14.13.158: Now EC 1.14.14.114, amorpha-4,11-diene 12-monooxygenase +EC 1.14.13.159: Now EC 1.14.14.24, vitamin D 25-hydroxylase +EC 1.14.13.160: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase +EC 1.14.13.161: (+)-camphor 6-exo-hydroxylase +EC 1.14.13.162: Now EC 1.14.14.108, 2,5-diketocamphane 1,2-monooxygenase +EC 1.14.13.163: 6-hydroxy-3-succinoylpyridine 3-monooxygenase +EC 1.14.13.164: withdrawn: see EC 1.13.11.65, carotenoid isomerooxygenase +EC 1.14.13.165: Now classified as EC 1.14.14.47, nitric-oxide synthase (flavodoxin) +EC 1.14.13.166: 4-nitrocatechol 4-monooxygenase +EC 1.14.13.167: 4-nitrophenol 4-monooxygenase +EC 1.14.13.168: indole-3-pyruvate monooxygenase +EC 1.14.13.169: Now EC 1.14.18.5, sphingolipid C4-monooxygenase +EC 1.14.13.170: pentalenolactone D synthase +EC 1.14.13.171: neopentalenolactone D synthase +EC 1.14.13.172: salicylate 5-hydroxylase +EC 1.14.13.173: Now EC 1.14.14.115, 11-oxo-β-amyrin 30-oxidase +EC 1.14.13.174: Now EC 1.14.14.116, averantin hydroxylase +EC 1.14.13.175: Now EC 1.14.14.117, aflatoxin B synthase +EC 1.14.13.176: Now EC 1.14.14.118, tryprostatin B 6-hydroxylase +EC 1.14.13.177: Now EC 1.14.14.119, fumitremorgin C monooxygenase +EC 1.14.13.178: methylxanthine N1-demethylase +EC 1.14.13.179: methylxanthine N3-demethylase +EC 1.14.13.180: aklavinone 12-hydroxylase +EC 1.14.13.181: 13-deoxydaunorubicin hydroxylase +EC 1.14.13.182: 2-heptyl-3-hydroxy-4(1H)-quinolone synthase +EC 1.14.13.183: Now EC 1.14.14.120, dammarenediol 12-hydroxylase +EC 1.14.13.184: Now EC 1.14.14.121, protopanaxadiol 6-hydroxylase +EC 1.14.13.185: Now EC 1.14.15.33, pikromycin synthase +EC 1.14.13.186: Now EC 1.14.15.34, 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase +EC 1.14.13.187: L-evernosamine nitrososynthase +EC 1.14.13.188: Now EC 1.14.15.35, 6-deoxyerythronolide B hydroxylase +EC 1.14.13.189: 5-methyl-1-naphthoate 3-hydroxylase +EC 1.14.13.190: Now EC 1.14.14.175, ferruginol synthase +EC 1.14.13.191: Now EC 1.14.14.70, ent-sandaracopimaradiene 3-hydroxylase +EC 1.14.13.192: Now EC 1.14.14.122, oryzalexin E synthase +EC 1.14.13.193: Now EC 1.14.14.123, oryzalexin D synthase +EC 1.14.13.194: Now EC 1.14.14.78, phylloquinone ω-hydroxylase +EC 1.14.13.195: L-ornithine N5-monooxygenase (NADPH) +EC 1.14.13.196: L-ornithine N5-monooxygenase [NAD(P)H] +EC 1.14.13.197: Now EC 1.14.14.124, dihydromonacolin L hydroxylase +EC 1.14.13.198: Now EC 1.14.14.125, monacolin L hydroxylase +EC 1.14.13.199: Now EC 1.14.14.79, docosahexaenoic acid ω-hydroxylase +EC 1.14.13.200: tetracenomycin A2 monooxygenase-dioxygenase +EC 1.14.13.201: Now EC 1.14.14.126, β-amyrin 28-monooxygenase +EC 1.14.13.202: Now EC 1.14.14.127, methyl farnesoate epoxidase +EC 1.14.13.203: Now EC 1.14.14.128, farnesoate epoxidase +EC 1.14.13.204: Now EC 1.14.14.129, long-chain acyl-CoA ω-monooxygenase +EC 1.14.13.205: Now EC 1.14.14.80, long-chain fatty acid ω-monooxygenase +EC 1.14.13.206: Now EC 1.14.14.130, laurate 7-monooxygenase +EC 1.14.13.207: Now EC 1.14.14.31, ipsdienol synthase +EC 1.14.13.208: benzoyl-CoA 2,3-epoxidase +EC 1.14.13.209: salicyloyl-CoA 5-hydroxylase +EC 1.14.13.210: 4-methyl-5-nitrocatechol 5-monooxygenase +EC 1.14.13.211: rifampicin monooxygenase +EC 1.14.13.212: 1,3,7-trimethyluric acid 5-monooxygenase +EC 1.14.13.213: Now EC 1.14.14.131, bursehernin 5-monooxygenase +EC 1.14.13.214: Now EC 1.14.14.132, (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase +EC 1.14.13.215: protoasukamycin 4-monooxygenase +EC 1.14.13.216: asperlicin C monooxygenase +EC 1.14.13.217: protodeoxyviolaceinate monooxygenase +EC 1.14.13.218: 5-methylphenazine-1-carboxylate 1-monooxygenase +EC 1.14.13.219: resorcinol 4-hydroxylase (NADPH) +EC 1.14.13.220: resorcinol 4-hydroxylase (NADH) +EC 1.14.13.221: Now EC 1.14.15.28, cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] +EC 1.14.13.222: aurachin C monooxygenase/isomerase +EC 1.14.13.223: 3-hydroxy-4-methylanthranilyl-[aryl-carrier protein] 5-monooxygenase +EC 1.14.13.224: violacein synthase +EC 1.14.13.225: F-actin monooxygenase +EC 1.14.13.226: acetone monooxygenase (methyl acetate-forming) +EC 1.14.13.227: propane 2-monooxygenase +EC 1.14.13.228: jasmonic acid 12-hydroxylase +EC 1.14.13.229: tert-butyl alcohol monooxygenase +EC 1.14.13.230: butane monooxygenase (soluble) +EC 1.14.13.231: tetracycline 11a-monooxygenase +EC 1.14.13.232: 6-methylpretetramide 4-monooxygenase +EC 1.14.13.233: 4-hydroxy-6-methylpretetramide 12a-monooxygenase +EC 1.14.13.234: 5a,11a-dehydrotetracycline 5-monooxygenase +EC 1.14.13.235: indole-3-acetate monooxygenase +EC 1.14.13.236: toluene 4-monooxygenase +EC 1.14.13.237: aliphatic glucosinolate S-oxygenase +EC 1.14.13.238: dimethylamine monooxygenase +EC 1.14.13.239: carnitine monooxygenase +EC 1.14.13.240: 2-polyprenylphenol 6-hydroxylase +EC 1.14.13.241: 5-pyridoxate monooxygenase +EC 1.14.13.242: 3-hydroxy-2-methylpyridine-5-carboxylate monooxygenase +EC 1.14.13.243: toluene 2-monooxygenase +EC 1.14.13.244: phenol 2-monooxygenase (NADH) +EC 1.14.13.245: assimilatory dimethylsulfide S-monooxygenase +EC 1.14.13.246: 4β-methylsterol monooxygenase +EC 1.14.13.247: stachydrine N-demethylase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-14.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-14.md new file mode 100644 index 000000000..263f2100f --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-14.md @@ -0,0 +1,190 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 15/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen === +EC 1.14.14.1: unspecific monooxygenase +EC 1.14.14.2: Now included with EC 1.14.14.1 unspecific monooxygenase +EC 1.14.14.3: alkanal monooxygenase (FMN-linked) +EC 1.14.14.4: identical to EC 1.14.15.7, choline monooxygenase. +EC 1.14.14.5: alkanesulfonate monooxygenase +EC 1.14.14.6: Now EC 1.14.13.111, methanesulfonate monooxygenase +EC 1.14.14.7: transferred to EC 1.14.19.9, tryptophan 7-halogenase +EC 1.14.14.8: anthranilate 3-monooxygenase (FAD) +EC 1.14.14.9: 4-hydroxyphenylacetate 3-monooxygenase +EC 1.14.14.10: nitrilotriacetate monooxygenase +EC 1.14.14.11: styrene monooxygenase +EC 1.14.14.12: 3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase +EC 1.14.14.13: 4-(γ-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase +EC 1.14.14.14: aromatase +EC 1.14.14.15: (3S)-3-amino-3-(3-chloro-4-hydroxyphenyl)propanoyl-[peptidyl-carrier protein SgcC2] monooxygenase +EC 1.14.14.16: steroid 21-monooxygenase +EC 1.14.14.17: squalene monooxygenase +EC 1.14.14.18: heme oxygenase (biliverdin-producing) +EC 1.14.14.19: steroid 17α-monooxygenase +EC 1.14.14.20: phenol 2-monooxygenase (FADH2) +EC 1.14.14.21: dibenzothiophene monooxygenase +EC 1.14.14.22: dibenzothiophene sulfone monooxygenase +EC 1.14.14.23: cholesterol 7α-monooxygenase +EC 1.14.14.24: vitamin D 25-hydroxylase +EC 1.14.14.25: cholesterol 24-hydroxylase +EC 1.14.14.26: 24-hydroxycholesterol 7α-hydroxylase +EC 1.14.14.27: resorcinol 4-hydroxylase (FADH2) +EC 1.14.14.28: long-chain alkane monooxygenase +EC 1.14.14.29: 25/26-hydroxycholesterol 7α-hydroxylase +EC 1.14.14.30: isobutylamine N-monooxygenase +EC 1.14.14.31: ipsdienol synthase +EC 1.14.14.32: 17α-hydroxyprogesterone deacetylase +EC 1.14.14.33: ethylenediaminetetraacetate monooxygenase +EC 1.14.14.34: methanesulfonate monooxygenase (FMNH2) +EC 1.14.14.35: dimethylsulfone monooxygenase +EC 1.14.14.36: tyrosine N-monooxygenase +EC 1.14.14.37: 4-hydroxyphenylacetaldehyde oxime monooxygenase +EC 1.14.14.38: valine N-monooxygenase +EC 1.14.14.39: isoleucine N-monooxygenase +EC 1.14.14.40: phenylalanine N-monooxygenase +EC 1.14.14.41: (E)-2-methylbutanal oxime monooxygenase +EC 1.14.14.42: homomethionine N-monooxygenase +EC 1.14.14.43: (methylsulfanyl)alkanaldoxime N-monooxygenase +EC 1.14.14.44: phenylacetaldehyde oxime monooxygenase +EC 1.14.14.45: aromatic aldoxime N-monooxygenase +EC 1.14.14.46: pimeloyl-[acyl-carrier protein] synthase +EC 1.14.14.47: nitric-oxide synthase (flavodoxin) +EC 1.14.14.48: jasmonoyl-L-amino acid 12-hydroxylase +EC 1.14.14.49: 12-hydroxyjasmonoyl-L-amino acid 12-hydroxylase +EC 1.14.14.50: tabersonine 3-oxygenase +EC 1.14.14.51: (S)-limonene 6-monooxygenase +EC 1.14.14.52: (S)-limonene 7-monooxygenase +EC 1.14.14.53: (R)-limonene 6-monooxygenase +EC 1.14.14.54: phenylacetate 2-hydroxylase +EC 1.14.14.55: quinine 3-monooxygenase +EC 1.14.14.56: 1,8-cineole 2-exo-monooxygenase +EC 1.14.14.57: taurochenodeoxycholate 6α-hydroxylase +EC 1.14.14.58: trimethyltridecatetraene synthase +EC 1.14.14.59: dimethylnonatriene synthase +EC 1.14.14.60: ferruginol monooxygenase +EC 1.14.14.61: carnosic acid synthase +EC 1.14.14.62: salviol synthase +EC 1.14.14.63: β-amyrin 16β-monooxygenase +EC 1.14.14.64: β-amyrin 6β-monooxygenase +EC 1.14.14.65: sugiol synthase +EC 1.14.14.66: marmesin synthase +EC 1.14.14.67: 11-hydroxysugiol 20-monooxygenase +EC 1.14.14.68: syn-pimaradiene 3-monooxygenase +EC 1.14.14.69: ent-cassadiene hydroxylase +EC 1.14.14.70: ent-sandaracopimaradiene 3-hydroxylase +EC 1.14.14.71: cucurbitadienol 11-hydroxylase +EC 1.14.14.72: drimenol monooxygenase +EC 1.14.14.73: albendazole monooxygenase (sulfoxide-forming) +EC 1.14.14.74: albendazole monooxygenase (hydroxylating) +EC 1.14.14.75: fenbendazole monooxygenase (4′-hydroxylating) +EC 1.14.14.76: ent-isokaurene C2/C3-hydroxylase +EC 1.14.14.77: phenylacetonitrile α-monooxygenase +EC 1.14.14.78: phylloquinone ω-hydroxylase +EC 1.14.14.79: docosahexaenoic acid ω-hydroxylase +EC 1.14.14.80: long-chain fatty acid ω-monooxygenase +EC 1.14.14.81: flavanoid 3′,5′-hydroxylase +EC 1.14.14.82: flavonoid 3′-monooxygenase +EC 1.14.14.83: geraniol 8-hydroxylase +EC 1.14.14.84: linalool 8-monooxygenase +EC 1.14.14.85: 7-deoxyloganate 7-hydroxylase +EC 1.14.14.86: ent-kaurene monooxygenase +EC 1.14.14.87: 2-hydroxyisoflavanone synthase +EC 1.14.14.88: isoflavone 3′-hydroxylase +EC 1.14.14.89: 4′-methoxyisoflavone 2′-hydroxylase +EC 1.14.14.90: isoflavone 2′-hydroxylase +EC 1.14.14.91: trans-cinnamate 4-monooxygenase +EC 1.14.14.92: benzoate 4-monooxygenase +EC 1.14.14.93: 3,9-dihydroxypterocarpan 6a-monooxygenase +EC 1.14.14.94: leukotriene-B4 20-monooxygenase +EC 1.14.14.95: germacrene A hydroxylase +EC 1.14.14.96: 5-O-(4-coumaroyl)-D-quinate 3′-monooxygenase +EC 1.14.14.97: methyltetrahydroprotoberberine 14-monooxygenase +EC 1.14.14.98: protopine 6-monooxygenase +EC 1.14.14.99: (S)-limonene 3-monooxygenase +EC 1.14.14.100: dihydrosanguinarine 10-monooxygenase +EC 1.14.14.101: dihydrochelirubine 12-monooxygenase +EC 1.14.14.102: N-methylcoclaurine 3′-monooxygenase +EC 1.14.14.103: tabersonine 16-hydroxylase +EC 1.14.14.104: vinorine hydroxylase +EC 1.14.14.105: taxane 10β-hydroxylase +EC 1.14.14.106: taxane 13α-hydroxylase +EC 1.14.14.107: ent-kaurenoic acid monooxygenase +EC 1.14.14.108: 2,5-diketocamphane 1,2-monooxygenase +EC 1.14.14.109: 3-hydroxyindolin-2-one monooxygenase +EC 1.14.14.110: 2-hydroxy-1,4-benzoxazin-3-one monooxygenase +EC 1.14.14.111: 9β-pimara-7,15-diene oxidase +EC 1.14.14.112: ent-cassa-12,15-diene 11-hydroxylase +EC 1.14.14.113: α-humulene 10-hydroxylase +EC 1.14.14.114: amorpha-4,11-diene 12-monooxygenase +EC 1.14.14.115: 11-oxo-β-amyrin 30-oxidase +EC 1.14.14.116: averantin hydroxylase +EC 1.14.14.117: aflatoxin B synthase +EC 1.14.14.118: tryprostatin B 6-hydroxylase +EC 1.14.14.119: fumitremorgin C monooxygenase +EC 1.14.14.120: dammarenediol 12-hydroxylase +EC 1.14.14.121: protopanaxadiol 6-hydroxylase +EC 1.14.14.122: oryzalexin E synthase +EC 1.14.14.123: oryzalexin D synthase +EC 1.14.14.124: dihydromonacolin L hydroxylase +EC 1.14.14.125: monacolin L hydroxylase +EC 1.14.14.126: β-amyrin 28-monooxygenase +EC 1.14.14.127: methyl farnesoate epoxidase +EC 1.14.14.128: farnesoate epoxidase +EC 1.14.14.129: long-chain acyl-CoA ω-monooxygenase +EC 1.14.14.130: laurate 7-monooxygenase +EC 1.14.14.131: bursehernin 5′-monooxygenase +EC 1.14.14.132: (–)-4′-demethyl-deoxypodophyllotoxin 4-hydroxylase +EC 1.14.14.133: 1,8-cineole 2-endo-monooxygenase +EC 1.14.14.134: β-amyrin 24-hydroxylase +EC 1.14.14.135: glyceollin synthase +EC 1.14.14.136: deoxysarpagine hydroxylase +EC 1.14.14.137: (+)-abscisic acid 8′-hydroxylase +EC 1.14.14.138: lithocholate 6β-hydroxylase +EC 1.14.14.139: 5β-cholestane-3α,7α-diol 12α-hydroxylase +EC 1.14.14.140: Now included with EC 1.14.14.162 EC 1.14.14.162, flavanone 2-hydroxylase +EC 1.14.14.141: psoralen synthase +EC 1.14.14.142: 8-dimethylallylnaringenin 2′-hydroxylase +EC 1.14.14.143: (+)-menthofuran synthase +EC 1.14.14.144: abieta-7,13-diene hydroxylase +EC 1.14.14.145: abieta-7,13-dien-18-ol hydroxylase +EC 1.14.14.146: geranylgeraniol 18-hydroxylase +EC 1.14.14.147: 3-epi-6-deoxocathasterone 23-monooxygenase +EC 1.14.14.148: angelicin synthase +EC 1.14.14.149: 5-epiaristolochene 1,3-dihydroxylase +EC 1.14.14.150: costunolide synthase +EC 1.14.14.151: premnaspirodiene oxygenase +EC 1.14.14.152: β-amyrin 11-oxidase +EC 1.14.14.153: indole-2-monooxygenase +EC 1.14.14.154: sterol 14α-demethylase +EC 1.14.14.155: 3,6-diketocamphane 1,2-monooxygenase +EC 1.14.14.156: tryptophan N-monooxygenase +EC 1.14.14.157: indolin-2-one monooxygenase +EC 1.14.14.158: carotenoid ε hydroxylase +EC 1.14.14.159: dolabradiene monooxygenase +EC 1.14.14.160: zealexin A1 synthase +EC 1.14.14.161: nepetalactol monooxygenase +EC 1.14.14.162: flavanone 2-hydroxylase +EC 1.14.14.163: (S)-1-hydroxy-N-methylcanadine 13-hydroxylase +EC 1.14.14.164: fraxetin 5-hydroxylase +EC 1.14.14.165: indole-3-carbonyl nitrile 4-hydroxylase +EC 1.14.14.166: (S)-N-methylcanadine 1-hydroxylase +EC 1.14.14.167: (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine 8-hydroxylase +EC 1.14.14.168: germacrene A acid 8β-hydroxylase +EC 1.14.14.169: eupatolide synthase +EC 1.14.14.170: 8-epi-inunolide synthase +EC 1.14.14.171: β-amyrin 16α-hydroxylase +EC 1.14.14.172: 3,5,6-trichloropyridin-2-ol monooxygenase +EC 1.14.14.173: 2,4,6-trichlorophenol monooxygenase +EC 1.14.14.174: geranylhydroquinone 3′′-hydroxylase +EC 1.14.14.175: ferruginol synthase +EC 1.14.14.176: taxadiene 5α-hydroxylase +EC 1.14.14.177: ultra-long-chain fatty acid ω-hydroxylase +EC 1.14.14.182: taxoid 7beta-hydroxylase +EC 1.14.14.197: progesterone 11alpha-monooxygenase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-15.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-15.md new file mode 100644 index 000000000..57a37f036 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-15.md @@ -0,0 +1,190 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 16/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.14.15 With reduced iron–sulfur protein as one donor, and incorporation of one atom of oxygen === +EC 1.14.15.1: camphor 5-monooxygenase +EC 1.14.15.2: Now EC 1.14.13.162, 2,5-diketocamphane 1,2-monooxygenase. +EC 1.14.15.3: alkane 1-monooxygenase +EC 1.14.15.4: steroid 11β-monooxygenase +EC 1.14.15.5: corticosterone 18-monooxygenase +EC 1.14.15.6: cholesterol monooxygenase (side-chain-cleaving) +EC 1.14.15.7: choline monooxygenase +EC 1.14.15.8: steroid 15β-monooxygenase +EC 1.14.15.9: spheroidene monooxygenase +EC 1.14.15.10: (+)-camphor 6-endo-hydroxylase +EC 1.14.15.11: pentalenic acid synthase +EC 1.14.15.12 : pimeloyl-[acyl-carrier protein] synthase. Now EC 1.14.14.46, pimeloyl-[acyl-carrier protein] synthase +EC 1.14.15.13: pulcherriminic acid synthase +EC 1.14.15.14: methyl-branched lipid ω-hydroxylase +EC 1.14.15.15: cholestanetriol 26-monooxygenase +EC 1.14.15.16: vitamin D3 24-hydroxylase +EC 1.14.15.17: pheophorbide a oxygenase +EC 1.14.15.18: calcidiol 1-monooxygenase +EC 1.14.15.19: C-19 steroid 1α-hydroxylase +EC 1.14.15.20: heme oxygenase (biliverdin-producing, ferredoxin) +EC 1.14.15.21: zeaxanthin epoxidase +EC 1.14.15.22: vitamin D 1,25-hydroxylase +EC 1.14.15.23: chloroacetanilide N-alkylformylase +EC 1.14.15.24: β-carotene 3-hydroxylase +EC 1.14.15.25: p-cymene methyl-monooxygenase +EC 1.14.15.26: toluene methyl-monooxygenase +EC 1.14.15.27: β-dihydromenaquinone-9 ω-hydroxylase +EC 1.14.15.28: cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] +EC 1.14.15.29: cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] +EC 1.14.15.30: 3-ketosteroid 9α-monooxygenase +EC 1.14.15.31: 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase +EC 1.14.15.32: pentalenene oxygenase +EC 1.14.15.33: pikromycin synthase +EC 1.14.15.34: 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase +EC 1.14.15.35: 6-deoxyerythronolide B hydroxylase +EC 1.14.15.36: sterol 14α-demethylase (ferredoxin) +EC 1.14.15.37: luteothin monooxygenase +EC 1.14.15.38: N,N-dimethyl phenylurea N-demethylase +EC 1.14.15.39: epi-isozizaene 5-monooxygenase + +=== EC 1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor === +EC 1.14.16.1: phenylalanine 4-monooxygenase +EC 1.14.16.2: tyrosine 3-monooxygenase +EC 1.14.16.3: withdrawn owing to insufficient evidence (anthranilate 3-monooxygenase) +EC 1.14.16.4: tryptophan 5-monooxygenase +EC 1.14.16.5: alkylglycerol monooxygenase +EC 1.14.16.6: mandelate 4-monooxygenase +EC 1.14.16.7: phenylalanine 3-monooxygenase + +=== EC 1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor === +EC 1.14.17.1: dopamine β-monooxygenase +EC |1.14.17.2: deleted, now included with EC 1.14.18.1 monophenol monooxygenase +EC 1.14.17.3: peptidylglycine monooxygenase +EC 1.14.17.4: aminocyclopropanecarboxylate oxidase + +=== EC 1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor === +EC 1.14.18.1: tyrosinase +EC 1.14.18.2: CMP-N-acetylneuraminate monooxygenase +EC 1.14.18.3: methane monooxygenase (particulate) +EC 1.14.18.4: phosphatidylcholine 12-monooxygenase +EC 1.14.18.5: sphingolipid C4-monooxygenase +EC 1.14.18.6: 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase +EC 1.14.18.7: dihydroceramide fatty acyl 2-hydroxylase +EC 1.14.18.8: Now included with EC 1.14.14.139, 5β-cholestane-3α,7α-diol 12α-hydroxylase +EC 1.14.18.9: 4α-methylsterol monooxygenase +EC 1.14.18.10: plant 4,4-dimethylsterol C-4α-methyl-monooxygenase +EC 1.14.18.11: plant 4α-monomethylsterol monooxygenase +EC 1.14.18.12: 2-hydroxy fatty acid dioxygenase + +=== EC 1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water === +EC 1.14.19.1: stearoyl-CoA 9-desaturase +EC 1.14.19.2: stearoyl-[acyl-carrier-protein] 9-desaturase +EC 1.14.19.3: linoleoyl-CoA desaturase +EC 1.14.19.4: acyl-lipid (11-3)-desaturase +EC 1.14.19.5: acyl-CoA 11-(Z)-desaturase +EC 1.14.19.6: acyl-CoA (9+3)-desaturase +EC 1.14.19.7: Now EC 1.11.1.23, (S)-2-hydroxypropylphosphonic acid epoxidase +EC 1.14.19.8: pentalenolactone synthase +EC 1.14.19.9: tryptophan 7-halogenase +EC 1.14.19.10: icosanoyl-CoA 5-desaturase +EC 1.14.19.11: acyl-[acyl-carrier-protein] 4-desaturase +EC 1.14.19.12: acyl-lipid ω-(9-4) desaturase +EC 1.14.19.13: acyl-CoA 15-desaturase +EC 1.14.19.14: linoleoyl-lipid Δ9 conjugase +EC 1.14.19.15: (11Z)-hexadec-11-enoyl-CoA conjugase +EC 1.14.19.16: linoleoyl-lipid Δ12 conjugase (11E,13Z-forming) +EC 1.14.19.17: sphingolipid 4-desaturase +EC 1.14.19.18: sphingolipid 8-(E)-desaturase +EC 1.14.19.19: sphingolipid 10-desaturase +EC 1.14.19.20: Δ7-sterol 5(6)-desaturase +EC 1.14.19.21: cholesterol 7-desaturase +EC 1.14.19.22: acyl-lipid ω-6 desaturase (cytochrome b5) +EC 1.14.19.23: acyl-lipid (n+3)-(Z)-desaturase (ferredoxin) +EC 1.14.19.24: acyl-CoA 11-(E)-desaturase +EC 1.14.19.25: acyl-lipid ω-3 desaturase (cytochrome b5) +EC 1.14.19.26: acyl-[acyl-carrier-protein] 6-desaturase +EC 1.14.19.27: sn-2 palmitoyl-lipid 9-desaturase +EC 1.14.19.28: sn-1 stearoyl-lipid 9-desaturase +EC 1.14.19.29: sphingolipid 8-(E/Z)-desaturase +EC 1.14.19.30: acyl-lipid (8-3)-desaturase +EC 1.14.19.31: acyl-lipid (7-3)-desaturase +EC 1.14.19.32: palmitoyl-CoA 14-(E/Z)-desaturase +EC 1.14.19.33: Δ12 acyl-lipid conjugase (11E,13E-forming) +EC 1.14.19.34: acyl-lipid (9+3)-(E)-desaturase +EC 1.14.19.35: sn-2 acyl-lipid ω-3 desaturase (ferredoxin) +EC 1.14.19.36: sn-1 acyl-lipid ω-3 desaturase (ferredoxin) +EC 1.14.19.37: acyl-CoA 5-desaturase +EC 1.14.19.38: acyl-lipid Δ6-acetylenase +EC 1.14.19.39: acyl-lipid Δ12-acetylenase +EC 1.14.19.40: hex-5-enoyl-[acyl-carrier protein] acetylenase +EC 1.14.19.41: sterol 22-desaturase +EC 1.14.19.42: palmitoyl-[glycerolipid] 7-desaturase +EC 1.14.19.43: palmitoyl-[glycerolipid] 3-(E)-desaturase +EC 1.14.19.44: acyl-CoA (8-3)-desaturase +EC 1.14.19.45: sn-1 oleoyl-lipid 12-desaturase +EC 1.14.19.46: sn-1 linoleoyl-lipid 6-desaturase +EC 1.14.19.47: acyl-lipid (9-3)-desaturase +EC 1.14.19.48: tert-amyl alcohol desaturase +EC 1.14.19.49: tetracycline 7-halogenase +EC 1.14.19.50: noroxomaritidine synthase +EC 1.14.19.51: (S)-corytuberine synthase +EC 1.14.19.52: camalexin synthase +EC 1.14.19.53: all-trans-retinol 3,4-desaturase +EC 1.14.19.54: 1,2-dehydroreticuline synthase +EC 1.14.19.55: 4-hydroxybenzoate brominase (decarboxylating) +EC 1.14.19.56: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase +EC 1.14.19.57: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase +EC 1.14.19.58: tryptophan 5-halogenase +EC 1.14.19.59: tryptophan 6-halogenase +EC 1.14.19.60: 7-chloro-L-tryptophan 6-halogenase +EC 1.14.19.61: dihydrorhizobitoxine desaturase +EC 1.14.19.62: secologanin synthase +EC 1.14.19.63: pseudobaptigenin synthase +EC 1.14.19.64: (S)-stylopine synthase +EC 1.14.19.65: (S)-cheilanthifoline synthase +EC 1.14.19.66: berbamunine synthase +EC 1.14.19.67: salutaridine synthase +EC 1.14.19.68: (S)-canadine synthase +EC 1.14.19.69: biflaviolin synthase +EC 1.14.19.70: mycocyclosin synthase +EC 1.14.19.71: fumitremorgin C synthase +EC 1.14.19.72: (–)-pluviatolide synthase +EC 1.14.19.73: (S)-nandinine synthase +EC 1.14.19.74: (+)-piperitol/(+)-sesamin synthase +EC 1.14.19.75: very-long-chain acyl-lipid ω-9 desaturase +EC 1.14.19.76: flavone synthase II +EC 1.14.19.77: plasmanylethanolamine desaturase +EC 1.14.19.78: decanoyl-[acyl-carrier protein] acetylenase + +=== EC 1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated === +EC 1.14.20.1: deacetoxycephalosporin-C synthase +EC 1.14.20.2: Now EC 1.14.11.59, 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase +EC 1.14.20.3: (5R)-carbapenem-3-carboxylate synthase +EC 1.14.20.4: anthocyanidin synthase +EC 1.14.20.5: flavone synthase I +EC 1.14.20.6: flavonol synthase +EC 1.14.20.7: 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming) +EC 1.14.20.8: (–)-deoxypodophyllotoxin synthase +EC 1.14.20.9: L-tyrosine isonitrile desaturase +EC 1.14.20.10: L-tyrosine isonitrile desaturase/decarboxylase +EC 1.14.20.11: 3-[(Z)-2-isocyanoethenyl]-1H-indole synthase +EC 1.14.20.12: 3-[(E)-2-isocyanoethenyl]-1H-indole synthase +EC 1.14.20.13: 6β-hydroxyhyoscyamine epoxidase +EC 1.14.20.14: hapalindole-type alkaloid chlorinase +EC 1.14.20.15: L-threonyl-[L-threonyl-carrier protein] 4-chlorinase + +=== EC 1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated === +EC 1.14.21.1: Now EC 1.14.19.64, (S)-stylopine synthase +EC 1.14.21.2: Now EC 1.14.19.65, (S)-cheilanthifoline synthase +EC 1.14.21.3: Now EC 1.14.19.66, berbamunine synthase +EC 1.14.21.4: Now EC 1.14.19.67, salutaridine synthase +EC 1.14.21.5: Now EC 1.14.19.68, (S)-canadine synthase +EC 1.14.21.6: Now EC 1.14.19.20, Δ7-sterol 5(6)-desaturase +EC 1.14.21.7: Now EC 1.14.19.69, biflaviolin synthase +EC 1.14.21.8: Now EC 1.14.19.63, pseudobaptigenin synthase +EC 1.14.21.9: Now EC 1.14.19.70, mycocyclosin synthase * +EC 1.14.21.10: Now EC 1.14.19.71, fumitremorgin C synthase * +EC 1.14.21.11: Now EC 1.14.19.72, (–)-pluviatolide synthase * +EC 1.14.21.12: Now EC 1.14.19.73, (S)-nandinine synthase * \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-16.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-16.md new file mode 100644 index 000000000..474c43513 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-16.md @@ -0,0 +1,185 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 17/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.14.99 Miscellaneous === +EC 1.14.99.1: prostaglandin-endoperoxide synthase +EC 1.14.99.2: kynurenine 7,8-hydroxylase +EC 1.14.99.3: Now EC 1.14.14.18, heme oxygenase (biliverdin-producing) +EC 1.14.99.4: progesterone monooxygenase +EC 1.14.99.5: Now EC 1.14.19.1, stearoyl-CoA 9-desaturase +EC 1.14.99.6: Now EC 1.14.19.2, acyl-[acyl-carrier-protein] desaturase +EC 1.14.99.7: Transferred to EC 1.14.13.132, squalene monooxygenase +EC 1.14.99.8: Now included with EC 1.14.14.1 unspecific monooxygenase +EC 1.14.99.9: Now classified as EC 1.14.14.19, steroid 17α-monooxygenase +EC 1.14.99.10: Now EC 1.14.14.16, steroid 21-monooxygenase +EC 1.14.99.11: estradiol 6β-monooxygenase +EC 1.14.99.12: 4-androstene-3,17-dione monooxygenase +EC 1.14.99.13: Now EC 1.14.13.23, 3-hydroxybenzoate 4-monooxygenase +EC 1.14.99.14: Now EC 1.14.14.197, progesterone 11α-monooxygenase +EC 1.14.99.15: 4-methoxybenzoate monooxygenase (O-demethylating) +EC 1.14.99.16: Now EC 1.14.13.72, methylsterol monooxygenase +EC 1.14.99.17: Now EC 1.14.16.5, glyceryl-ether monooxygenase +EC 1.14.99.18: deleted +EC 1.14.99.19: Now classified as EC 1.14.19.77, plasmanylethanolamine desaturase +EC 1.14.99.20: phylloquinone monooxygenase (2,3-epoxidizing) +EC 1.14.99.21: Latia-luciferin monooxygenase (demethylating) +EC 1.14.99.22: ecdysone 20-monooxygenase +EC 1.14.99.23: 3-hydroxybenzoate 2-monooxygenase +EC 1.14.99.24: steroid 9α-monooxygenase +EC 1.14.99.25: Now EC 1.14.19.3, linoleoyl-CoA desaturase +EC 1.14.99.26: 2-hydroxypyridine 5-monooxygenase +EC 1.14.99.27: Now classified as EC 1.17.3.4, juglone 3-monooxygenase +EC 1.14.99.28: Now EC 1.14.14.84, linalool 8-monooxygenase +EC 1.14.99.29: deoxyhypusine monooxygenase +EC 1.14.99.30: Now EC 1.3.5.6, 9,9′-dicis-ζ-carotene desaturase. +EC 1.14.99.31: Now classified as EC 1.14.19.24, myristoyl-CoA 11-(E) desaturase +EC 1.14.99.32: Now classified as EC 1.14.19.5, acyl-CoA 11-(Z)-desaturase +EC 1.14.99.33: Now EC 1.14.19.39, acyl-lipid Δ12-acetylenase +EC 1.14.99.34: monoprenyl isoflavone epoxidase +EC 1.14.99.35: thiophene-2-carbonyl-CoA monooxygenase +EC 1.14.99.36: Now classified as EC 1.13.11.63, β-carotene 15,15′-dioxygenase +EC 1.14.99.37: Now EC 1.14.14.176, taxadiene 5α-hydroxylase +EC 1.14.99.38: cholesterol 25-hydroxylase +EC 1.14.99.39: ammonia monooxygenase +EC 1.14.99.40: Now EC 1.13.11.79, 5,6-dimethylbenzimidazole synthase +EC 1.14.99.41: Now EC 1.13.11.75, all-trans-8′-apo-β-carotenal 15,15′-oxygenase +EC 1.14.99.42: Now EC 1.13.11.84, crocetin dialdehyde synthase +EC 1.14.99.43: Now EC 1.14.14.134, β-amyrin 24-hydroxylase +EC 1.14.99.44: diapolycopene oxygenase +EC 1.14.99.45: Now EC 1.14.14.158, carotene ε-monooxygenase +EC 1.14.99.46: pyrimidine oxygenase +EC 1.14.99.47: (+)-larreatricin hydroxylase +EC 1.14.99.48: heme oxygenase (staphylobilin-producing) +EC 1.14.99.49: Now EC 1.14.15.31, 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase +EC 1.14.99.50: γ-glutamyl hercynylcysteine S-oxide synthase +EC 1.14.99.51: hercynylcysteine S-oxide synthase +EC 1.14.99.52: L-cysteinyl-L-histidinylsulfoxide synthase +EC 1.14.99.53: lytic chitin monooxygenase +EC 1.14.99.54: lytic cellulose monooxygenase (C1-hydroxylating) +EC 1.14.99.55: lytic starch monooxygenase +EC 1.14.99.56: lytic cellulose monooxygenase (C4-dehydrogenating) +EC 1.14.99.57: heme oxygenase (mycobilin-producing) +EC 1.14.99.58: heme oxygenase (biliverdin-IX-β and δ-forming) +EC 1.14.99.59: tryptamine 4-monooxygenase +EC 1.14.99.60: 3-demethoxyubiquinol 3-hydroxylase +EC 1.14.99.61: cyclooctat-9-en-7-ol 5-monooxygenase +EC 1.14.99.62: cyclooctatin synthase +EC 1.14.99.63: β-carotene 4-ketolase +EC 1.14.99.64: zeaxanthin 4-ketolase +EC 1.14.99.65: 4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase +EC 1.14.99.66: [histone H3]-N6,N6-dimethyl-L-lysine4 FAD-dependent demethylase +EC 1.14.99.67: α-N-dichloroacetyl-p-aminophenylserinol N-oxygenase +EC 1.14.99.68: 4-aminobenzoate N-oxygenase +EC 1.14.99.69: tRNA 2-(methylsulfanyl)-N6-isopentenyladenosine37 hydroxylase + +== EC 1.15 Acting on superoxide as acceptor == + +=== EC 1.15.1 === +EC 1.15.1.1: superoxide dismutase +EC 1.15.1.2: superoxide reductase + +== EC 1.16 Oxidizing metal ions == + +=== EC 1.16.1 With NAD+ or NADP+ as acceptor === +EC 1.16.1.1: mercury(II) reductase +EC 1.16.1.2: diferric-transferrin reductase +EC 1.16.1.3: deleted since no specific enzyme catalysing this activity has been identified +EC 1.16.1.4: cob(II)alamin reductase +EC 1.16.1.5: deleted since the enzyme the entry was based on was later shown to be EC 1.2.1.51, pyruvate dehydrogenase (NADP+). +EC 1.16.1.6: cyanocobalamin reductase (cyanide-eliminating) +EC 1.16.1.7: ferric-chelate reductase +EC 1.16.1.8: [methionine synthase] reductase +EC 1.16.1.9: ferric-chelate reductase (NADPH) +EC 1.16.1.10: ferric-chelate reductase [NAD(P)H] + +=== EC 1.16.3 With oxygen as acceptor === +EC 1.16.3.1: ferroxidase +EC 1.16.3.2: bacterial non-heme ferritin +EC 1.16.3.3: manganese oxidase + +=== EC 1.16.5 With a quinone or similar compound as acceptor === +EC 1.16.5.1: Now EC 7.2.1.3, ascorbate ferrireductase (transmembrane) + +=== EC 1.16.8 With a flavin as acceptor === +EC 1.16.8.1: activity now known to be catalyzed by EC 2.5.1.17, corrinoid adenosyltransferase + +=== EC 1.16.9 With a copper protein as acceptor === +EC 1.16.9.1: iron:rusticyanin reductase + +=== EC 1.16.98 With other, known, physiological acceptors === +EC 1.16.98.1: Now EC 1.16.9.1 iron:rusticyanin reductase + +=== EC 1.16.99 With unknown physiological acceptors === +EC 1.16.99.1: [Co(II) methylated amine-specific corrinoid protein] reductase + +== EC 1.17 Acting on CH or CH2 groups == + +=== EC 1.17.1 With NAD or NADP as acceptor === +EC 1.17.1.1: CDP-4-dehydro-6-deoxyglucose reductase +EC 1.17.1.2: now classified as EC 1.17.7.4, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase +EC 1.17.1.3: leucoanthocyanidin reductase +EC 1.17.1.4: xanthine dehydrogenase +EC 1.17.1.5: nicotinate dehydrogenase +EC 1.17.1.6: Now EC 1.17.99.5, bile-acid 7α-dehydroxylase. It is now known that FAD is the acceptor and not NAD+ as was thought previously +EC 1.17.1.7: Now EC 1.2.1.91, 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase +EC 1.17.1.8: 4-hydroxy-tetrahydrodipicolinate reductase +EC 1.17.1.9: formate dehydrogenase +EC 1.17.1.10: formate dehydrogenase (NADP+) +EC 1.17.1.11: formate dehydrogenase (NAD+, ferredoxin) + +=== EC 1.17.2 With a cytochrome as acceptor === +EC 1.17.2.1: nicotinate dehydrogenase (cytochrome) +EC 1.17.2.2: lupanine 17-hydroxylase (cytochrome c) +EC 1.17.2.3: formate dehydrogenase (cytochrome-c-553) + +=== EC 1.17.3 With oxygen as acceptor === +EC 1.17.3.1: pteridine oxidase +EC 1.17.3.2: xanthine oxidase +EC 1.17.3.3: 6-hydroxynicotinate dehydrogenase +EC 1.17.3.4: juglone 3-hydroxylase + +=== EC 1.17.4 With a disulfide as acceptor === +EC 1.17.4.1: ribonucleoside-diphosphate reductase +EC 1.17.4.2: ribonucleoside-triphosphate reductase (thioredoxin) +EC 1.17.4.3: transferred to EC 1.17.7.1, (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase. +EC 1.17.4.4: vitamin-K-epoxide reductase (warfarin-sensitive) +EC 1.17.4.5: vitamin-K-epoxide reductase (warfarin-insensitive) + +=== EC 1.17.5 With a quinone or similar compound as acceptor === +EC 1.17.5.1: phenylacetyl-CoA dehydrogenase +EC 1.17.5.2: caffeine dehydrogenase +EC 1.17.5.3: formate dehydrogenase-N + +=== EC 1.17.7 With an iron–sulfur protein as acceptor === +EC 1.17.7.1: (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (ferredoxin) +EC 1.17.7.2: 7-hydroxymethyl chlorophyll a reductase +EC 1.17.7.3: (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase (flavodoxin) +EC 1.17.7.4: 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase + +=== EC 1.17.98 With other, known, physiological acceptors === +EC 1.17.98.1: bile-acid 7α-dehydroxylase. Now known to be catalyzed by multiple enzymes. +EC 1.17.98.2: bacteriochlorophyllide c C-71-hydroxylase +EC 1.17.98.3: formate dehydrogenase (coenzyme F420) +EC 1.17.98.4: formate dehydrogenase (hydrogenase) + +=== EC 1.17.99 With unknown physiological acceptors === +EC 1.17.99.1: Now EC 1.17.9.1, 4-methylphenol dehydrogenase (hydroxylating) +EC 1.17.99.2: ethylbenzene hydroxylase +EC 1.17.99.3: 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA 24-hydroxylase +EC 1.17.99.4: uracil/thymine dehydrogenase +EC 1.17.99.5: Now classified as EC 1.17.98.1, bile-acid 7α-dehydroxylase +EC 1.17.99.6: epoxyqueuosine reductase +EC 1.17.99.7: Now classified as EC 1.17.98.4, formate dehydrogenase (hydrogenase) +EC 1.17.99.8: limonene dehydrogenase +EC 1.17.99.9: heme a synthase +EC 1.17.99.10: steroid C-25 hydroxylase +EC 1.17.99.11: 3-oxo-Δ1-steroid hydratase/dehydrogenase + +== EC 1.18 Acting on iron–sulfur proteins as donors == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-17.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-17.md new file mode 100644 index 000000000..9607be768 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-17.md @@ -0,0 +1,159 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 18/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.18.1 With NAD+ or NADP+ as acceptor === +EC 1.18.1.1: rubredoxin—NAD+ reductase +EC 1.18.1.2: ferredoxin—NADP+ reductase +EC 1.18.1.3: ferredoxin—NAD+ reductase +EC 1.18.1.4: rubredoxin—NAD(P)+ reductase +EC 1.18.1.5: Putidaredoxin—NAD+ reductase +EC 1.18.1.6: adrenodoxin-NADP+ reductase +EC 1.18.1.7: ferredoxin—NAD(P)+ reductase (naphthalene dioxygenase ferredoxin-specific) +EC 1.18.1.8: Now EC 7.2.1.2, ferredoxin—NAD+ oxidoreductase (Na+-transporting) + +=== EC 1.18.2 With dinitrogen as acceptor (deleted sub-subclass) === +EC 1.18.2.1: now EC 1.18.6.1, nitrogenase + +=== EC 1.18.3 With H+ as acceptor (deleted sub-subclass) === +EC 1.18.3.1: Now EC 1.12.7.2, ferredoxin hydrogenase + +=== EC 1.18.6 With dinitrogen as acceptor === +EC 1.18.6.1: nitrogenase +EC 1.18.6.2: vanadium-dependent nitrogenase + +=== EC 1.18.96 With other, known, acceptors (deleted sub-subclass) === +EC 1.18.96.1: Now EC 1.15.1.2, superoxide reductase + +=== EC 1.18.99 With H+ as acceptor (deleted sub-subclass) === +EC 1.18.99.1: Now EC 1.12.7.2, ferredoxin hydrogenase + +== EC 1.19 Acting on reduced flavodoxin as donor == + +=== EC 1.19.1 With NAD+ or NADP+ as acceptor === +EC 1.19.1.1: flavodoxin—NADP+ reductase + +=== EC 1.19.6 With dinitrogen as acceptor === +EC 1.19.6.1: nitrogenase (flavodoxin) + +== EC 1.20 Acting on phosphorus or arsenic in donors == + +=== EC 1.20.1 Acting on phosphorus or arsenic in donors, with NAD+ as acceptor === +EC 1.20.1.1: phosphonate dehydrogenase + +=== EC 1.20.2 Acting on phosphorus or arsenic in donors, with NAD(P)+ as acceptor === +EC 1.20.2.1: arsenate reductase (cytochrome c) + +=== EC 1.20.4 Acting on phosphorus or arsenic in donors, with disulfide as acceptor === +EC 1.20.4.1: arsenate reductase (glutaredoxin) +EC 1.20.4.2: methylarsonate reductase +EC 1.20.4.3: mycoredoxin +EC 1.20.4.4: arsenate reductase (thioredoxin) + +=== EC 1.20.9 With a copper protein as acceptor === +EC 1.20.9.1: arsenate reductase (azurin) + +=== EC 1.20.98 With other, known acceptors === +EC 1.20.98.1: Now EC 1.20.9.1, arsenate reductase (azurin) + +=== EC 1.20.99 With unknown physiological acceptors === +EC 1.20.99.1: arsenate reductase (donor) + +== EC 1.21 Catalysing the reaction X-H + Y-H = X-Y == + +=== EC 1.21.3 With oxygen as acceptor === +EC 1.21.3.1: isopenicillin-N synthase +EC 1.21.3.2: columbamine oxidase +EC 1.21.3.3: reticuline oxidase +EC 1.21.3.4: sulochrin oxidase ((+)-bisdechlorogeodin-forming) +EC 1.21.3.5: sulochrin oxidase ((-)-bisdechlorogeodin-forming) +EC 1.21.3.6: aureusidin synthase +EC 1.21.3.7: tetrahydrocannabinolic acid synthase +EC 1.21.3.8: cannabidiolic acid synthase +EC 1.21.3.9: now classified as EC 1.21.98.2, dichlorochromopyrrolate synthase + +=== EC 1.21.4 With a disulfide as acceptor === +EC 1.21.4.1: D-proline reductase (dithiol) +EC 1.21.4.2: glycine reductase +EC 1.21.4.3: sarcosine reductase +EC 1.21.4.4: betaine reductase +EC 1.21.4.5: tetrachlorohydroquinone reductive dehalogenase + +=== EC 1.21.98 With other, known, physiological acceptors === +EC 1.21.98.1: cyclic dehypoxanthinyl futalosine synthase +EC 1.21.98.2: dichlorochromopyrrolate synthase +EC 1.21.98.3: anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase +EC 1.21.98.4: PqqA peptide cyclase + +=== EC 1.21.99 With unknown physiological acceptors === +EC 1.21.99.1 EC 1.21.99.1: β-cyclopiazonate dehydrogenase +EC 1.21.99.2: Now classified as EC 1.21.98.1, cyclic dehypoxanthinyl futalosine synthase. +EC 1.21.99.3: thyroxine 5-deiodinase +EC 1.21.99.4: thyroxine 5′-deiodinase +EC 1.21.99.5: tetrachloroethene reductive dehalogenase + +== EC 1.22 Acting on halogen in donors == + +=== EC 1.22.1 With NAD+ or NADP+ as acceptor === +EC 1.22.1.1: Now EC 1.21.1.1, iodotyrosine deiodinase + +== EC 1.23 Reducing C-O-C group as acceptor == + +=== EC 1.23.1 With NADH or NADPH as donor === +EC 1.23.1.1: (+)-pinoresinol reductase +EC 1.23.1.2: (+)-lariciresinol reductase +EC 1.23.1.3: (–)-pinoresinol reductase +EC 1.23.1.4: (–)-lariciresinol reductase + +== EC 1.97 Other oxidoreductases == + +=== EC 1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses === +EC 1.97.1.1: chlorate reductase +EC 1.97.1.2: Now EC 5.4.4.9, pyrogallol hydroxytransferase +EC 1.97.1.3: Now EC 1.12.98.4, sulfhydrogenase, since hydrogen is known to be the electron donor +EC 1.97.1.4: [formate-C-acetyltransferase]-activating enzyme +EC 1.97.1.5: Now EC 1.20.4.1, arsenate reductase (glutaredoxin +EC 1.97.1.6: Now EC 1.20.99.1, arsenate reductase (donor) +EC 1.97.1.7: Now EC 1.20.4.2, methylarsonate reductase +EC 1.97.1.8: Now EC 1.21.99.5, tetrachloroethene reductive dehalogenase +EC 1.97.1.9: selenate reductase +EC 1.97.1.10: Now EC 1.21.99.4 thyroxine 5′-deiodinase +EC 1.97.1.11: Now EC 1.21.99.3 thyroxine 5-deiodinase. +EC 1.97.1.12: photosystem I + +=== EC 1.98 Enzymes using H2 as reductant (deleted subclass) === +EC 1.98.1.1: Now EC 1.12.7.2, ferredoxin hydrogenase + +== EC 1.99 Other enzymes using O2 as oxidant == + +=== EC 1.99.1 Hydroxylases (now covered by EC 1.14) === +EC 1.99.1.1: deleted, Now EC 1.12.7.2, ferredoxin hydrogenase +EC 1.99.1.2: deleted, Now EC 1.14.16.1, phenylalanine 4-monooxygenase +EC 1.99.1.3: deleted, nicotinate 6-hydroxylase +EC 1.99.1.4: deleted, tryptophan 5-hydroxylase +EC 1.99.1.5: deleted, Now EC 1.14.13.9, kynurenine 3-monooxygenase +EC 1.99.1.6: deleted, steroid 11α-hydroxylase +EC 1.99.1.7: deleted, Now EC 1.14.15.4, steroid 11β-monooxygenase +EC 1.99.1.8: deleted, steroid 6β-hydroxylase +EC 1.99.1.9: deleted, Now EC 1.14.99.9, steroid 17α-monooxygenase +EC 1.99.1.10: deleted, steroid 19-hydroxylase +EC 1.99.1.11: deleted, Now EC 1.14.99.10, steroid 21-monooxygenase +EC 1.99.1.12: deleted, alkoxyaryl hydroxylase +EC 1.99.1.13: deleted, covered by EC 1.14.99.7 (squalene monooxygenase) and by EC 5.4.99.7 (lanosterol synthase) +EC 1.99.1.14: deleted, Now EC 1.13.11.27, 4-hydroxyphenylpyruvate dioxygenase + +=== EC 1.99.2 Oxygenases (now covered by EC 1.13) === +EC 1.99.2.1: deleted, now EC 1.13.11.12, lipoxygenase +EC 1.99.2.2: deleted, now EC 1.13.11.1, catechol 1,2-dioxygenase +EC 1.99.2.3: deleted, now EC 1.13.11.3, protocatechuate 3,4-dioxygenase +EC 1.99.2.4: deleted, now EC 1.13.11.4, gentisate 1,2-dioxygenase +EC 1.99.2.5: deleted, now EC 1.13.11.5, homogentisate 1,2-dioxygenase +EC 1.99.2.6: deleted, now EC 1.13.99.1, inositol oxygenase + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-2.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-2.md new file mode 100644 index 000000000..8160ddac0 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-2.md @@ -0,0 +1,144 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 3/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +This enzyme was already in the Enzyme List as EC 1.1.1.206, tropine dehydrogenase so EC 1.1.1.293 has been withdrawn at the public-review stage +EC 1.1.1.294: chlorophyll(ide) b reductase +EC 1.1.1.295: momilactone-A synthase +EC 1.1.1.296: dihydrocarveol dehydrogenase +EC 1.1.1.297: limonene-1,2-diol dehydrogenase +EC 1.1.1.298: 3-hydroxypropionate dehydrogenase (NADP+) +EC 1.1.1.299: malate dehydrogenase [NAD(P)+)] +EC 1.1.1.300: NADP-retinol dehydrogenase +EC 1.1.1.301: D-arabitol-phosphate dehydrogenase +EC 1.1.1.302: 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5′-phosphate reductase +EC 1.1.1.303: Diacetyl reductase ((R)-acetoin forming) +EC 1.1.1.304: Diacetyl reductase ((S)-acetoin forming) +EC 1.1.1.305: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) +EC 1.1.1.306: S-(hydroxymethyl)mycothiol dehydrogenase +EC 1.1.1.307: D-xylose reductase +EC 1.1.1.308: sulfopropanediol 3-dehydrogenase +EC 1.1.1.309: phosphonoacetaldehyde reductase (NADH) +EC 1.1.1.310: (S)-sulfolactate dehydrogenase +EC 1.1.1.311: (S)-1-phenylethanol dehydrogenase +EC 1.1.1.312: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase +EC 1.1.1.313: sulfoacetaldehyde reductase +EC 1.1.1.314: Now known to be catalyzed by EC 1.14.14.95, germacrene A hydroxylase +EC 1.1.1.315: 11-cis-retinol dehydrogenase +EC 1.1.1.316: L-galactose 1-dehydrogenase +EC 1.1.1.317: perakine reductase +EC 1.1.1.318: eugenol synthase +EC 1.1.1.319: isoeugenol synthase +EC 1.1.1.320: benzil reductase [(S)-benzoin forming] +EC 1.1.1.321: benzil reductase [(R)-benzoin forming] +EC 1.1.1.322: (–)-endo-fenchol dehydrogenase +EC 1.1.1.323: (+)-thujan-3-ol dehydrogenase +EC 1.1.1.324: 8-hydroxygeraniol dehydrogenase +EC 1.1.1.325: sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming) +EC 1.1.1.326: zerumbone synthase +EC 1.1.1.327: 5-exo-hydroxycamphor dehydrogenase +EC 1.1.1.328: nicotine blue oxidoreductase +EC 1.1.1.329: 2-deoxy-scyllo-inosamine dehydrogenase +EC 1.1.1.330: very-long-chain 3-oxoacyl-CoA reductase +EC 1.1.1.331: secoisolariciresinol dehydrogenase +EC 1.1.1.332: chanoclavine-I dehydrogenase +EC 1.1.1.333: decaprenylphospho-β-D-erythro-pentofuranosid-2-ulose 2-reductase +EC 1.1.1.334: methylecgonone reductase +EC 1.1.1.335: UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase +EC 1.1.1.336: UDP-N-acetyl-D-mannosamine dehydrogenase +EC 1.1.1.337: L-2-hydroxycarboxylate dehydrogenase (NAD+) +EC 1.1.1.338: (2R)-3-sulfolactate dehydrogenase (NADP+) +EC 1.1.1.339: dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD+) +EC 1.1.1.340: 1-deoxy-11β-hydroxypentalenate dehydrogenase +EC 1.1.1.341: CDP-abequose synthase +EC 1.1.1.342: CDP-paratose synthase +EC 1.1.1.343: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) +EC 1.1.1.344: dTDP-6-deoxy-L-talose 4-dehydrogenase [NAD(P)+] +EC 1.1.1.345: D-2-hydroxyacid dehydrogenase (NAD+) +EC 1.1.1.346: 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming) +EC 1.1.1.347: geraniol dehydrogenase (NAD+) +EC 1.1.1.348: (3R)-2′-hydroxyisoflavanone reductase +EC 1.1.1.349: norsolorinic acid ketoreductase +EC 1.1.1.350: ureidoglycolate dehydrogenase (NAD+) +EC 1.1.1.351: phosphogluconate dehydrogenase [NAD(P)+-dependent, decarboxylating] +EC 1.1.1.352: 5′-hydroxyaverantin dehydrogenase +EC 1.1.1.353: versiconal hemiacetal acetate reductase +EC 1.1.1.354: farnesol dehydrogenase (NAD+) +EC 1.1.1.355: 2′-dehydrokanamycin reductase +EC 1.1.1.356: GDP-L-colitose synthase +EC 1.1.1.357: 3α-hydroxysteroid 3-dehydrogenase +EC 1.1.1.358: 2-dehydropantolactone reductase +EC 1.1.1.359: aldose 1-dehydrogenase [NAD(P)+] +EC 1.1.1.360: glucose/galactose 1-dehydrogenase +EC 1.1.1.361: glucose-6-phosphate 3-dehydrogenase +EC 1.1.1.362: aklaviketone reductase +EC 1.1.1.363: glucose-6-phosphate dehydrogenase [NAD(P)+] +EC 1.1.1.364: dTDP-4-dehydro-6-deoxy-α-D-gulose 4-ketoreductase +EC 1.1.1.365: D-galacturonate reductase +EC 1.1.1.366: L-idonate 5-dehydrogenase (NAD+) +EC 1.1.1.367: UDP-2-acetamido-2,6-β-L-arabino-hexul-4-ose reductase +EC 1.1.1.368: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase +EC 1.1.1.369: D-chiro-inositol 1-dehydrogenase +EC 1.1.1.370: scyllo-inositol 2-dehydrogenase (NAD+) +EC 1.1.1.371: scyllo-inositol 2-dehydrogenase (NADP+) +EC 1.1.1.372: D/L-glyceraldehyde reductase +EC 1.1.1.373: sulfolactaldehyde 3-reductase +EC 1.1.1.374: UDP-N-acetylglucosamine 3-dehydrogenase +EC 1.1.1.375: L-2-hydroxycarboxylate dehydrogenase [NAD(P)+] +EC 1.1.1.376: L-arabinose 1-dehydrogenase [NAD(P)+] +EC 1.1.1.377: L-rhamnose 1-dehydrogenase (NADP+) +EC 1.1.1.378: L-rhamnose 1-dehydrogenase [NAD(P)+] +EC 1.1.1.379: (R)-mandelate dehydrogenase +EC 1.1.1.380: L-gulonate 5-dehydrogenase +EC 1.1.1.381: 3-hydroxy acid dehydrogenase +EC 1.1.1.382: ketol-acid reductoisomerase (NAD+) +EC 1.1.1.383: ketol-acid reductoisomerase [NAD(P)+] +EC 1.1.1.384: dTDP-3,4-didehydro-2,6-dideoxy-α-D-glucose 3-reductase +EC 1.1.1.385: dihydroanticapsin dehydrogenase +EC 1.1.1.386: ipsdienol dehydrogenase +EC 1.1.1.387: L-serine 3-dehydrogenase (NAD+) +EC 1.1.1.388: glucose-6-phosphate dehydrogenase (NAD+) +EC 1.1.1.389: 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase +EC 1.1.1.390: sulfoquinovose 1-dehydrogenase +EC 1.1.1.391: 3β-hydroxycholanate 3-dehydrogenase (NAD+) +EC 1.1.1.392: 3α-hydroxycholanate dehydrogenase (NADP+) +EC 1.1.1.393: 3β-hydroxycholanate 3-dehydrogenase (NADP+) +EC 1.1.1.394: aurachin B dehydrogenase +EC 1.1.1.395: 3α-hydroxy bile acid-CoA-ester 3-dehydrogenase +EC 1.1.1.396: bacteriochlorophyllide a dehydrogenase +EC 1.1.1.397: β-methylindole-3-pyruvate reductase +EC 1.1.1.398: 2-glutathionyl-2-methylbut-3-en-1-ol dehydrogenase +EC 1.1.1.399: 2-oxoglutarate reductase +EC 1.1.1.400: 2-methyl-1,2-propanediol dehydrogenase +EC 1.1.1.401: 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+) +EC 1.1.1.402: D-erythritol 1-phosphate dehydrogenase +EC 1.1.1.403: D-threitol dehydrogenase (NAD+) +EC 1.1.1.404: tetrachlorobenzoquinone reductase +EC 1.1.1.405: ribitol-5-phosphate 2-dehydrogenase (NADP+) +EC 1.1.1.406: galactitol 2-dehydrogenase (L-tagatose-forming) +EC 1.1.1.407: D-altritol 5-dehydrogenase +EC 1.1.1.408: 4-phospho-D-threonate 3-dehydrogenase +EC 1.1.1.409: 4-phospho-D-erythronate 3-dehydrogenase +EC 1.1.1.410: D-erythronate 2-dehydrogenase +EC 1.1.1.411: L-threonate 2-dehydrogenase +EC 1.1.1.412: 2-alkyl-3-oxoalkanoate reductase +EC 1.1.1.413: A-factor type γ-butyrolactone 1′-reductase (1S-forming) +EC 1.1.1.414: L-galactonate 5-dehydrogenase +EC 1.1.1.415: noscapine synthase +EC 1.1.1.416: isopyridoxal dehydrogenase (5-pyridoxolactone-forming) +EC 1.1.1.417: 3β-hydroxysteroid-4β-carboxylate 3-dehydrogenase (decarboxylating) +EC 1.1.1.418: plant 3β-hydroxysteroid-4α-carboxylate 3-dehydrogenase (decarboxylating) +EC 1.1.1.419: nepetalactol dehydrogenase +EC 1.1.1.420: D-apiose dehydrogenase +EC 1.1.1.421: D-apionate oxidoisomerase +EC 1.1.1.422: pseudoephedrine dehydrogenase +EC 1.1.1.423: (1R,2S)-ephedrine 1-dehydrogenase +EC 1.1.1.424: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,4-lactone-forming) +EC 1.1.1.425: levoglucosan dehydrogenase +EC 1.1.1.426: UDP-N-acetyl-α-D-quinovosamine dehydrogenase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-3.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-3.md new file mode 100644 index 000000000..69c2f28e7 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-3.md @@ -0,0 +1,146 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 4/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.1.2 With a cytochrome as acceptor === +EC 1.1.2.1: glycerolphosphate dehydrogenase. As the acceptor is now known, the enzyme has been transferred to EC 1.1.5.3, glycerol-3-phosphate dehydrogenase. +EC 1.1.2.2: mannitol dehydrogenase (cytochrome) +EC 1.1.2.3: L-lactate dehydrogenase (cytochrome) +EC 1.1.2.4: D-lactate dehydrogenase (cytochrome) +EC 1.1.2.5: D-lactate dehydrogenase (cytochrome c-553) +EC 1.1.2.6: polyvinyl alcohol dehydrogenase (cytochrome) +EC 1.1.2.7: methanol dehydrogenase (cytochrome c) +EC 1.1.2.8: alcohol dehydrogenase (cytochrome c) +EC 1.1.2.9: 1-butanol dehydrogenase (cytochrome c) +EC 1.1.2.10: lanthanide-dependent methanol dehydrogenase +EC 1.1.2.11: glucoside 3-dehydrogenase (cytochrome c) + +=== EC 1.1.3 With oxygen as acceptor === +EC 1.1.3.1: Now included with EC 1.1.3.15 (S)-2-hydroxy-acid oxidase +EC 1.1.3.2: L-lactate oxidase +EC 1.1.3.3: malate oxidase +EC 1.1.3.4: glucose oxidase +EC 1.1.3.5: hexose oxidase +EC 1.1.3.6: cholesterol oxidase +EC 1.1.3.7: aryl-alcohol oxidase +EC 1.1.3.8: L-gulonolactone oxidase +EC 1.1.3.9: galactose oxidase +EC 1.1.3.10: pyranose oxidase +EC 1.1.3.11: L-sorbose oxidase +EC 1.1.3.12: pyridoxine 4-oxidase +EC 1.1.3.13: alcohol oxidase +EC 1.1.3.14: catechol oxidase (dimerizing) +EC 1.1.3.15: (S)-2-hydroxy-acid oxidase +EC 1.1.3.16: ecdysone oxidase +EC 1.1.3.17: choline oxidase +EC 1.1.3.18: Secondary-alcohol oxidase +EC 1.1.3.19: 4-hydroxymandelate oxidase +EC 1.1.3.20: long-chain-alcohol oxidase +EC 1.1.3.21: glycerol-3-phosphate oxidase +EC 1.1.3.22: Now EC 1.17.3.2, xanthine oxidase. The enzyme was incorrectly classified as acting on a CH-OH group +EC 1.1.3.23: Thiamine oxidase +EC 1.1.3.24: L-galactonolactone oxidase +EC 1.1.3.25: Now included with EC 1.1.99.18, cellobiose dehydrogenase (acceptor) +EC 1.1.3.26: Now EC 1.21.3.2, columbamine oxidase +EC 1.1.3.27: hydroxyphytanate oxidase +EC 1.1.3.28: nucleoside oxidase +EC 1.1.3.29: N-acylhexosamine oxidase +EC 1.1.3.30: polyvinyl-alcohol oxidase +EC 1.1.3.31: deleted, cannot be distinguished from EC 1.1.3.13, alcohol oxidase +EC 1.1.3.32: Now EC 1.14.21.1, (S)-stylopine synthase +EC 1.1.3.33: Now EC 1.14.21.2, (S)-cheilanthifoline synthase +EC 1.1.3.34: Now EC 1.14.21.3, berbamunine synthase +EC 1.1.3.35: Now EC 1.14.21.4, salutaridine synthase +EC 1.1.3.36: Now EC 1.14.21.5, (S)-canadine synthase +EC 1.1.3.37: D-arabinono-1,4-lactone oxidase +EC 1.1.3.38: vanillyl-alcohol oxidase +EC 1.1.3.39: nucleoside oxidase (H2O2-forming) +EC 1.1.3.40: D-mannitol oxidase +EC 1.1.3.41: xylitol oxidase +EC 1.1.3.42: prosolanapyrone-II oxidase +EC 1.1.3.43: paromamine 6′-oxidase +EC 1.1.3.44: 6′′′-hydroxyneomycin C oxidase +EC 1.1.3.45: aclacinomycin-N oxidase +EC 1.1.3.46: 4-hydroxymandelate oxidase +EC 1.1.3.47: 5-(hydroxymethyl)furfural oxidase +EC 1.1.3.48: 3-deoxy-α-D-manno-octulosonate 8-oxidase +EC 1.1.3.49: (R)-mandelonitrile oxidase + +=== EC 1.1.4 With a disulfide as acceptor === +EC 1.1.4.1: Now EC 1.17.4.4, vitamin-K-epoxide reductase (warfarin-sensitive) +EC 1.1.4.2: Now EC 1.17.4.5, vitamin-K-epoxide reductase (warfarin-insensitive) + +=== EC 1.1.5 With a quinone or similar compound as acceptor === +EC 1.1.5.1: deleted, see EC 1.1.99.18 cellobiose dehydrogenase (acceptor) +EC 1.1.5.2: quinoprotein glucose dehydrogenase +EC 1.1.5.3: glycerol-3-phosphate dehydrogenase (quinone) +EC 1.1.5.4: malate dehydrogenase (quinone) +EC 1.1.5.5: alcohol dehydrogenase (quinone) +EC 1.1.5.6: formate dehydrogenase-N +EC 1.1.5.7: cyclic alcohol dehydrogenase (quinone) +EC 1.1.5.8: quinate dehydrogenase (quinone) + +=== EC 1.1.9 With a copper protein as acceptor === +EC 1.1.9.1: alcohol dehydrogenase (azurin) + +=== EC 1.1.98 With other, known, acceptors === +EC 1.1.98.1: Now EC 1.1.9.1, alcohol dehydrogenase (azurin) +EC 1.1.98.2: glucose-6-phosphate dehydrogenase (coenzyme-F420) +EC 1.1.98.3: decaprenylphospho-β-D-ribofuranose 2-oxidase +EC 1.1.98.3: decaprenylphospho-β-D-ribofuranose 2-dehydrogenase +EC 1.1.98.4: F420H2:quinone oxidoreductase +EC 1.1.98.5: secondary-alcohol dehydrogenase (coenzyme-F420) +EC 1.1.98.6: ribonucleoside-triphosphate reductase (formate) +EC 1.1.98.7: serine-type anaerobic sulfatase-maturating enzyme + +=== EC 1.1.99 With unknown physiological acceptors === +EC 1.1.99.1: choline dehydrogenase +EC 1.1.99.2: L-2-hydroxyglutarate dehydrogenase +EC 1.1.99.3: gluconate 2-dehydrogenase (acceptor) +EC 1.1.99.4: dehydrogluconate dehydrogenase +EC 1.1.99.5: now EC 1.1.5.3, glycerol-3-phosphate dehydrogenase +EC 1.1.99.6: D-2-hydroxy-acid dehydrogenase +EC 1.1.99.7: lactate—malate transhydrogenase +EC 1.1.99.8: Now EC 1.1.2.7, methanol dehydrogenase (cytochrome c) and EC 1.1.2.8, alcohol dehydrogenase (cytochrome c). +EC 1.1.99.9: pyridoxine 5-dehydrogenase +EC 1.1.99.10: Now EC 1.1.5.9, glucose 1-dehydrogenase (FAD, quinone) +EC 1.1.99.11: Now classified as EC 1.1.5.14, fructose 5-dehydrogenase +EC 1.1.99.12: sorbose dehydrogenase +EC 1.1.99.13: glucoside 3-dehydrogenase +EC 1.1.99.14: glycolate dehydrogenase +EC 1.1.99.15: Now EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H] +EC 1.1.99.16: Now EC EC 1.1.5.4, malate dehydrogenase (quinone) +EC 1.1.99.17: Now EC 1.1.5.2, quinoprotein glucose dehydrogenase +EC 1.1.99.18: cellobiose dehydrogenase (acceptor) +EC 1.1.99.19: Now EC 1.17.99.4, uracil/thymine dehydrogenase +EC 1.1.99.20: alkan-1-ol dehydrogenase (acceptor) +EC 1.1.99.21: D-sorbitol dehydrogenase (acceptor) +EC 1.1.99.22: glycerol dehydrogenase (acceptor) +EC 1.1.99.23: Now EC 1.1.2.6, polyvinyl alcohol dehydrogenase (cytochrome) +EC 1.1.99.24: hydroxyacid-oxoacid transhydrogenase +EC 1.1.99.25: Now EC 1.1.5.8, quinate dehydrogenase (quinone), +EC 1.1.99.26: 3-hydroxycyclohexanone dehydrogenase +EC 1.1.99.27: (R)-pantolactone dehydrogenase (flavin) +EC 1.1.99.28: glucose-fructose oxidoreductase +EC 1.1.99.29: pyranose dehydrogenase (acceptor) +EC 1.1.99.30: 2-oxoacid reductase +EC 1.1.99.31: (S)-mandelate dehydrogenase +EC 1.1.99.32: L-sorbose 1-dehydrogenase +EC 1.1.99.33: Now EC 1.17.99.7, formate dehydrogenase (acceptor) +EC 1.1.99.34: now EC 1.1.98.2, glucose-6-phosphate dehydrogenase (coenzyme-F420) +EC 1.1.99.35: soluble quinoprotein glucose dehydrogenase +EC 1.1.99.36: alcohol dehydrogenase (nicotinoprotein) +EC 1.1.99.37: methanol dehydrogenase (nicotinoprotein) +EC 1.1.99.38: 2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent) +EC 1.1.99.39: D-2-hydroxyglutarate dehydrogenase +EC 1.1.99.40: (R)-2-hydroxyglutarate—pyruvate transhydrogenase +EC 1.1.99.41: 3-hydroxy-1,2-didehydro-2,3-dihydrotabersonine reductase +EC 1.1.99.42: 4-pyridoxic acid dehydrogenase + +== EC 1.2 Acting on the aldehyde or oxo group of donors == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-4.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-4.md new file mode 100644 index 000000000..8a04d78bd --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-4.md @@ -0,0 +1,183 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 5/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.2.1 With NAD+ or NADP+ as acceptor === +EC 1.2.1.1: deleted, replaced by EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase and EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase +EC 1.2.1.2: Now EC 1.17.1.9, formate dehydrogenase +EC 1.2.1.3: aldehyde dehydrogenase (NAD+) +EC 1.2.1.4: aldehyde dehydrogenase (NADP+) +EC 1.2.1.5: aldehyde dehydrogenase (NAD(P)+) +EC 1.2.1.6: deleted (was benzaldehyde dehydrogenase) +EC 1.2.1.7: benzaldehyde dehydrogenase (NADP+) +EC 1.2.1.8: betaine-aldehyde dehydrogenase +EC 1.2.1.9: glyceraldehyde-3-phosphate dehydrogenase (NADP+) +EC 1.2.1.10: acetaldehyde dehydrogenase (acetylating) +EC 1.2.1.11: aspartate-semialdehyde dehydrogenase +EC 1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) +EC 1.2.1.13: glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) +EC 1.2.1.14: Now EC 1.1.1.205, IMP dehydrogenase +EC 1.2.1.15: malonate-semialdehyde dehydrogenase +EC 1.2.1.16: succinate-semialdehyde dehydrogenase [NAD(P)+] +EC 1.2.1.17: glyoxylate dehydrogenase (acylating) +EC 1.2.1.18: malonate-semialdehyde dehydrogenase (acetylating) +EC 1.2.1.19: aminobutyraldehyde dehydrogenase +EC 1.2.1.20: glutarate-semialdehyde dehydrogenase +EC 1.2.1.21: glycolaldehyde dehydrogenase +EC 1.2.1.22: lactaldehyde dehydrogenase +EC 1.2.1.23: 2-oxoaldehyde dehydrogenase (NAD+) +EC 1.2.1.24: succinate-semialdehyde dehydrogenase (NAD+) +EC 1.2.1.25: branched-chain α-keto acid dehydrogenase system +EC 1.2.1.26: 2,5-dioxovalerate dehydrogenase +EC 1.2.1.27: methylmalonate-semialdehyde dehydrogenase (CoA-acylating) +EC 1.2.1.28: benzaldehyde dehydrogenase (NAD+) +EC 1.2.1.29: aryl-aldehyde dehydrogenase +EC 1.2.1.30: aryl-aldehyde dehydrogenase (NADP+) +EC 1.2.1.31: L-aminoadipate-semialdehyde dehydrogenase +EC 1.2.1.32: aminomuconate-semialdehyde dehydrogenase +EC 1.2.1.33: (R)-dehydropantoate dehydrogenase +EC 1.2.1.34: Now EC 1.1.1.131, mannuronate reductase +EC 1.2.1.35: Now EC 1.1.1.203, uronate dehydrogenase +EC 1.2.1.36: retinal dehydrogenase +EC 1.2.1.37: Now EC 1.17.1.4, xanthine dehydrogenase +EC 1.2.1.38: N-acetyl-γ-glutamyl-phosphate reductase +EC 1.2.1.39: phenylacetaldehyde dehydrogenase +EC 1.2.1.40: part of EC 1.14.13.15, cholestanetriol 26-monooxygenase +EC 1.2.1.41: glutamate-5-semialdehyde dehydrogenase +EC 1.2.1.42: hexadecanal dehydrogenase (acylating) +EC 1.2.1.43: Now EC 1.17.1.10, formate dehydrogenase (NADP+) +EC 1.2.1.44: cinnamoyl-CoA reductase +EC 1.2.1.45: Now EC 1.1.1.312, 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase +EC 1.2.1.46: formaldehyde dehydrogenase +EC 1.2.1.47: 4-trimethylammoniobutyraldehyde dehydrogenase +EC 1.2.1.48: long-chain-aldehyde dehydrogenase +EC 1.2.1.49: 2-oxoaldehyde dehydrogenase (NADP+) +EC 1.2.1.50: long-chain-fatty-acyl-CoA reductase +EC 1.2.1.51: pyruvate dehydrogenase (NADP+) +EC 1.2.1.52: deleted 2025 (was oxoglutarate dehydrogenase (NADP+)) +EC 1.2.1.53: 4-hydroxyphenylacetaldehyde dehydrogenase +EC 1.2.1.54: γ-guanidinobutyraldehyde dehydrogenase +EC 1.2.1.55: Now EC 1.1.1.279, (R)-3-hydroxyacid-ester dehydrogenase +EC 1.2.1.56: Now EC 1.1.1.280, (S)-3-hydroxyacid-ester dehydrogenase +EC 1.2.1.57: butanal dehydrogenase +EC 1.2.1.58: phenylglyoxylate dehydrogenase (acylating) +EC 1.2.1.59: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) +EC 1.2.1.60: 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase +EC 1.2.1.61: 4-hydroxymuconic-semialdehyde dehydrogenase +EC 1.2.1.62: 4-formylbenzenesulfonate dehydrogenase +EC 1.2.1.63: 6-oxohexanoate dehydrogenase +EC 1.2.1.64: 4-hydroxybenzaldehyde dehydrogenase (NAD+) +EC 1.2.1.65: salicylaldehyde dehydrogenase +EC 1.2.1.66: Now EC 1.1.1.306, S-(hydroxymethyl)mycothiol dehydrogenase +EC 1.2.1.67: vanillin dehydrogenase +EC 1.2.1.68: coniferyl-aldehyde dehydrogenase +EC 1.2.1.69: fluoroacetaldehyde dehydrogenase +EC 1.2.1.70: glutamyl-tRNA reductase +EC 1.2.1.71: succinylglutamate-semialdehyde dehydrogenase +EC 1.2.1.72: erythrose-4-phosphate dehydrogenase +EC 1.2.1.73: sulfoacetaldehyde dehydrogenase +EC 1.2.1.74: abieta-7,13-dien-18-al dehydrogenase +EC 1.2.1.75: malonyl CoA reductase (malonate semialdehyde-forming) +EC 1.2.1.76: succinate-semialdehyde dehydrogenase (acylating) +EC 1.2.1.77: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) +EC 1.2.1.78: 2-formylbenzoate dehydrogenase +EC 1.2.1.79: succinate-semialdehyde dehydrogenase (NADP+) +EC 1.2.1.80: long-chain acyl-[acyl-carrier-protein] reductase +EC 1.2.1.81: sulfoacetaldehyde dehydrogenase (acylating) +EC 1.2.1.82: β-apo-4′-carotenal oxygenase +EC 1.2.1.83: 3-succinoylsemialdehyde-pyridine dehydrogenase +EC 1.2.1.84: alcohol-forming fatty acyl-CoA reductase +EC 1.2.1.85: 2-hydroxymuconate-6-semialdehyde dehydrogenase +EC 1.2.1.86: geranial dehydrogenase +EC 1.2.1.87: propanal dehydrogenase (CoA-propanoylating) +EC 1.2.1.88: L-glutamate γ-semialdehyde dehydrogenase +EC 1.2.1.89: D-glyceraldehyde dehydrogenase (NADP+) +EC 1.2.1.90: glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] +EC 1.2.1.91: 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase +EC 1.2.1.92: 3,6-anhydro-α-L-galactose dehydrogenase +EC 1.2.1.93: formate dehydrogenase (NAD+, ferredoxin). Now EC 1.17.1.11, formate dehydrogenase (NAD+, ferredoxin) * +EC 1.2.1.94: farnesal dehydrogenase +EC 1.2.1.95: L-2-aminoadipate reductase +EC 1.2.1.96: 4-hydroxybenzaldehyde dehydrogenase (++) +EC 1.2.1.97: 3-sulfolactaldehyde dehydrogenase +EC 1.2.1.98: 2-hydroxy-2-methylpropanal dehydrogenase +EC 1.2.1.99: 4-(γ-glutamylamino)butanal dehydrogenase +EC 1.2.1.100: 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase +EC 1.2.1.101: L-tyrosine reductase +EC 1.2.1.102: isopyridoxal dehydrogenase (5-pyridoxate-forming) +EC 1.2.1.103: [amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase +EC 1.2.1.104: pyruvate dehydrogenase system +EC 1.2.1.105: 2-oxoglutarate dehydrogenase system +EC 1.2.1.106: [amino-group carrier protein]-5-phospho-L-glutamate reductase +EC 1.2.1.107: glyceraldehyde-3-phosphate dehydrogenase (arsenate-transferring) + +=== EC 1.2.2 With a cytochrome as acceptor === +EC 1.2.2.1: formate dehydrogenase (cytochrome) +EC 1.2.2.2: Now covered by EC 1.2.5.1, pyruvate dehydrogenase (quinone) +EC 1.2.2.3: Now EC 1.17.2.3, formate dehydrogenase (cytochrome-c-553) +EC 1.2.2.4: Now classified as EC 1.2.5.3, aerobic carbon monoxide dehydrogenase + +=== EC 1.2.3 With oxygen as acceptor === +EC 1.2.3.1: aldehyde oxidase +EC 1.2.3.2: Now EC 1.17.3.2, xanthine oxidase +EC 1.2.3.3: pyruvate oxidase +EC 1.2.3.4: oxalate oxidase +EC 1.2.3.5: glyoxylate oxidase +EC 1.2.3.6: pyruvate oxidase (CoA-acetylating) +EC 1.2.3.7: indole-3-acetaldehyde oxidase +EC 1.2.3.8: pyridoxal oxidase +EC 1.2.3.9: aryl-aldehyde oxidase +EC 1.2.3.10: deleted, activity due to EC 1.2.2.4 carbon-monoxide dehydrogenase (cytochrome b-561) +EC 1.2.3.11: Now included with EC 1.2.3.1, aldehyde oxidase +EC 1.2.3.12: Now included with EC 1.2.3.1, aldehyde oxidase +EC 1.2.3.13: Now EC 1.14.13.82, vanillate monooxygenase +EC 1.2.3.14: Abscisic-aldehyde oxidase +EC 1.2.3.15: (methyl)glyoxal oxidase + +=== EC 1.2.4 With a disulfide as acceptor === +EC 1.2.4.1: pyruvate dehydrogenase (acetyl-transferring) +EC 1.2.4.2: oxoglutarate dehydrogenase (succinyl-transferring) +EC 1.2.4.3: Now included with EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) +EC 1.2.4.4: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) + +=== EC 1.2.5 With a quinone or similar compound as acceptor === +EC 1.2.5.1: pyruvate dehydrogenase (quinone) +EC 1.2.5.2: aldehyde dehydrogenase (quinone) +EC 1.2.5.3: aerobic carbon monoxide dehydrogenase + +=== EC 1.2.7 With an iron–sulfur protein as acceptor === +EC 1.2.7.1: pyruvate synthase +EC 1.2.7.2: Now included with EC 1.2.7.1, pyruvate synthase. +EC 1.2.7.3: 2-oxoglutarate synthase +EC 1.2.7.4: anaerobic carbon monoxide dehydrogenase +EC 1.2.7.5: aldehyde ferredoxin oxidoreductase +EC 1.2.7.6: glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) +EC 1.2.7.7: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) +EC 1.2.7.8: indolepyruvate ferredoxin oxidoreductase +EC 1.2.7.9: deleted, identical to EC 1.2.7.3, 2-oxoglutarate synthase +EC 1.2.7.10: oxalate oxidoreductase +EC 1.2.7.11: 2-oxoacid oxidoreductase (ferredoxin) +EC 1.2.7.12: formylmethanofuran dehydrogenase + +=== EC 1.2.98: With other, known physiological acceptors === +EC 1.2.98.1: formaldehyde dismutase + +=== EC 1.2.99: With unknown physiological acceptors === +EC 1.2.99.1: Now EC 1.17.99.4, uracil/thymine dehydrogenase +EC 1.2.99.2: Now EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) +EC 1.2.99.3: Now EC 1.2.5.2, aldehyde dehydrogenase (quinone) +EC 1.2.99.4: Now EC 1.2.98.1, formaldehyde dismutase +EC 1.2.99.5: Now EC 1.2.7.12, formylmethanofuran dehydrogenase +EC 1.2.99.6: carboxylate reductase +EC 1.2.99.7: aldehyde dehydrogenase (FAD-independent) +EC 1.2.99.8: glyceraldehyde dehydrogenase (FAD-containing) +EC 1.2.99.9: Now EC 1.17.98.3, formate dehydrogenase (coenzyme F420) +EC 1.2.99.10: 4,4′-diapolycopenoate synthase + +== EC 1.3 Acting on the CH-CH group of donors == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-5.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-5.md new file mode 100644 index 000000000..db75bdbce --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-5.md @@ -0,0 +1,202 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 6/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.3.1 With NAD+ or NADP+ as acceptor === +EC 1.3.1.1: dihydrouracil dehydrogenase (NAD+) +EC 1.3.1.2: dihydropyrimidine dehydrogenase (NADP+) +EC 1.3.1.3: Δ4-3-oxosteroid 5β-reductase +EC 1.3.1.4: transferred to EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+) +EC 1.3.1.5: cucurbitacin Δ23-reductase +EC 1.3.1.6: fumarate reductase (NADH) +EC 1.3.1.7: meso-tartrate dehydrogenase +EC 1.3.1.8: acyl-CoA dehydrogenase (NADP+) +EC 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH) +EC 1.3.1.10: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) +EC 1.3.1.11: 2-coumarate reductase +EC 1.3.1.12: prephenate dehydrogenase +EC 1.3.1.13: prephenate dehydrogenase (NADP+) +EC 1.3.1.14: dihydroorotate dehydrogenase (NAD+) +EC 1.3.1.15: dihydroorotate dehydrogenase (NADP+) +EC 1.3.1.16: β-nitroacrylate reductase +EC 1.3.1.17: 3-methyleneoxindole reductase +EC 1.3.1.18: kynurenate-7,8-dihydrodiol dehydrogenase +EC 1.3.1.19: cis-1,2-dihydrobenzene-1,2-diol dehydrogenase +EC 1.3.1.20: trans-1,2-dihydrobenzene-1,2-diol dehydrogenase +EC 1.3.1.21: 7-dehydrocholesterol reductase +EC 1.3.1.22: 3-oxo-5α-steroid 4-dehydrogenase (NADP+) +EC 1.3.1.23: Identical to EC 1.3.1.3, Δ4-3-oxosteroid 5β-reductase +EC 1.3.1.24: biliverdin reductase +EC 1.3.1.25: 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase +EC 1.3.1.26: Now EC 1.17.1.8, 4-hydroxy-tetrahydrodipicolinate reductase +EC 1.3.1.27: 2-hexadecenal reductase +EC 1.3.1.28: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase +EC 1.3.1.29: cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase +EC 1.3.1.30: transferred to EC 1.3.1.22, 3-oxo-5α-steroid 4-dehydrogenase (NADP+) +EC 1.3.1.31: 2-enoate reductase +EC 1.3.1.32: maleylacetate reductase +EC 1.3.1.33: protochlorophyllide reductase +EC 1.3.1.34: 2,4 Dienoyl-CoA reductase (NADPH) +EC 1.3.1.35: Now EC 1.14.19.22, microsomal oleoyl-lipid 12-desaturase +EC 1.3.1.36: geissoschizine dehydrogenase +EC 1.3.1.37: cis-2-enoyl-CoA reductase (NADPH) +EC 1.3.1.38: trans-2-enoyl-CoA reductase (NADPH) +EC 1.3.1.39: trans-2-enoyl-CoA reductase (NADPH) +EC 1.3.1.40: 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase +EC 1.3.1.41: xanthommatin reductase +EC 1.3.1.42: 12-oxophytodienoate reductase +EC 1.3.1.43: arogenate dehydrogenase +EC 1.3.1.44: trans-2-enoyl-CoA reductase (NAD+) +EC 1.3.1.45: 2′-hydroxyisoflavone reductase +EC 1.3.1.46: biochanin-A reductase +EC 1.3.1.47: α-santonin 1,2-reductase +EC 1.3.1.48: 13,14-dehydro-15-oxoprostaglandin 13-reductase +EC 1.3.1.49: cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase +EC 1.3.1.50: n Now EC 1.1.1.252 tetrahydroxynaphthalene reductase +EC 1.3.1.51: 2′-hydroxydaidzein reductase +EC 1.3.1.52: Now EC 1.3.8.5, 2-methyl-branched-chain-enoyl-CoA reductase +EC 1.3.1.53: (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase +EC 1.3.1.54: precorrin-6A reductase +EC 1.3.1.55: identical to EC 1.3.1.25, 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase +EC 1.3.1.56: cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase +EC 1.3.1.57: phloroglucinol reductase +EC 1.3.1.58: 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase +EC 1.3.1.59: There is no evidence that the enzyme exists +EC 1.3.1.60: dibenzothiophene dihydrodiol dehydrogenase +EC 1.3.1.61: identical to EC 1.3.1.53, (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase +EC 1.3.1.62: pimeloyl-CoA dehydrogenase +EC 1.3.1.63: Now EC 1.21.1.2, 2,4-dichlorobenzoyl-CoA reductase +EC 1.3.1.64: phthalate 4,5-cis-dihydrodiol dehydrogenase +EC 1.3.1.65: 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline dehydrogenase +EC 1.3.1.66: cis-dihydroethylcatechol dehydrogenase +EC 1.3.1.67: cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate dehydrogenase +EC 1.3.1.68: 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase +EC 1.3.1.69: zeatin reductase +EC 1.3.1.70: Δ14-sterol reductase +EC 1.3.1.71: Δ24(241)-sterol reductase +EC 1.3.1.72: Δ24-sterol reductase +EC 1.3.1.73: 1,2-dihydrovomilenine reductase +EC 1.3.1.74: 2-alkenal reductase [NAD(P)+] +EC 1.3.1.75: 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH) +EC 1.3.1.76: precorrin-2 dehydrogenase +EC 1.3.1.77: anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming] +EC 1.3.1.78: arogenate dehydrogenase (NADP+) +EC 1.3.1.79: arogenate dehydrogenase (NAD(P)+) +EC 1.3.1.80: Now classified as EC 1.3.7.12, red chlorophyll catabolite reductase +EC 1.3.1.81: (+)-pulegone reductase +EC 1.3.1.82: (-)-isopiperitenone reductase +EC 1.3.1.83: geranylgeranyl diphosphate reductase +EC 1.3.1.84: acrylyl-CoA reductase (NADPH) +EC 1.3.1.85: crotonyl-CoA carboxylase/reductase +EC 1.3.1.86: crotonyl-CoA reductase +EC 1.3.1.87: 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase +EC 1.3.1.88: tRNA-dihydrouridine16/17 synthase (NAD(P)+) +EC 1.3.1.89: tRNA-dihydrouridine47 synthase (NAD(P)+) +EC 1.3.1.90: tRNA-dihydrouridine20a/20b synthase (NAD(P)+) +EC 1.3.1.91: tRNA-dihydrouridine20 synthase (NAD(P)+) +EC 1.3.1.92: artemisinic aldehyde Δ11(13)-reductase +EC 1.3.1.93: very-long-chain enoyl-CoA reductase +EC 1.3.1.94: polyprenol reductase +EC 1.3.1.95: acrylyl-CoA reductase (NADH) +EC 1.3.1.96: Botryococcus squalene synthase +EC 1.3.1.97: botryococcene synthase +EC 1.3.1.98: Now known to be catalyzed by two different enzymes, EC 1.3.1.122, (S)-8-oxocitronellyl enol synthase, and EC 5.5.1.34, (+)-cis,trans-nepetalactol synthase +EC 1.3.1.100: chanoclavine-I aldehyde reductase +EC 1.3.1.101: 2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase [NAD(P)H] +EC 1.3.1.102: 2-alkenal reductase (NADP+) +EC 1.3.1.103: 2-haloacrylate reductase +EC 1.3.1.104: enoyl-[acyl-carrier-protein] reductase (NADPH) +EC 1.3.1.105: 2-methylene-furan-3-one reductase +EC 1.3.1.106: cobalt-precorrin-6A reductase +EC 1.3.1.107: sanguinarine reductase +EC 1.3.1.108: caffeoyl-CoA reductase +EC 1.3.1.109: butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin) +EC 1.3.1.110: lactate dehydrogenase (NAD+,ferredoxin) +EC 1.3.1.111: geranylgeranyl-bacteriochlorophyllide a reductase +EC 1.3.1.112: anthocyanidin reductase [(2S)-flavan-3-ol-forming] +EC 1.3.1.113: (4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate reductase +EC 1.3.1.114: 3-dehydro-bile acid Δ4,6-reductase +EC 1.3.1.115: 3-oxocholoyl-CoA 4-desaturase +EC 1.3.1.116: 7β-hydroxy-3-oxochol-24-oyl-CoA 4-desaturase +EC 1.3.1.117: hydroxycinnamoyl-CoA reductase +EC 1.3.1.118: meromycolic acid enoyl-[acyl-carrier-protein] reductase +EC 1.3.1.119: chlorobenzene dihydrodiol dehydrogenase +EC 1.3.1.120: cyclohexane-1-carbonyl-CoA reductase NADP+) +EC 1.3.1.121: 4-amino-4-deoxyprephenate dehydrogenase +EC 1.3.1.122: (S)-8-oxocitronellyl enol synthase +EC 1.3.1.123: 8-oxogeranial reductase +EC 1.3.1.124: 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing] + +=== EC 1.3.2 With a cytochrome as acceptor === +EC 1.3.2.1: now EC 1.3.99.2 +EC 1.3.2.2: now EC 1.3.99.3 +EC 1.3.2.3: galactonolactone dehydrogenase + +=== EC 1.3.3 With oxygen as acceptor === +EC 1.3.3.1: dihydroorotate oxidase +EC 1.3.3.2: Now EC 1.14.19.20 Δ7-sterol 5(6)-desaturase +EC 1.3.3.3: coproporphyrinogen oxidase +EC 1.3.3.4: protoporphyrinogen oxidase +EC 1.3.3.5: bilirubin oxidase +EC 1.3.3.6: acyl-CoA oxidase +EC 1.3.3.7: dihydrouracil oxidase +EC 1.3.3.8: tetrahydroberberine oxidase +EC 1.3.3.9: Now EC 1.14.19.62 secologanin synthase +EC 1.3.3.10: tryptophan a,b-oxidase +EC 1.3.3.11: pyrroloquinoline-quinone synthase +EC 1.3.3.12: l-galactonolactone oxidase + +=== EC 1.3.5 With a quinone or related compound as acceptor === +EC 1.3.5.1: succinate dehydrogenase (quinone) +EC 1.3.5.2: dihydroorotate dehydrogenase (quinone) +EC 1.3.5.3: protoporphyrinogen IX dehydrogenase (menaquinone) +EC 1.3.5.4: fumarate reductase (quinol) +EC 1.3.5.5: 15-cis-phytoene desaturase +EC 1.3.5.6: 9,9'-dicis-zeta-carotene desaturase + +=== EC 1.3.7 With an iron–sulfur protein as acceptor === +EC 1.3.7.1: 6-hydroxynicotinate reductase +EC 1.3.7.2: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase +EC 1.3.7.3: phycoerythrobilin:ferredoxin oxidoreductase +EC 1.3.7.4: phytochromobilin:ferredoxin oxidoreductase +EC 1.3.7.5: phycocyanobilin:ferredoxin oxidoreductase +EC 1.3.7.6: phycoerythrobilin synthase +EC 1.3.7.7: ferredoxin:protochlorophyllide reductase (ATP-dependent) +EC 1.3.7.8: benzoyl-CoA reductase +EC 1.3.7.9: 4-hydroxybenzoyl-CoA reductase +EC 1.3.7.10: pentalenolactone synthase +EC 1.3.7.15: chlorophyllide a reductase + +=== EC 1.3.8 With a flavin as acceptor === +EC 1.3.8.1: short-chain acyl-CoA dehydrogenase +EC 1.3.8.2: 4,4′-diapophytoene desaturase (4,4′-diapolycopene-forming) +EC 1.3.8.3: (R)-benzylsuccinyl-CoA dehydrogenase +EC 1.3.8.4: isovaleryl-CoA dehydrogenase +EC 1.3.8.5: 2-methyl-branched-chain-enoyl-CoA reductase +EC 1.3.8.6: glutaryl-CoA dehydrogenase (ETF) +EC 1.3.8.7: medium-chain acyl-CoA dehydrogenase +EC 1.3.8.8: long-chain acyl-CoA dehydrogenase +EC 1.3.8.9: very-long-chain acyl-CoA dehydrogenase +EC 1.3.8.10: cyclohex-1-ene-1-carbonyl-CoA dehydrogenase +EC 1.3.8.11: cyclohexane-1-carbonyl-CoA dehydrogenase (electron-transfer flavoprotein) +EC 1.3.8.12: (2S)-methylsuccinyl-CoA dehydrogenase +EC 1.3.8.13: crotonobetainyl-CoA reductase +EC 1.3.8.14: L-prolyl-[peptidyl-carrier protein] dehydrogenase +EC 1.3.8.15: 3-(aryl)acrylate reductase +EC 1.3.8.16: 2-amino-4-deoxychorismate dehydrogenase +EC 1.3.8.17: dehydro coenzyme F420 reductase + +=== EC 1.3.98 With other,known physiological acceptors === +EC 1.3.98.1: dihydroorotate dehydrogenase (fumarate) +EC 1.3.98.2: Now EC 1.3.4.1, fumarate reductase (CoM/CoB) +EC 1.3.98.3: coproporphyrinogen dehydrogenase +EC 1.3.98.4: 5a,11a-dehydrotetracycline reductase +EC 1.3.98.5: hydrogen peroxide-dependent heme synthase +EC 1.3.98.6: AdoMet-dependent heme synthase +EC 1.3.98.7: [mycofactocin precursor peptide]-tyrosine decarboxylase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-6.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-6.md new file mode 100644 index 000000000..882cbcddb --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-6.md @@ -0,0 +1,141 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 7/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.3.99 With unknown physiological acceptors === +EC 1.3.99.1: The activity is included in EC 1.3.5.1, succinate dehydrogenase (quinone) +EC 1.3.99.2: Now EC 1.3.8.1, butyryl-CoA dehydrogenase. +EC 1.3.99.3: now EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase +EC 1.3.99.4: 3-oxosteroid 1-dehydrogenase +EC 1.3.99.5: 3-oxo-5α-steroid 4-dehydrogenase (acceptor) +EC 1.3.99.6: 3-oxo-5β-steroid 4-dehydrogenase +EC 1.3.99.7: Now EC 1.3.8.6, glutaryl-CoA dehydrogenase +EC 1.3.99.8: 2-furoyl-CoA dehydrogenase +EC 1.3.99.9: Now EC 1.21.99.1, β-cyclopiazonate dehydrogenase +EC 1.3.99.10: Now EC 1.3.8.4, isovaleryl-CoA dehydrogenase +EC 1.3.99.11: transferred to EC 1.3.5.2, dihydroorotate dehydrogenase +EC 1.3.99.12: Now classified as EC 1.3.8.5, 2-methyl-branched-chain-enoyl-CoA reductase +EC 1.3.99.13: Now EC 1.3.8.8, long-chain-acyl-CoA dehydrogenase +EC 1.3.99.14: cyclohexanone dehydrogenase +EC 1.3.99.15: Now EC 1.3.7.8 +EC 1.3.99.16: isoquinoline 1-oxidoreductase +EC 1.3.99.17: quinoline 2-oxidoreductase +EC 1.3.99.18: quinaldate 4-oxidoreductase +EC 1.3.99.19: quinoline-4-carboxylate 2-oxidoreductase +EC 1.3.99.20: Now EC 1.3.7.9, 4-hydroxybenzoyl-CoA reductase +EC 1.3.99.21: Now EC 1.3.8.3, (R)-benzylsuccinyl-CoA dehydrogenase +EC 1.3.99.22: Now EC 1.3.98.3, coproporphyrinogen dehydrogenase +EC 1.3.99.23: all-trans-retinol 13,14-reductase +EC 1.3.99.24: Now EC 1.3.8.16, 2-amino-4-deoxychorismate dehydrogenase +EC 1.3.99.25: carvone reductase +EC 1.3.99.26: all-trans-ζ-carotene desaturase +EC 1.3.99.27: 1-hydroxycarotenoid 3,4-desaturase +EC 1.3.99.28: phytoene desaturase (neurosporene-forming) +EC 1.3.99.29: phytoene desaturase (zeta-carotene-forming) +EC 1.3.99.30: phytoene desaturase (3,4-didehydrolycopene-forming) +EC 1.3.99.31: phytoene desaturase (lycopene-forming) +EC 1.3.99.32: glutaryl-CoA dehydrogenase (non-decarboxylating) +EC 1.3.99.33: urocanate reductase +EC 1.3.99.34: Now classified as EC 1.3.7.11, 2,3-bis-O-geranylgeranyl-sn-glycero-phospholipid reductase +EC 1.3.99.35: Now EC 1.3.7.15, chlorophyllide a reductase * +EC 1.3.99.36: cypemycin cysteine dehydrogenase (decarboxylating) +EC 1.3.99.37: 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase +EC 1.3.99.38: menaquinone-9 β-reductase +EC 1.3.99.39: carotenoid φ-ring synthase +EC 1.3.99.40: carotenoid χ-ring synthase + +== EC 1.4 Acting on the CH-NH2 group of donors == + +=== EC 1.4.1 With NAD+ or NADP+ as acceptor === +EC 1.4.1.1: alanine dehydrogenase +EC 1.4.1.2: glutamate dehydrogenase +EC 1.4.1.3: glutamate dehydrogenase (NAD(P)+) +EC 1.4.1.4: glutamate dehydrogenase (NADP+) +EC 1.4.1.5: L-amino-acid dehydrogenase +EC 1.4.1.6: deleted, Now included with EC 1.21.4.1, D-proline reductase (dithiol) +EC 1.4.1.7: serine 2-dehydrogenase +EC 1.4.1.8: valine dehydrogenase (NADP+) +EC 1.4.1.9: leucine dehydrogenase +EC 1.4.1.10: glycine dehydrogenase +EC 1.4.1.11: L-erythro-3,5-diaminohexanoate dehydrogenase +EC 1.4.1.12: 2,4-diaminopentanoate dehydrogenase +EC 1.4.1.13: glutamate synthase (NADPH) +EC 1.4.1.14: glutamate synthase (NADH) +EC 1.4.1.15: lysine dehydrogenase +EC 1.4.1.16: diaminopimelate dehydrogenase +EC 1.4.1.17: N-methylalanine dehydrogenase +EC 1.4.1.18: lysine 6-dehydrogenase +EC 1.4.1.19: tryptophan dehydrogenase +EC 1.4.1.20: phenylalanine dehydrogenase +EC 1.4.1.21: aspartate dehydrogenase +EC 1.4.1.22: there is no overall consumption of NAD+ during the reaction. As a result, transfer of the enzyme from EC 4.3.1.12 was not necessary and EC 1.4.1.22 was withdrawn before being made official +EC 1.4.1.23: valine dehydrogenase (NAD+) +EC 1.4.1.24: 3-dehydroquinate synthase II +EC 1.4.1.25: L-arginine dehydrogenase +EC 1.4.1.26: 2,4-diaminopentanoate dehydrogenase (NAD+) +EC 1.4.1.27: glycine cleavage system + +=== EC 1.4.2 With a cytochrome as acceptor === +EC 1.4.2.1: glycine dehydrogenase (cytochrome) +EC 1.4.2.3: pseudooxynicotine oxidase + +=== EC 1.4.3 With oxygen as acceptor === +EC 1.4.3.1: D-aspartate oxidase +EC 1.4.3.2: L-amino-acid oxidase +EC 1.4.3.3: D-amino-acid oxidase +EC 1.4.3.4: monoamine oxidase +EC 1.4.3.5: pyridoxal 5′-phosphate synthase +EC 1.4.3.6: replaced by two enzymes, EC 1.4.3.21 (primary-amine oxidase) and EC 1.4.3.22 (diamine oxidase) +EC 1.4.3.7: D-glutamate oxidase +EC 1.4.3.8: ethanolamine oxidase +EC 1.4.3.9: Now included with EC 1.4.3.4 amine oxidase (flavin-containing) +EC 1.4.3.10: putrescine oxidase +EC 1.4.3.11: L-glutamate oxidase +EC 1.4.3.12: cyclohexylamine oxidase +EC 1.4.3.13: protein-lysine 6-oxidase +EC 1.4.3.14: L-lysine oxidase +EC 1.4.3.15: D-glutamate(D-aspartate) oxidase +EC 1.4.3.16: L-aspartate oxidase +EC 1.4.3.17: Now EC 1.3.3.10, tryptophan α,β-oxidase +EC 1.4.3.18: Not approved as the enzyme was shown to be a dehydrogenase and not an oxidase (see EC 1.5.99.12, cytokinin dehydrogenase) +EC 1.4.3.19: glycine oxidase +EC 1.4.3.20: L-lysine 6-oxidase +EC 1.4.3.21: primary-amine oxidase +EC 1.4.3.22: diamine oxidase +EC 1.4.3.23: 7-chloro-L-tryptophan oxidase +EC 1.4.3.24: Now EC 1.4.2.3, pseudooxynicotine oxidase +EC 1.4.3.25: L-arginine oxidase +EC 1.4.3.26: pre-mycofactocin synthase + +=== EC 1.4.4 With a disulfide as acceptor === +EC 1.4.4.1: Now EC 1.21.4.1, D-proline reductase (dithiol) +EC 1.4.4.2: glycine dehydrogenase (aminomethyl-transferring) + +=== EC 1.4.5 With a quinone or other compound as acceptor === +EC 1.4.5.1: D-amino acid dehydrogenase (quinone) + +=== EC 1.4.7 With an iron–sulfur protein as acceptor === +EC 1.4.7.1: glutamate synthase (ferredoxin) + +=== EC 1.4.9 With a copper protein as acceptor === +EC 1.4.9.1: methylamine dehydrogenase (amicyanin) +EC 1.4.9.2: aralkylamine dehydrogenase (azurin) + +=== EC 1.4.98 With other, known physiological acceptors === +EC 1.4.98.1: NOW 1.4.9.1 methylamine dehydrogenase (amicyanin) + +=== EC 1.4.99 With unknown physiological acceptors === +EC 1.4.99.1: Now EC 1.4.99.6, D-arginine dehydrogenase +EC 1.4.99.2: taurine dehydrogenase +EC 1.4.99.3: Now EC 1.4.9.1, methylamine dehydrogenase (amicyanin) +EC 1.4.99.4: Now EC 1.4.9.2, aralkylamine dehydrogenase (azurin) +EC 1.4.99.5: glycine dehydrogenase (cyanide-forming) +EC 1.4.99.6: D-arginine dehydrogenase + +== EC 1.5 Acting on the CH-NH group of donors == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-7.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-7.md new file mode 100644 index 000000000..b052e4134 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-7.md @@ -0,0 +1,177 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 8/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.5.1 With NAD+ or NADP+ as acceptor === +EC 1.5.1.1: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NAD(P)H) +EC 1.5.1.2: pyrroline-5-carboxylate reductase +EC 1.5.1.3: dihydrofolate reductase +EC 1.5.1.4: Now included with EC 1.5.1.3 dihydrofolate reductase +EC 1.5.1.5: methylenetetrahydrofolate dehydrogenase (NADP+) +EC 1.5.1.6: formyltetrahydrofolate dehydrogenase +EC 1.5.1.7: saccharopine dehydrogenase (NAD+, L-lysine-forming) +EC 1.5.1.8: saccharopine dehydrogenase (NADP+, L-lysine-forming) +EC 1.5.1.9: saccharopine dehydrogenase (NAD+, L-glutamate-forming) +EC 1.5.1.10: saccharopine dehydrogenase (NADP+, L-glutamate-forming) +EC 1.5.1.11: D-octopine dehydrogenase +EC 1.5.1.12: Now EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase +EC 1.5.1.13: Now EC 1.17.1.5, nicotinate dehydrogenase +EC 1.5.1.14: Now included with EC 1.5.1.21 Δ1-piperideine-2-carboxylate reductase +EC 1.5.1.15: methylenetetrahydrofolate dehydrogenase (NAD+) +EC 1.5.1.16: D-lysopine dehydrogenase +EC 1.5.1.17: alanopine dehydrogenase +EC 1.5.1.18: ephedrine dehydrogenase +EC 1.5.1.19: D-nopaline dehydrogenase +EC 1.5.1.20: methylenetetrahydrofolate reductase (NAD(P)H) +EC 1.5.1.21: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase (NADPH) +EC 1.5.1.22: strombine dehydrogenase +EC 1.5.1.23: tauropine dehydrogenase +EC 1.5.1.24: N5-(carboxyethyl)ornithine synthase +EC 1.5.1.25: thiomorpholine-carboxylate dehydrogenase +EC 1.5.1.26: β-alanopine dehydrogenase +EC 1.5.1.27: 1,2-dehydroreticulinium reductase (NADPH) +EC 1.5.1.28: opine dehydrogenase +EC 1.5.1.29: Now covered by EC 1.5.1.38 [FMN reductase (NADPH)], EC 1.5.1.39 [FMN reductase [NAD(P)H])] and EC 1.5.1.41 (riboflavin reductase [NAD(P)H]) +EC 1.5.1.30: flavin reductase (NADPH) +EC 1.5.1.31: berberine reductase +EC 1.5.1.32: vomilenine reductase +EC 1.5.1.33: pteridine reductase +EC 1.5.1.34: 6,7-dihydropteridine reductase +EC 1.5.1.35: identical to EC 1.2.1.19, aminobutyraldehyde dehydrogenase, as the substrates 1-pyrroline and 4-aminobutanal are interconvertible +EC 1.5.1.36: flavin reductase (NADH) +EC 1.5.1.37: FAD reductase (NADH) +EC 1.5.1.38: FMN reductase (NADPH) +EC 1.5.1.39: FMN reductase (NAD(P)H) +EC 1.5.1.40: 8-hydroxy-5-deazaflavin:NADPH oxidoreductase +EC 1.5.1.41: riboflavin reductase (NAD(P)H) +EC 1.5.1.42: FMN reductase (NADH) +EC 1.5.1.43: carboxynorspermidine synthase +EC 1.5.1.44: festuclavine dehydrogenase +EC 1.5.1.45: FAD reductase (NAD(P)H) +EC 1.5.1.46: agroclavine dehydrogenase +EC 1.5.1.47: dihydromethanopterin reductase [NAD(P)+] +EC 1.5.1.48: 2-methyl-1-pyrroline reductase +EC 1.5.1.49: 1-pyrroline-2-carboxylate reductase [NAD(P)H] +EC 1.5.1.50: dihydromonapterin reductase +EC 1.5.1.51: N-[(2S)-2-amino-2-carboxyethyl]-L-lutamate dehydrogenase +EC 1.5.1.52: staphylopine dehydrogenase +EC 1.5.1.53: methylenetetrahydrofolate reductase (NADPH) +EC 1.5.1.54: methylenetetrahydrofolate reductase (NADH) + +=== EC 1.5.3 With oxygen as acceptor === +EC 1.5.3.1: sarcosine oxidase +EC 1.5.3.2: N-methyl-L-amino-acid oxidase +EC 1.5.3.3: deleted +EC 1.5.3.4: N6-methyl-lysine oxidase +EC 1.5.3.5: (S)-6-hydroxynicotine oxidase +EC 1.5.3.6: (R)-6-hydroxynicotine oxidase +EC 1.5.3.7: L-pipecolate oxidase +EC 1.5.3.8: Now included with EC 1.3.3.8, tetrahydroberberine oxidase +EC 1.5.3.9: Now EC 1.21.3.3, reticuline oxidase +EC 1.5.3.10: dimethylglycine oxidase +EC 1.5.3.11: Now included with EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase) +EC 1.5.3.12: dihydrobenzophenanthridine oxidase +EC 1.5.3.13: N1-acetylpolyamine oxidase +EC 1.5.3.14: polyamine oxidase (propane-1,3-diamine-forming) +EC 1.5.3.15: N8-acetylspermidine oxidase (propane-1,3-diamine-forming) +EC 1.5.3.16: spermine oxidase +EC 1.5.3.17: non-specific polyamine oxidase +EC 1.5.3.18: L-saccharopine oxidase +EC 1.5.3.19: 4-methylaminobutanoate oxidase (formaldehyde-forming) +EC 1.5.3.20: N-alkylglycine oxidase +EC 1.5.3.21: 4-methylaminobutanoate oxidase (methylamine-forming) +EC 1.5.3.22: coenzyme F420H2 oxidase +EC 1.5.3.23: glyphosate oxidoreductase + +=== EC 1.5.4 With a disulfide as acceptor === +EC 1.5.4.1: pyrimidodiazepine synthase + +=== EC 1.5.5 With a quinone or similar compound as acceptor === +EC 1.5.5.1: electron-transferring-flavoprotein dehydrogenase +EC 1.5.5.2: proline dehydrogenase +EC 1.5.5.3: hydroxyproline dehydrogenase + +=== EC 1.5.7 With an iron–sulfur protein as acceptor === +EC 1.5.7.1: methylenetetrahydrofolate reductase (ferredoxin) +EC 1.5.7.2: coenzyme F420 oxidoreductase (ferredoxin) + +=== EC 1.5.8 With a flavin or flavoprotein as acceptor === +EC 1.5.8.1: dimethylamine dehydrogenase +EC 1.5.8.2: trimethylamine dehydrogenase +EC 1.5.8.3: sarcosine dehydrogenase +EC 1.5.8.4: dimethylglycine dehydrogenase + +=== EC 1.5.98 With other, known, physiological acceptors === +EC 1.5.98.1: ethylenetetrahydromethanopterin dehydrogenase +EC 1.5.98.2: 5,10-methylenetetrahydromethanopterin reductase +EC 1.5.98.3: coenzyme F420:methanophenazine dehydrogenase + +=== EC 1.5.99 With unknown physiological acceptors === +EC 1.5.99.1: Now EC 1.5.8.3, sarcosine dehydrogenase +EC 1.5.99.2: Now EC 1.5.8.4, dimethylglycine dehydrogenase +EC 1.5.99.3: L-pipecolate dehydrogenase +EC 1.5.99.4: nicotine dehydrogenase +EC 1.5.99.5: methylglutamate dehydrogenase +EC 1.5.99.6: spermidine dehydrogenase +EC 1.5.99.7: Now EC 1.5.8.2, trimethylamine dehydrogenase +EC 1.5.99.8: Now EC 1.5.5.2, proline dehydrogenase +EC 1.5.99.9: transferred to EC 1.5.98.1, methylenetetrahydromethanopterin dehydrogenase +EC 1.5.99.10: Now EC 1.5.8.1, dimethylamine dehydrogenase +EC 1.5.99.11: transferred to EC 1.5.98.2, 5,10-methylenetetrahydromethanopterin reductase +EC 1.5.99.12: cytokinin dehydrogenase +EC 1.5.99.13: D-proline dehydrogenase +EC 1.5.99.14: 6-hydroxypseudooxynicotine dehydrogenase +EC 1.5.99.15: dihydromethanopterin reductase (acceptor) + +== EC 1.6 Acting on NADH or NADPH == + +=== EC 1.6.1 With NAD or NADP as acceptor === +EC 1.6.1.1: NAD(P)+ transhydrogenase (Si-specific) +EC 1.6.1.2: NAD(P)+ transhydrogenase (Re/Si-specific) + +=== EC 1.6.2 With a heme protein as acceptor === +EC 1.6.2.1: now EC 1.6.99.3 NADH dehydrogenase +EC 1.6.2.2: cytochrome-b5 reductase +EC 1.6.2.3: deleted +EC 1.6.2.4: NADPH—hemoprotein reductase +EC 1.6.2.5: NADPH—cytochrome-c2 reductase +EC 1.6.2.6: leghemoglobin reductase + +=== EC 1.6.3 With oxygen as acceptor === +EC 1.6.3.1: NAD(P)H oxidase (H2O2-forming) +EC 1.6.3.2: NAD(P)H oxidase (H2O-forming) +EC 1.6.3.3: NADH oxidase (H2O2-forming) +EC 1.6.3.4: NADH oxidase (H2O-forming) +EC 1.6.3.5: renalase + +=== EC 1.6.4 With a disulfide as acceptor (deleted sub-class) === +EC 1.6.4.1: now EC 1.8.1.6 cystine reductase +EC 1.6.4.2: now EC 1.8.1.7 glutathione-disulfide reductase +EC 1.6.4.3: now EC 1.8.1.4 dihydrolipoyl dehydrogenase +EC 1.6.4.4: now EC 1.8.1.8 protein-disulfide reductase +EC 1.6.4.5: now EC 1.8.1.9 thioredoxin-disulfide reductase +EC 1.6.4.6: now EC 1.8.1.10 CoA-glutathione reductase +EC 1.6.4.7: now EC 1.8.1.11 asparagusate reductase +EC 1.6.4.8: now EC 1.8.1.12 trypanothione-disulfide reductase +EC 1.6.4.9: now EC 1.8.1.13 bis-γ-glutamylcystine reductase +EC 1.6.4.10: now EC 1.8.1.14 CoA-disulfide reductase + +=== EC 1.6.5 With a quinone or similar compound as acceptor === +EC 1.6.5.1: deleted +EC 1.6.5.2: NAD(P)H dehydrogenase (quinone) +EC 1.6.5.3: now EC 7.1.1.2 NADH:ubiquinone reductase (H+-translocating) +EC 1.6.5.4: monodehydroascorbate reductase (NADH) +EC 1.6.5.5: NADPH:quinone reductase +EC 1.6.5.6: p-benzoquinone reductase (NADPH) +EC 1.6.5.7: 2-hydroxy-1,4-benzoquinone reductase +EC 1.6.5.8: Now EC 7.2.1.1, NADH:ubiquinone reductase (Na+-transporting) +EC 1.6.5.9: NADH:ubiquinone reductase (non-electrogenic) +EC 1.6.5.10: NADPH dehydrogenase (quinone) +EC 1.6.5.11: Identical to EC 1.6.5.9, NADH:quinone reductase (non-electrogenic) +EC 1.6.5.12: demethylphylloquinone reductase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-8.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-8.md new file mode 100644 index 000000000..9a35954e7 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-8.md @@ -0,0 +1,183 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 9/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.6.6 With a nitrogenous group as acceptor === +EC 1.6.6.1: Now EC 1.7.1.1, nitrate reductase (NADH) +EC 1.6.6.2: Now EC 1.7.1.2, nitrate reductase [NAD(P)H] +EC 1.6.6.3: Now EC 1.7.1.3, nitrate reductase (NADPH) +EC 1.6.6.4: Now EC 1.7.1.4, nitrite reductase [NAD(P)H] +EC 1.6.6.5: Now EC 1.7.2.1, nitrite reductase (NO-forming) +EC 1.6.6.6: Now EC 1.7.1.5, hyponitrite reductase +EC 1.6.6.7: Now EC 1.7.1.6, azobenzene reductase +EC 1.6.6.8: Now EC 1.7.1.7, GMP reductase +EC 1.6.6.9: Now known to be catalysed by EC 1.7.2.3, trimethylamine-N-oxide reductase +EC 1.6.6.10: Now EC 1.7.1.9, nitroquinoline-N-oxide reductase] +EC 1.6.6.11: Now EC 1.7.1.10, hydroxylamine reductase (NADH) +EC 1.6.6.12: Now EC 1.7.1.11, 4-(dimethylamino)phenylazoxybenzene reductase +EC 1.6.6.13: Now EC 1.7.1.12, N-hydroxy-2-acetamidofluorene reductase + +=== EC 1.6.7 With an iron–sulfur protein as acceptor (deleted sub-subclass) === +EC 1.6.7.1: now EC 1.18.1.2 ferredoxin—NADP+ reductase +EC 1.6.7.2: now EC 1.18.1.1 rubredoxin—NAD+ reductase +EC 1.6.7.3: now EC 1.18.1.3 ferredoxin—NAD+ reductase + +=== EC 1.6.8 With a flavin as acceptor (deleted sub-subclass) === +EC 1.6.8.1: Now EC 1.5.1.29 FMN reductase +EC 1.6.8.2: Now EC 1.5.1.30 flavin reductase + +=== EC 1.6.99 With unknown physiological acceptors === +EC 1.6.99.1: NADPH dehydrogenase +EC 1.6.99.2: Now EC 1.6.5.2, NAD(P)H dehydrogenase (quinone +EC 1.6.99.3: The activity is covered by EC 7.1.1.2, NADH:ubiquinone reductase (H+-translocating) +EC 1.6.99.4: Now EC 1.18.1.2, ferredoxin—NADP+ reductase +EC 1.6.99.5: Now EC 1.6.5.11, NADH dehydrogenase (quinone) +EC 1.6.99.6: Now EC 1.6.5.10, NADPH dehydrogenase (quinone) +EC 1.6.99.7: Now EC 1.5.1.34, 6,7-dihydropteridine reductase +EC 1.6.99.8: Deleted +EC 1.6.99.9: Now EC 1.16.1.4, cob(II)alamin reductase +EC 1.6.99.10: included in EC 1.5.1.34, 6,7-dihydropteridine reductase +EC 1.6.99.11: Deleted +EC 1.6.99.12: Now EC 1.16.1.6, cyanocobalamin reductase (cyanide-eliminating) +EC 1.6.99.13: Now EC 1.16.1.7, ferric-chelate reductase + +== EC 1.7 Acting on other nitrogenous compounds as donors == + +=== EC 1.7.1 With NAD+ or NADP+ as acceptor === +EC 1.7.1.1: nitrate reductase (NADH) +EC 1.7.1.2: nitrate reductase (NAD(P)H) +EC 1.7.1.3: nitrate reductase (NADPH) +EC 1.7.1.4: nitrite reductase (NAD(P)H) +EC 1.7.1.5: hyponitrite reductase +EC 1.7.1.6: azobenzene reductase +EC 1.7.1.7: GMP reductase +EC 1.7.1.8: deleted +EC 1.7.1.9: nitroquinoline-N-oxide reductase +EC 1.7.1.10: hydroxylamine reductase (NADH) +EC 1.7.1.11: 4-(dimethylamino)phenylazoxybenzene reductase +EC 1.7.1.12: N-hydroxy-2-acetamidofluorene reductase +EC 1.7.1.13: preQ1 synthase +EC 1.7.1.14: nitric oxide reductase (NAD(P), nitrous oxide-forming) +EC 1.7.1.15: nitrite reductase (NADH) +EC 1.7.1.16: nitrobenzene nitroreductase +EC 1.7.1.17: FMN-dependent NADH-azoreductase + +=== EC 1.7.2 With a cytochrome as acceptor === +EC 1.7.2.1: nitrite reductase (NO-forming) +EC 1.7.2.2: nitrite reductase (cytochrome; ammonia-forming) +EC 1.7.2.3: trimethylamine-N-oxide reductase +EC 1.7.2.4: nitrous-oxide reductase +EC 1.7.2.5: nitric oxide reductase (cytochrome c) +EC 1.7.2.6: hydroxylamine dehydrogenase +EC 1.7.2.7: hydrazine synthase +EC 1.7.2.8: hydrazine dehydrogenase + +=== EC 1.7.3 With oxygen as acceptor === +EC 1.7.3.1: nitroalkane oxidase +EC 1.7.3.2: acetylindoxyl oxidase +EC 1.7.3.3: factor-independent urate hydroxylase +EC 1.7.3.4: Now covered by EC 1.7.2.6, hydroxylamine dehydrogenase, and EC 1.7.3.6, hydroxylamine oxidase (cytochrome) +EC 1.7.3.5: 3-aci-nitropropanoate oxidase +EC 1.7.3.6: hydroxylamine oxidase (cytochrome) + +=== EC 1.7.5 With a quinone or similar compound as acceptor === +EC 1.7.5.1: nitrate reductase (quinone) +EC 1.7.5.2: nitric oxide reductase (menaquinol) + +=== EC 1.7.6 With a nitrogenous group as acceptor === +EC 1.7.6.1: nitrite dismutase + +=== EC 1.7.7 With an iron–sulfur protein as acceptor === +EC 1.7.7.1: ferredoxin—nitrite reductase +EC 1.7.7.2: ferredoxin—nitrate reductase + +=== EC 1.7.99 With other acceptors === +EC 1.7.99.1: hydroxylamine reductase +EC 1.7.99.2: deleted: reaction may have been due to the combined action of EC 1.7.99.6 nitrous-oxide reductase and EC 1.7.99.7 nitric-oxide reductase +EC 1.7.99.3: Now included with EC 1.7.2.1, nitrite reductase (NO-forming) +EC 1.7.99.4: Now EC 1.7.1.1, nitrate reductase (NADH), EC 1.7.1.2, nitrate reductase [NAD(P)H], EC 1.7.1.3, nitrate reductase (NADPH), EC 1.7.5.1, nitrate reductase (quinone), EC 1.7.7.2, nitrate reductase (ferredoxin) and EC 1.9.6.1, nitrate reductase (cytochrome) +EC 1.7.99.5: Now included with EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H] +EC 1.7.99.6: Now EC 1.7.2.4 nitrous-oxide reductase +EC 1.7.99.7: Now EC 1.7.2.5 nitric oxide reductase (cytochrome c) +EC 1.7.99.8: hydroxylamine oxidoreductase +EC 1.7.99.8: Now classified as EC 1.7.2.8, hydrazine dehydrogenase + +== EC 1.8 Acting on a sulfur group of donors == + +=== EC 1.8.1 With NAD+ or NADP+ as acceptor === +EC 1.8.1.1: deleted +EC 1.8.1.2: sulfite reductase (NADPH) +EC 1.8.1.3: deleted; reaction shown to be due to EC 1.14.13.8, flavin-containing monooxygenase +EC 1.8.1.4: dihydrolipoyl dehydrogenase +EC 1.8.1.5: 2-oxopropyl-CoM reductase (carboxylating) +EC 1.8.1.6: cystine reductase +EC 1.8.1.7: glutathione-disulfide reductase +EC 1.8.1.8: protein-disulfide reductase +EC 1.8.1.9: thioredoxin-disulfide reductase +EC 1.8.1.10: CoA-glutathione reductase +EC 1.8.1.11: asparagusate reductase +EC 1.8.1.12: trypanothione-disulfide reductase +EC 1.8.1.13: bis-γ-glutamylcystine reductase +EC 1.8.1.14: CoA-disulfide reductase +EC 1.8.1.15: mycothione reductase +EC 1.8.1.16: glutathione amide reductase +EC 1.8.1.17: dimethylsulfone reductase +EC 1.8.1.18: NAD(P)H sulfur oxidoreductase (CoA-dependent) +EC 1.8.1.19: sulfide dehydrogenase +EC 1.8.1.20: 4,4′-dithiodibutanoate disulfide reductase +EC 1.8.1.21: dissimilatory dimethyldisulfide reductase +EC 1.8.1.22: dissimilatory sulfite reductase + +=== EC 1.8.2 With a cytochrome as acceptor === +EC 1.8.2.1: sulfite dehydrogenase (cytochrome) +EC 1.8.2.2: thiosulfate dehydrogenase +EC 1.8.2.3: sulfide-cytochrome-c reductase (flavocytochrome c) +EC 1.8.2.4: dimethyl sulfide:cytochrome c2 reductase +EC 1.8.2.5: thiosulfate reductase (cytochrome) +EC 1.8.2.6: S-disulfanyl-L-cysteine oxidoreductase +EC 1.8.2.7: thiocyanate desulfurase + +=== EC 1.8.3 With oxygen as acceptor === +EC 1.8.3.1: sulfite oxidase +EC 1.8.3.2: thiol oxidase +EC 1.8.3.3: glutathione oxidase +EC 1.8.3.4: methanethiol oxidase +EC 1.8.3.5: prenylcysteine oxidase +EC 1.8.3.6: farnesylcysteine lyase +EC 1.8.3.7: formylglycine-generating enzyme + +=== EC 1.8.4 With a disulfide as acceptor === +EC 1.8.4.1: glutathione—homocystine transhydrogenase +EC 1.8.4.2: protein-disulfide reductase (glutathione) +EC 1.8.4.3: glutathione—CoA-glutathione transhydrogenase +EC 1.8.4.4: glutathione—cystine transhydrogenase +EC 1.8.4.5: Now EC 1.8.4.13, L-methionine (S)-S-oxide reductase and EC 1.8.4.14, L-methionine (R)-S-oxide reductase +EC 1.8.4.6: due to EC 1.8.4.11, peptide-methionine (S)-S-oxide reductase +EC 1.8.4.7: enzyme-thiol transhydrogenase (glutathione-disulfide) +EC 1.8.4.8: phosphoadenylyl-sulfate reductase (thioredoxin) +EC 1.8.4.9: adenylyl-sulfate reductase (glutathione) +EC 1.8.4.10: adenylyl-sulfate reductase (thioredoxin) +EC 1.8.4.11: peptide-methionine (S)-S-oxide reductase +EC 1.8.4.12: peptide-methionine (R)-S-oxide reductase +EC 1.8.4.13: L-methionine (S)-S-oxide reductase +EC 1.8.4.14: L-methionine (R)-S-oxide reductase +EC 1.8.4.15: protein dithiol oxidoreductase (disulfide-forming) +EC 1.8.4.16: thioredoxin:protein disulfide reductase + +=== EC 1.8.5 With a quinone or similar compound as acceptor === +EC 1.8.5.1: glutathione dehydrogenase (ascorbate) +EC 1.8.5.2: thiosulfate dehydrogenase (quinone) +EC 1.8.5.3: respiratory dimethylsulfoxide reductase +EC 1.8.5.4: bacterial sulfide:quinone reductase +EC 1.8.5.5: thiosulfate reductase (quinone) +EC 1.8.5.6: sulfite dehydrogenase (quinone) +EC 1.8.5.7: glutathionyl-hydroquinone reductase +EC 1.8.5.8: eukaryotic sulfide quinone oxidoreductase +EC 1.8.5.9: protein dithiol:quinone oxidoreductase DsbB +EC 1.8.5.10: DsrC-trisulfide reductase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-9.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-9.md new file mode 100644 index 000000000..b2cf64044 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)-9.md @@ -0,0 +1,158 @@ +--- +title: "List of EC numbers (EC 1)" +chunk: 10/18 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_1)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:04.950617+00:00" +instance: "kb-cron" +--- + +=== EC 1.8.6 With a nitrogenous group as acceptor (deleted sub-subclass) === +EC 1.8.6.1: Now included with EC 2.5.1.18 glutathione transferase + +=== EC 1.8.7 With an iron–sulfur protein as acceptor === +EC 1.8.7.1: assimilatory sulfite reductase (ferredoxin) +EC 1.8.7.2: ferredoxin:thioredoxin reductase +EC 1.8.7.3: ferredoxin:CoB-CoM heterodisulfide reductase + +=== EC 1.8.98 With other, known, acceptors === +EC 1.8.98.1: dihydromethanophenazine:CoB-CoM heterodisulfide reductase +EC 1.8.98.2: sulfiredoxin + +=== EC 1.8.99 With other acceptors === +EC 1.8.99.1: Now covered by EC 1.8.1.2, assimilatory sulfite reductase (NADPH) and EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin) +EC 1.8.99.2: adenylyl-sulfate reductase +EC 1.8.99.3: an in vitro artifact of EC 1.8.1.22, dissimilatory sulfite reductase +EC 1.8.99.4: Now EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin) +EC 1.8.99.5: Now EC 1.8.1.22, dissimilatory sulfite reductase + +== EC 1.9 Acting on a heme group of donors == + +=== EC 1.9.3 With oxygen as acceptor === +EC 1.9.3.1: Now EC 7.1.1.9, cytochrome-c oxidase +EC 1.9.3.2: Now included with EC 1.7.2.1, nitrite reductase (NO-forming) + +=== EC 1.9.6 With a nitrogenous group as acceptor === +EC 1.9.6.1: nitrate reductase (cytochrome) + +=== EC 1.9.98 With other, known, physiological acceptors === +EC 1.9.98.1: iron—cytochrome-c reductase + +=== EC 1.9.99 With other acceptors === +EC 1.9.99.1: Now EC 1.9.98.1, iron—cytochrome-c reductase + +== EC 1.10 Acting on diphenols and related substances as donors == + +=== EC 1.10.1 With NAD+ or NADP+ as acceptor === +EC 1.10.1.1: trans-acenaphthene-1,2-diol dehydrogenase + +=== EC 1.10.2 With a cytochrome as acceptor === +EC 1.10.2.1: The activity is covered by EC 7.2.1.3, ascorbate ferrireductase (transmembrane) +EC 1.10.2.2: Now EC 7.1.1.8, quinol—cytochrome-c reductase + +=== EC 1.10.3 With oxygen as acceptor === +EC 1.10.3.1: catechol oxidase +EC 1.10.3.2: laccase +EC 1.10.3.3: L-ascorbate oxidase +EC 1.10.3.4: o-aminophenol oxidase +EC 1.10.3.5: 3-hydroxyanthranilate oxidase +EC 1.10.3.6: rifamycin-B oxidase +EC 1.10.3.7: Now EC 1.21.3.4, sulochrin oxidase [(+)-bisdechlorogeodin-forming] +EC 1.10.3.8: Now EC 1.21.3.5, sulochrin oxidase [(-)-bisdechlorogeodin-forming] +EC 1.10.3.9: photosystem II +EC 1.10.3.10: Now EC 7.1.1.3, ubiquinol oxidase (H+-transporting) +EC 1.10.3.11: ubiquinol oxidase (non-electrogenic) +EC 1.10.3.12: Now EC 7.1.1.5, menaquinol oxidase (H+-transporting) +EC 1.10.3.13: Now EC 7.1.1.4, caldariellaquinol oxidase (H+-transporting) +EC 1.10.3.14: Now EC 7.1.1.7, ubiquinol oxidase (electrogenic, proton-motive force generating) +EC 1.10.3.15: grixazone synthase +EC 1.10.3.16: dihydrophenazinedicarboxylate synthase +EC 1.10.3.17: superoxide oxidase + +=== EC 1.10.5 With a quinone or related compound as acceptor === +EC 1.10.5.1: ribosyldihydronicotinamide dehydrogenase (quinone) + +=== EC 1.10.9 With a copper protein as acceptor === +EC 1.10.9.1: Now EC 7.1.1.6, plastoquinol—plastocyanin reductase + +=== EC 1.10.99 With unknown physiological acceptors === +EC 1.10.99.1: Now EC 1.10.9.1 plastoquinol—plastocyanin reductase +EC 1.10.99.2: Now EC 1.10.5.1 ribosyldihydronicotinamide dehydrogenase (quinone) +EC 1.10.99.3: Now EC 1.23.5.1 violaxanthin de-epoxidase + +== EC 1.11 Acting on a peroxide as acceptor == + +=== EC 1.11.1 Peroxidases === +EC 1.11.1.1: NADH peroxidase +EC 1.11.1.2: NADPH peroxidase +EC 1.11.1.3: fatty-acid peroxidase +EC 1.11.1.4: Now EC 1.13.11.11 EC 1.13.11.11 tryptophan 2,3-dioxygenase +EC 1.11.1.5: cytochrome-c peroxidase +EC 1.11.1.6: catalase +EC 1.11.1.7: peroxidase +EC 1.11.1.8: iodide peroxidase +EC 1.11.1.9: glutathione peroxidase +EC 1.11.1.10: chloride peroxidase +EC 1.11.1.11: L-ascorbate peroxidase +EC 1.11.1.12: phospholipid-hydroperoxide glutathione peroxidase +EC 1.11.1.13: manganese peroxidase +EC 1.11.1.14: lignin peroxidase +EC 1.11.1.15: Now described by EC 1.11.1.24, thioredoxin-dependent peroxiredoxin; EC 1.11.1.25, glutaredoxin-dependent peroxiredoxin; EC 1.11.1.26, NADH-dependent peroxiredoxin; EC 1.11.1.27, glutathione-dependent peroxiredoxin; EC 1.11.1.28, lipoyl-dependent peroxiredoxin; and EC 1.11.1.29, mycoredoxin-dependent peroxiredoxin +EC 1.11.1.16: versatile peroxidase +EC 1.11.1.17: glutathione amide-dependent peroxidase +EC 1.11.1.18: bromide peroxidase +EC 1.11.1.19: dye decolorizing peroxidase +EC 1.11.1.20: prostamide/prostaglandin F2α synthase +EC 1.11.1.21: catalase-peroxidase +EC 1.11.1.22: hydroperoxy fatty acid reductase +EC 1.11.1.23: (S)-2-hydroxypropylphosphonic acid epoxidase +EC 1.11.1.24: thioredoxin-dependent peroxiredoxin +EC 1.11.1.25: glutaredoxin-dependent peroxiredoxin +EC 1.11.1.26: NADH-dependent peroxiredoxin +EC 1.11.1.27: glutathione-dependent peroxiredoxin +EC 1.11.1.28: lipoyl-dependent peroxiredoxin +EC 1.11.1.29: mycoredoxin-dependent peroxiredoxin + +=== EC 1.11.2 Peroxygenase === +EC 1.11.2.1: unspecific peroxygenase +EC 1.11.2.2: myeloperoxidase +EC 1.11.2.3: plant seed peroxygenase +EC 1.11.2.4: fatty-acid peroxygenase +EC 1.11.2.5: 3-methyl-L-tyrosine peroxygenase +EC 1.11.2.6: L-tyrosine peroxygenase + +== EC 1.12 Acting on hydrogen as donor == + +=== EC 1.12.1 With NAD+ or NADP+ as acceptor === +EC 1.12.1.1: Now EC 1.12.7.2, ferredoxin hydrogenase +EC 1.12.1.2: hydrogen dehydrogenase +EC 1.12.1.3: hydrogen dehydrogenase (NADP+) +EC 1.12.1.4: hydrogenase (NAD+, ferredoxin) +EC 1.12.1.5: hydrogen dehydrogenase [NAD(P)+] + +=== EC 1.12.2 With a cytochrome as acceptor === +EC 1.12.2.1: cytochrome-c3 hydrogenase + +=== EC 1.12.5 With a quinone or similar compound as acceptor === +EC 1.12.5.1: hydrogen:quinone oxidoreductase + +=== EC 1.12.7 With an iron–sulfur protein as acceptor === +EC 1.12.7.1: Now EC 1.12.7.2, ferredoxin hydrogenase +EC 1.12.7.2: ferredoxin hydrogenase + +=== EC 1.12.98 With other known acceptors === +EC 1.12.98.1: coenzyme F420 hydrogenase +EC 1.12.98.2: 5,10-methenyltetrahydromethanopterin hydrogenase +EC 1.12.98.3: Methanosarcina-phenazine hydrogenase +EC 1.12.98.4: Sulfhydrogenase + +=== EC 1.12.99 With unknown physiological acceptors === +EC 1.12.99.1: Now EC 1.12.98.1, coenzyme F420 hydrogenase +EC 1.12.99.2: Now shown to be two enzymes, EC 1.12.98.3, Methanosarcina-phenazine hydrogenase and EC 1.8.98.1, CoB—CoM heterodisulfide reductase +EC 1.12.99.3: Now EC 1.12.5.1, hydrogen:quinone oxidoreductase +EC 1.12.99.4: Now EC 1.12.98.2, 5,10-methenyltetrahydromethanopterin hydrogenase +EC 1.12.99.5: Identical to EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase +EC 1.12.99.6: hydrogenase (acceptor) + +== EC 1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases) == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-0.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-0.md new file mode 100644 index 000000000..7cab3d8a4 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-0.md @@ -0,0 +1,13 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 1/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +This list contains a list of EC numbers for the second group, EC 2, transferases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. + +== EC 2.1: Transferring One-Carbon Groups == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-1.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-1.md new file mode 100644 index 000000000..f175206ea --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-1.md @@ -0,0 +1,369 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 2/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.1.1: Methyltransferases === +EC 2.1.1.1: nicotinamide N-methyltransferase +EC 2.1.1.2: guanidinoacetate N-methyltransferase +EC 2.1.1.3: thetin—homocysteine S-methyltransferase +EC 2.1.1.4: acetylserotonin O-methyltransferase +EC 2.1.1.5: betaine—homocysteine S-methyltransferase +EC 2.1.1.6: catechol O-methyltransferase +EC 2.1.1.7: nicotinate N-methyltransferase +EC 2.1.1.8: histamine N-methyltransferase +EC 2.1.1.9: thiol S-methyltransferase +EC 2.1.1.10: homocysteine S-methyltransferase +EC 2.1.1.11: magnesium protoporphyrin IX methyltransferase +EC 2.1.1.12: methionine S-methyltransferase +EC 2.1.1.13: methionine synthase +EC 2.1.1.14: 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase +EC 2.1.1.15: fatty-acid O-methyltransferase +EC 2.1.1.16: methylene-fatty-acyl-phospholipid synthase +EC 2.1.1.17: phosphatidylethanolamine N-methyltransferase +EC 2.1.1.18: polysaccharide O-methyltransferase +EC 2.1.1.19: trimethylsulfonium—tetrahydrofolate N-methyltransferase +EC 2.1.1.20: glycine N-methyltransferase +EC 2.1.1.21: methylamine—glutamate N-methyltransferase +EC 2.1.1.22: carnosine N-methyltransferase +EC 2.1.1.23: now covered by EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126 +EC 2.1.1.24: now covered by EC 2.1.1.77, EC 2.1.1.80 and EC 2.1.1.100 +EC 2.1.1.25: phenol O-methyltransferase +EC 2.1.1.26: iodophenol O-methyltransferase +EC 2.1.1.27: tyramine N-methyltransferase +EC 2.1.1.28: phenylethanolamine N-methyltransferase +EC 2.1.1.29: Now covered by EC 2.1.1.202, EC 2.1.1.203 and EC .1.1.204 +EC 2.1.1.30: tRNA (purine-2- or -6-)-methyltransferase: Reactions previously described are due to EC 2.1.1.32 +EC 2.1.1.31: Now covered by EC 2.1.1.221 and EC 2.1.1.228 +EC 2.1.1.32: Now covered by EC 2.1.1.213, EC 2.1.1.214, EC 2.1.1.215 and EC 2.1.1.216 +EC 2.1.1.33: tRNA (guanine46-N7)-methyltransferase +EC 2.1.1.34: tRNA (guanosine18-2′-O)-methyltransferase +EC 2.1.1.35: tRNA (uracil54-C5)-methyltransferase +EC 2.1.1.36: Now covered by EC 2.1.1.217, EC 2.1.1.218, EC 2.1.1.219, EC 2.1.1.220 +EC 2.1.1.37: DNA (cytosine-5-)-methyltransferase +EC 2.1.1.38: O-demethylpuromycin O-methyltransferase +EC 2.1.1.39: inositol 3-methyltransferase +EC 2.1.1.40: inositol 1-methyltransferase +EC 2.1.1.41: sterol 24-C-methyltransferase +EC 2.1.1.42: flavone 3′-O-methyltransferase +EC 2.1.1.43: Now described by EC 2.1.1.354, EC 2.1.1.355, EC 2.1.1.356, EC 2.1.1.357, EC 2.1.1.358, EC 2.1.1.359, EC 2.1.1.360, EC 2.1.1.361 and EC 2.1.1.362 +EC 2.1.1.44: L-histidine Nα-methyltransferase +EC 2.1.1.45: thymidylate synthase +EC 2.1.1.46: isoflavone 4′-O-methyltransferase +EC 2.1.1.47: indolepyruvate C-methyltransferase +EC 2.1.1.48: Now covered by EC 2.1.1.181, EC 2.1.1.182, EC 2.1.1.183 and EC 2.1.1.184 +EC 2.1.1.49: amine N-methyltransferase +EC 2.1.1.50: loganate O-methyltransferase +EC 2.1.1.51: Now covered by EC 2.1.1.187 and EC 2.1.1.188 +EC 2.1.1.52: Now covered by EC 2.1.1.171, EC 2.1.1.172, EC 2.1.1.173 and EC 2.1.1.174 +EC 2.1.1.53: putrescine N-methyltransferase +EC 2.1.1.54: deoxycytidylate C-methyltransferase +EC 2.1.1.55: tRNA (adenine-N6-)-methyltransferase +EC 2.1.1.56: mRNA (guanine-N7)-methyltransferase +EC 2.1.1.57: methyltransferase cap1 +EC 2.1.1.58: deleted, included in EC 2.1.1.57 +EC 2.1.1.59: [cytochrome c]-lysine N-methyltransferase|[cytochrome c]-lysine N-methyltransferase +EC 2.1.1.60: calmodulin-lysine N-methyltransferase +EC 2.1.1.61: tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase +EC 2.1.1.62: mRNA (2′-O-methyladenosine-N6-)-methyltransferase +EC 2.1.1.63: methylated-DNA—[protein]-cysteine S-methyltransferase +EC 2.1.1.64: 3-demethylubiquinol 3-O-methyltransferase +EC 2.1.1.65: licodione 2′-O-methyltransferase +EC 2.1.1.66: Now covered by EC 2.1.1.230 +EC 2.1.1.67: thiopurine S-methyltransferase +EC 2.1.1.68: caffeate O-methyltransferase +EC 2.1.1.69: 5-hydroxyfuranocoumarin 5-O-methyltransferase +EC 2.1.1.70: 8-hydroxyfuranocoumarin 8-O-methyltransferase +EC 2.1.1.71: phosphatidyl-N-methylethanolamine N-methyltransferase +EC 2.1.1.72: site-specific DNA-methyltransferase (adenine-specific) +EC 2.1.1.73: deleted: reaction is that of EC 2.1.1.37, DNA (cytosine-5-)-methyltransferase +EC 2.1.1.74: methylenetetrahydrofolate—tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing] +EC 2.1.1.75: apigenin 4′-O-methyltransferase +EC 2.1.1.76: quercetin 3-O-methyltransferase +EC 2.1.1.77: protein-L-isoaspartate(D-aspartate) O-methyltransferase +EC 2.1.1.78: isoorientin 3′-O-methyltransferase +EC 2.1.1.79: cyclopropane-fatty-acyl-phospholipid synthase +EC 2.1.1.80: protein-glutamate O-methyltransferase +EC 2.1.1.81: deleted, included in EC 2.1.1.49 +EC 2.1.1.82: 3-methylquercetin 7-O-methyltransferase +EC 2.1.1.83: 3,7-dimethylquercetin 4′-O-methyltransferase +EC 2.1.1.84: methylquercetagetin 6-O-methyltransferase +EC 2.1.1.85: protein-histidine N-methyltransferase +EC 2.1.1.86: Now covered by EC 7.2.1.4 +EC 2.1.1.87: pyridine N-methyltransferase +EC 2.1.1.88: 8-hydroxyquercetin 8-O-methyltransferase +EC 2.1.1.89: tetrahydrocolumbamine 2-O-methyltransferase +EC 2.1.1.90: methanol—5-hydroxybenzimidazolylcobamide Co-methyltransferase +EC 2.1.1.91: isobutyraldoxime O-methyltransferase +EC 2.1.1.92: Now included with EC 2.1.1.69 +EC 2.1.1.93: is identical to EC 2.1.1.70, 8-hydroxyfuranocoumarin 8-O-methyltransferase +EC 2.1.1.94: tabersonine 16-O-methyltransferase +EC 2.1.1.95: tocopherol C-methyltransferase +EC 2.1.1.96: thioether S-methyltransferase +EC 2.1.1.97: 3-hydroxyanthranilate 4-C-methyltransferase +EC 2.1.1.98: diphthine synthase +EC 2.1.1.99: 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase +EC 2.1.1.100: protein-S-isoprenylcysteine O-methyltransferase +EC 2.1.1.101: macrocin O-methyltransferase +EC 2.1.1.102: demethylmacrocin O-methyltransferase +EC 2.1.1.103: phosphoethanolamine N-methyltransferase +EC 2.1.1.104: caffeoyl-CoA O-methyltransferase +EC 2.1.1.105: N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase +EC 2.1.1.106: tryptophan 2-C-methyltransferase +EC 2.1.1.107: uroporphyrinogen-III C-methyltransferase +EC 2.1.1.108: 6-hydroxymellein O-methyltransferase +EC 2.1.1.109: demethylsterigmatocystin 6-O-methyltransferase +EC 2.1.1.110: sterigmatocystin 8-O-methyltransferase +EC 2.1.1.111: anthranilate N-methyltransferase +EC 2.1.1.112: glucuronoxylan 4-O-methyltransferase +EC 2.1.1.113: site-specific DNA-methyltransferase (cytosine-N4-specific) +EC 2.1.1.114: polyprenyldihydroxybenzoate methyltransferase +EC 2.1.1.115: (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase +EC 2.1.1.116: 3′-hydroxy-N-methyl-(S)-coclaurine 4′-O-methyltransferase +EC 2.1.1.117: (S)-scoulerine 9-O-methyltransferase +EC 2.1.1.118: columbamine O-methyltransferase +EC 2.1.1.119: 10-hydroxydihydrosanguinarine 10-O-methyltransferase +EC 2.1.1.120: 12-hydroxydihydrochelirubine 12-O-methyltransferase +EC 2.1.1.121: 6-O-methylnorlaudanosoline 5′-O-methyltransferase +EC 2.1.1.122: (S)-tetrahydroprotoberberine N-methyltransferase +EC 2.1.1.123: [cytochrome-c]-methionine S-methyltransferase +EC 2.1.1.124: Now covered by EC 2.1.1.319, EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322 +EC 2.1.1.125: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 +EC 2.1.1.126: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 +EC 2.1.1.127: [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase +EC 2.1.1.128: (RS)-norcoclaurine 6-O-methyltransferase +EC 2.1.1.129: inositol 4-methyltransferase +EC 2.1.1.130: precorrin-2 C20-methyltransferase +EC 2.1.1.131: precorrin-2 C17-methyltransferase +EC 2.1.1.132: precorrin-6B C5,15-methyltransferase (decarboxylating) +EC 2.1.1.133: precorrin-4 C11-methyltransferase +EC 2.1.1.134: now with EC 2.1.1.129 +EC 2.1.1.135: now EC 1.16.1.8 +EC 2.1.1.136: chlorophenol O-methyltransferase +EC 2.1.1.137: arsenite methyltransferase +EC 2.1.1.138: deleted: Reaction due to EC 2.1.1.137 +EC 2.1.1.139: 3′-demethylstaurosporine O-methyltransferase +EC 2.1.1.140: (S)-coclaurine-N-methyltransferase +EC 2.1.1.141: jasmonate O-methyltransferase +EC 2.1.1.142: cycloartenol 24-C-methyltransferase +EC 2.1.1.143: 24-methylenesterol C-methyltransferase +EC 2.1.1.144: trans-aconitate 2-methyltransferase +EC 2.1.1.145: trans-aconitate 3-methyltransferase +EC 2.1.1.146: (iso)eugenol O-methyltransferase +EC 2.1.1.147: corydaline synthase +EC 2.1.1.148: thymidylate synthase (FAD) +EC 2.1.1.149: Now covered by EC 2.1.1.267, flavonoid 3′,5′-methyltransferase +EC 2.1.1.150: isoflavone 7-O-methyltransferase +EC 2.1.1.151: cobalt-factor II C20-methyltransferase +EC 2.1.1.152: precorrin-6A synthase (deacetylating) +EC 2.1.1.153: vitexin 2′′-O-rhamnoside 7-O-methyltransferase +EC 2.1.1.154: isoliquiritigenin 2′-O-methyltransferase +EC 2.1.1.155: kaempferol 4′-O-methyltransferase +EC 2.1.1.156: glycine/sarcosine N-methyltransferase +EC 2.1.1.157: sarcosine/dimethylglycine N-methyltransferase +EC 2.1.1.158: 7-methylxanthosine synthase +EC 2.1.1.159: theobromine synthase +EC 2.1.1.160: caffeine synthase +EC 2.1.1.161: dimethylglycine N-methyltransferase +EC 2.1.1.162: glycine/sarcosine/dimethylglycine N-methyltransferase +EC 2.1.1.163: demethylmenaquinone methyltransferase +EC 2.1.1.164: demethylrebeccamycin-D-glucose O-methyltransferase +EC 2.1.1.165: methyl halide transferase +EC 2.1.1.166: 23S rRNA (uridine2552-2′-O)-methyltransferase +EC 2.1.1.167: 27S pre-rRNA (guanosine2922-2′-O)-methyltransferase +EC 2.1.1.168: 21S rRNA (uridine2791-2′-O)-methyltransferase +EC 2.1.1.169: tricetin 3′,4′,5′-O-trimethyltransferase +EC 2.1.1.170: 16S rRNA (guanine527-N7)-methyltransferase +EC 2.1.1.171: 16S rRNA (guanine966-N2)-methyltransferase +EC 2.1.1.172: 16S rRNA (guanine1207-N2))-methyltransferase +EC 2.1.1.173: 23S rRNA (guanine2445-N2)-methyltransferase +EC 2.1.1.174: 23S rRNA (guanine1835-N2)-methyltransferase +EC 2.1.1.175: tricin synthase +EC 2.1.1.176: 16S rRNA (cytosine967-C5)-methyltransferase +EC 2.1.1.177: 23S rRNA (pseudouridine1915-N3)-methyltransferase +EC 2.1.1.178: 16S rRNA (cytosine1407-C5)-methyltransferase +EC 2.1.1.179: 16S rRNA (guanine1405-N7)-methyltransferase +EC 2.1.1.180: 16S rRNA (adenine1408-N1)-methyltransferase +EC 2.1.1.181: 23S rRNA (adenine1618-N6)-methyltransferase +EC 2.1.1.182: 16S rRNA (adenine1518-N6/adenineadenine1519-N6)-dimethyltransferase +EC 2.1.1.183: 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase +EC 2.1.1.184: 23S rRNA (adenine2085-N6)-dimethyltransferase +EC 2.1.1.185: 23S rRNA (guanosine2251-2′-O)-methyltransferase +EC 2.1.1.186: 23S rRNA (cytidine2498-2′-O)-methyltransferase +EC 2.1.1.187: 23S rRNA (guanine745-N1)-methyltransferase +EC 2.1.1.188: 23S rRNA (guanine748-N1)-methyltransferase +EC 2.1.1.189: 23S rRNA (uracil747-C5)-methyltransferase +EC 2.1.1.190: 23S rRNA (uracil1939-C5)-methyltransferase +EC 2.1.1.191: 23S rRNA (cytosine1962-C5)-methyltransferase +EC 2.1.1.192: 23S rRNA (adenine2503-C2)-methyltransferase +EC 2.1.1.193: 16S rRNA (uracil1498-N3)-methyltransferase +EC 2.1.1.194: [[A mixture of EC 2.1.1.192 and EC 2.1.1.224]] +EC 2.1.1.195: cobalt-precorrin-5B (C1)-methyltransferase +EC 2.1.1.196: cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) +EC 2.1.1.197: malonyl-[acyl-carrier protein] O-methyltransferase +EC 2.1.1.198: 16S rRNA (cytidine1402-2′-O)-methyltransferase +EC 2.1.1.199: 16S rRNA (cytosine1402-N4)-methyltransferase +EC 2.1.1.200: tRNA (cytidine32/uridine32-2′-O)-methyltransferase +EC 2.1.1.201: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase +EC 2.1.1.202: multisite-specific tRNA:(cytosine-C5)-methyltransferase +EC 2.1.1.203: tRNA (cytosine34-C5)-methyltransferase +EC 2.1.1.204: tRNA (cytosine38-C5)-methyltransferase +EC 2.1.1.205: tRNA (cytidine32/guanosine34-2′-O)-methyltransferase +EC 2.1.1.206: tRNA (cytidine56-2′-O)-methyltransferase +EC 2.1.1.207: tRNA (cytidine34-2′-O)-methyltransferase +EC 2.1.1.208: 23S rRNA (uridine2479-2′-O)-methyltransferase +EC 2.1.1.209: 23S rRNA (guanine2535-N1)-methyltransferase +EC 2.1.1.210: demethylspheroidene O-methyltransferase +EC 2.1.1.211: tRNASer(uridine44-2′-O)-methyltransferase +EC 2.1.1.212: 2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase +EC 2.1.1.213: tRNA (guanine110-N2)-dimethyltransferase +EC 2.1.1.214: tRNA (guanine10-N2)-methyltransferase +EC 2.1.1.215: tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase +EC 2.1.1.216: tRNA (guanine26-N2)-dimethyltransferase +EC 2.1.1.217: tRNA (adenine22-N1)-methyltransferase +EC 2.1.1.218: tRNA (adenine9-N1)-methyltransferase +EC 2.1.1.219: tRNA (adenine57-N1/adenine58-N1)-methyltransferase +EC 2.1.1.220: tRNA (adenine58-N1)-methyltransferase +EC 2.1.1.221: tRNA (guanine9-N1)-methyltransferase +EC 2.1.1.222: 2-polyprenyl-6-hydroxyphenyl methylase +EC 2.1.1.223: tRNA1Val (adenine937-N6)-methyltransferase +EC 2.1.1.224: 23S rRNA (adenine2503-C8)-methyltransferase +EC 2.1.1.225: tRNA:m4X modification enzyme +EC 2.1.1.226: 23S rRNA (cytidine1920-2′-O)-methyltransferase +EC 2.1.1.227: 16S rRNA (cytidine1409-2′-O)-methyltransferase +EC 2.1.1.228: tRNA (guanine37-N1)-methyltransferase +EC 2.1.1.229: tRNA (carboxymethyluridine34-5-O)-methyltransferase +EC 2.1.1.230: 23S rRNA (adenosine1067-2′-O)-methyltransferase +EC 2.1.1.231: flavonoid 4′-O-methyltransferase +EC 2.1.1.232: naringenin 7-O-methyltransferase +EC 2.1.1.233: [phosphatase 2A protein]-leucine-carboxy methyltransferase +EC 2.1.1.234: dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose N,N-dimethyltransferase +EC 2.1.1.235: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose N,N-dimethyltransferase +EC 2.1.1.236: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose N,N-dimethyltransferase +EC 2.1.1.237: mycinamicin III 3′′-O-methyltransferase +EC 2.1.1.238: mycinamicin VI 2′′-O-methyltransferaseD +EC 2.1.1.239: [L-olivosyl-oleandolide 3-O-methyltransferase +EC 2.1.1.240: trans-resveratrol di-O-methyltransferase +EC 2.1.1.241: 2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase +EC 2.1.1.242: 16S rRNA (guanine1516-N2)-methyltransferase +EC 2.1.1.243: 2-ketoarginine methyltransferase +EC 2.1.1.244: protein N-terminal methyltransferase +EC 2.1.1.245: 5-methyltetrahydrosarcinapterin—corrinoid/iron-sulfur protein Co-methyltransferase +EC 2.1.1.246: [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase +EC 2.1.1.247: [methyl-Co(III) methylamine-specific corrinoid protein—coenzyme M methyltransferase +EC 2.1.1.248: methylamine—corrinoid protein Co-methyltransferase +EC 2.1.1.249: dimethylamine—corrinoid protein Co-methyltransferase +EC 2.1.1.250: trimethylamine—corrinoid protein Co-methyltransferase +EC 2.1.1.251: methylated-thiol—coenzyme M methyltransferase +EC 2.1.1.252: tetramethylammonium—corrinoid protein Co-methyltransferase +EC 2.1.1.253: [methyl-Co(III) tetramethylammonium-specific corrinoid protein]—coenzyme M methyltransferase +EC 2.1.1.254: erythromycin 3′′-O-methyltransferase +EC 2.1.1.255: geranyl diphosphate 2-C-methyltransferase +EC 2.1.1.256: tRNA (guanine6-N6-methyltransferase) +EC 2.1.1.257: tRNA (pseudouridine54-N1)-methyltransferase +EC 2.1.1.258: 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase +EC 2.1.1.259: [fructose-bisphosphate aldolase]-lysine N-methyltransferase +EC 2.1.1.260: rRNA small subunit pseudouridine methyltransferase Nep1 +EC 2.1.1.261: 4-dimethylallyltryptophan N-methyltransferase +EC 2.1.1.262: squalene methyltransferase +EC 2.1.1.263: botryococcene C-methyltransferase +EC 2.1.1.264: 23S rRNA (guanine2069-N7)-methyltransferase +EC 2.1.1.265: tellurite methyltransferase +EC 2.1.1.266: 23S rRNA (adenine2030-N6)-methyltransferase +EC 2.1.1.267: flavonoid 3′,5′-methyltransferase +EC 2.1.1.268: tRNAThr (cytosine32-N3)-methyltransferase +EC 2.1.1.269: dimethylsulfoniopropionate demethylase +EC 2.1.1.270: (+)-6a-hydroxymaackiain 3-O-methyltransferase +EC 2.1.1.271: cobalt-precorrin-4 methyltransferase +EC 2.1.1.272: cobalt-factor III methyltransferase +EC 2.1.1.273: benzoate O-methyltransferase +EC 2.1.1.274: salicylate 1-O-methyltransferase +EC 2.1.1.275: gibberellin A9 O-methyltransferase +EC 2.1.1.276: gibberellin A4 carboxyl methyltransferase +EC 2.1.1.277: anthranilate O-methyltransferase +EC 2.1.1.278: indole-3-acetate O-methyltransferase +EC 2.1.1.279: trans-anol O-methyltransferase +EC 2.1.1.280: selenocysteine Se-methyltransferase +EC 2.1.1.281: phenylpyruvate C3-methyltransferase +EC 2.1.1.282: tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase +EC 2.1.1.283: emodin O-methyltransferase +EC 2.1.1.284: 8-demethylnovobiocic acid C8-methyltransferase +EC 2.1.1.285: demethyldecarbamoylnovobiocin O-methyltransferase +EC 2.1.1.286: 25S rRNA (adenine2142-N1)-methyltransferase +EC 2.1.1.287: 25S rRNA (adenine645-N1)-methyltransferase +EC 2.1.1.288: aklanonic acid methyltransferase +EC 2.1.1.289: cobalt-precorrin-7 (C5)-methyltransferase +EC 2.1.1.290: tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase +EC 2.1.1.291: (R,S)-reticuline 7-O-methyltransferase +EC 2.1.1.292: carminomycin 4-O-methyltransferase +EC 2.1.1.293: 6-hydroxytryprostatin B O-methyltransferase +EC 2.1.1.294: 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase +EC 2.1.1.295: 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase +EC 2.1.1.296: methyltransferase cap2 +EC 2.1.1.297: peptide chain release factor N5-glutamine methyltransferase +EC 2.1.1.298: ribosomal protein L3 N5-glutamine methyltransferase +EC 2.1.1.299: protein N-terminal monomethyltransferase +EC 2.1.1.300: pavine N-methyltransferase +EC 2.1.1.301: cypemycin N-terminal methyltransferase +EC 2.1.1.302: 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase +EC 2.1.1.303: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase +EC 2.1.1.304: L-tyrosine C3-methyltransferase +EC 2.1.1.305: 8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2′-O-methyltransferase +EC 2.1.1.306: 8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3′-O-methyltransferase +EC 2.1.1.307: 8-demethyl-8-(2,3-dimethoxy-α-L-rhamnosyl)tetracenomycin-C 4′-O-methyltransferase +EC 2.1.1.308: cytidylyl-2-hydroxyethylphosphonate methyltransferase +EC 2.1.1.309: 18S rRNA (guanine1575-N7)-methyltransferase +EC 2.1.1.310: 25S rRNA (cytosine2870-C5)-methyltransferase +EC 2.1.1.311: 25S rRNA (cytosine2278-C5)-methyltransferase +EC 2.1.1.312: 25S rRNA (uracil2843-N3)-methyltransferase +EC 2.1.1.313: 25S rRNA (uracil2634-N3)-methyltransferase +EC 2.1.1.314: diphthine methyl ester synthase +EC 2.1.1.315: 27-O-demethylrifamycin SV methyltransferase +EC 2.1.1.316: mitomycin 6-O-methyltransferase +EC 2.1.1.317: sphingolipid C9-methyltransferase +EC 2.1.1.318: [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase +EC 2.1.1.319: type I protein arginine methyltransferase +EC 2.1.1.320: type II protein arginine methyltransferase +EC 2.1.1.321: type III protein arginine methyltransferase +EC 2.1.1.322: type IV protein arginine methyltransferase +EC 2.1.1.323: (–)-pluviatolide 4-O-methyltransferase +EC 2.1.1.324: dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase +EC 2.1.1.325: juvenile hormone-III synthase +EC 2.1.1.326: N-acetyldemethylphosphinothricin P-methyltransferase +EC 2.1.1.327: phenazine-1-carboxylate N-methyltransferase +EC 2.1.1.328: N-demethylindolmycin N-methyltransferase +EC 2.1.1.329: demethylphylloquinol methyltransferase +EC 2.1.1.330: 5′-demethylyatein 5′-O-methyltransferase +EC 2.1.1.331: bacteriochlorophyllide d C-121-methyltransferase +EC 2.1.1.332: bacteriochlorophyllide d C-82-methyltransferase +EC 2.1.1.333: bacteriochlorophyllide d C-20 methyltransferase +EC 2.1.1.334: methanethiol S-methyltransferase +EC 2.1.1.335: 4-amino-anhydrotetracycline N4-methyltransferase +EC 2.1.1.336: norbelladine O-methyltransferase +EC 2.1.1.337: reticuline N-methyltransferase +EC 2.1.1.338: desmethylxanthohumol 6′-O-methyltransferase +EC 2.1.1.339: xanthohumol 4-O-methyltransferase +EC 2.1.1.340: 3-aminomethylindole N'-methyltransferase +EC 2.1.1.341: vanillate/3-O-methylgallate O-demethylase +EC 2.1.1.342: anaerobilin synthase +EC 2.1.1.343: 8-amino-8-demethylriboflavin N,N-dimethyltransferase +EC 2.1.1.344: ornithine lipid N-methyltransferase +EC 2.1.1.345: psilocybin synthase +EC 2.1.1.346: U6 snRNA m6A methyltransferase +EC 2.1.1.347: (+)-O-methylkolavelool synthase +EC 2.1.1.348: mRNA m6A methyltransferase +EC 2.1.1.349: toxoflavin synthase +EC 2.1.1.350: menaquinone C8-methyltransferase +EC 2.1.1.351: nocamycin O-methyltransferase +EC 2.1.1.352: 3-O-acetyl-4′-O-demethylpapaveroxine 4′-O-methyltransferase +EC 2.1.1.353: demethylluteothin O-methyltransferase +EC 2.1.1.354: [histone H3]-lysine4 N-trimethyltransferase +EC 2.1.1.355: [histone H3]-lysine9 N-trimethyltransferase +EC 2.1.1.356: [histone H3]-lysine27 N-trimethyltransferase +EC 2.1.1.357: [histone H3]-lysine36 N-dimethyltransferase +EC 2.1.1.358: [histone H3]-dimethyl-L-lysine36 N-methyltransferase. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-10.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-10.md new file mode 100644 index 000000000..25595f939 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-10.md @@ -0,0 +1,144 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 11/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.6.1: Transaminases === +EC 2.6.1.1: aspartate transaminase +EC 2.6.1.2: alanine transaminase +EC 2.6.1.3: cysteine transaminase +EC 2.6.1.4: glycine transaminase +EC 2.6.1.5: tyrosine transaminase +EC 2.6.1.6: leucine transaminase +EC 2.6.1.7: kynurenine—oxoglutarate transaminase +EC 2.6.1.8: 2,5-diaminovalerate transaminase +EC 2.6.1.9: histidinol-phosphate transaminase +EC 2.6.1.10: deleted, included with EC 2.6.1.21, D-amino-acid transaminase +EC 2.6.1.11: acetylornithine transaminase +EC 2.6.1.12: alanine—oxo-acid transaminase +EC 2.6.1.13: ornithine aminotransferase +EC 2.6.1.14: asparagine—oxo-acid transaminase +EC 2.6.1.15: glutamine—pyruvate transaminase +EC 2.6.1.16: glutamine—fructose-6-phosphate transaminase (isomerizing) +EC 2.6.1.17: succinyldiaminopimelate transaminase +EC 2.6.1.18: β-alanine—pyruvate transaminase +EC 2.6.1.19: 4-aminobutyrate transaminase +EC 2.6.1.20: deleted +EC 2.6.1.21: D-amino-acid transaminase +EC 2.6.1.22: (S)-3-amino-2-methylpropionate transaminase +EC 2.6.1.23: 4-hydroxyglutamate transaminase +EC 2.6.1.24: diiodotyrosine transaminase +EC 2.6.1.25: deleted, Now included with EC 2.6.1.24 diiodotyrosine transaminase +EC 2.6.1.26: thyroid-hormone transaminase +EC 2.6.1.27: tryptophan transaminase +EC 2.6.1.28: tryptophan—phenylpyruvate transaminase +EC 2.6.1.29: diamine transaminase +EC 2.6.1.30: pyridoxamine—pyruvate transaminase +EC 2.6.1.31: pyridoxamine—oxaloacetate transaminase +EC 2.6.1.32: valine—3-methyl-2-oxovalerate transaminase +EC 2.6.1.33: dTDP-4-amino-4,6-dideoxy-D-glucose transaminase +EC 2.6.1.34: UDP-N-acetylbacillosamine transaminase +EC 2.6.1.35: glycine—oxaloacetate transaminase +EC 2.6.1.36: L-lysine 6-transaminase +EC 2.6.1.37: (2-aminoethyl)phosphonate—pyruvate transaminase +EC 2.6.1.38: histidine transaminase +EC 2.6.1.39: 2-aminoadipate transaminase +EC 2.6.1.40: (R)-3-amino-2-methylpropionate—pyruvate transaminase +EC 2.6.1.41: D-methionine—pyruvate transaminase +EC 2.6.1.42: branched-chain-amino-acid transaminase +EC 2.6.1.43: aminolevulinate transaminase +EC 2.6.1.44: alanine—glyoxylate transaminase +EC 2.6.1.45: serine—glyoxylate transaminase +EC 2.6.1.46: diaminobutyrate—pyruvate transaminase +EC 2.6.1.47: alanine—oxomalonate transaminase +EC 2.6.1.48: 5-aminovalerate transaminase +EC 2.6.1.49: dihydroxyphenylalanine transaminase +EC 2.6.1.50: glutamine—scyllo-inositol transaminase +EC 2.6.1.51: serine—pyruvate transaminase +EC 2.6.1.52: phosphoserine transaminase +EC 2.6.1.53: Now EC 1.4.1.13, glutamate synthase (NADPH) +EC 2.6.1.54: pyridoxamine-phosphate transaminase +EC 2.6.1.55: taurine—2-oxoglutarate transaminase +EC 2.6.1.56: 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase +EC 2.6.1.57: aromatic-amino-acid transaminase +EC 2.6.1.58: phenylalanine(histidine) transaminase +EC 2.6.1.59: dTDP-4-amino-4,6-dideoxygalactose transaminase +EC 2.6.1.60: aromatic-amino-acid—glyoxylate transaminase +EC 2.6.1.61: [[identical to EC 2.6.1.40, (((R)-3-amino-2-methylpropionate-pyruvate transaminase|(R)-3-amino-2-methylpropionate—pyruvate transaminase))|identical to EC 2.6.1.40, (R)-3-amino-2-methylpropionate—pyruvate transaminase]] +EC 2.6.1.62: adenosylmethionine—8-amino-7-oxononanoate transaminase +EC 2.6.1.63: kynurenine—glyoxylate transaminase +EC 2.6.1.64: glutamine—phenylpyruvate transaminase +EC 2.6.1.65: N6-acetyl-β-lysine transaminase +EC 2.6.1.66: valine—pyruvate transaminase +EC 2.6.1.67: 2-aminohexanoate transaminase +EC 2.6.1.68: Now classified as EC 2.6.1.13, ornithine aminotransferase and EC 2.6.1.36, L-lysine 6-transaminase +EC 2.6.1.69: [[identical to EC 2.6.1.11, ((acetylornithine transaminase))|identical to EC 2.6.1.11, acetylornithine transaminase]] +EC 2.6.1.70: aspartate—phenylpyruvate transaminase +EC 2.6.1.71: lysine—pyruvate 6-transaminase +EC 2.6.1.72: D-4-hydroxyphenylglycine transaminase +EC 2.6.1.73: methionine—glyoxylate transaminase +EC 2.6.1.74: cephalosporin-C transaminase +EC 2.6.1.75: cysteine-conjugate transaminase +EC 2.6.1.76: diaminobutyrate—2-oxoglutarate transaminase +EC 2.6.1.77: taurine—pyruvate aminotransferase +EC 2.6.1.78: aspartate—prephenate aminotransferase +EC 2.6.1.79: glutamate—prephenate aminotransferase +EC 2.6.1.80: nicotianamine aminotransferase +EC 2.6.1.81: succinylornithine transaminase +EC 2.6.1.82: putrescine aminotransferase +EC 2.6.1.83: LL-diaminopimelate aminotransferase +EC 2.6.1.84: arginine—pyruvate transaminase +EC 2.6.1.85: aminodeoxychorismate synthase +EC 2.6.1.86: 2-amino-4-deoxychorismate synthase +EC 2.6.1.87: UDP-4-amino-4-deoxy-L-arabinose aminotransferase +EC 2.6.1.88: methionine transaminase +EC 2.6.1.89: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose transaminase +EC 2.6.1.90: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose transaminase +EC 2.6.1.91: [[Identical to EC 2.6.1.34, ((UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase|UDP-N-acetylbacillosamine transaminase))|Identical to EC 2.6.1.34, UDP-N-acetylbacillosamine transaminase]] +EC 2.6.1.92: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine transaminase +EC 2.6.1.93: neamine transaminase +EC 2.6.1.94: 2′-deamino-2′-hydroxyneamine transaminase +EC 2.6.1.95: neomycin C transaminase +EC 2.6.1.96: 4-aminobutyrate—pyruvate transaminase +EC 2.6.1.97: archaeosine synthase +EC 2.6.1.98: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase +EC 2.6.1.99: L-tryptophan—pyruvate aminotransferase +EC 2.6.1.100: L-glutamine:2-deoxy-scyllo-inosose aminotransferase +EC 2.6.1.101: L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase +EC 2.6.1.102: GDP-perosamine synthase +EC 2.6.1.103: (S)-3,5-dihydroxyphenylglycine transaminase +EC 2.6.1.104: 3-dehydro-glucose-6-phosphate—glutamate transaminase +EC 2.6.1.105: lysine—8-amino-7-oxononanoate transaminase +EC 2.6.1.106: dTDP-3-amino-3,4,6-trideoxy-α-D-glucose transaminase +EC 2.6.1.107: β-methylphenylalanine transaminase +EC 2.6.1.108: (5-formylfuran-3-yl)methyl phosphate transaminase +EC 2.6.1.109: 8-amino-3,8-dideoxy-α-D-manno-octulosonate transaminase +EC 2.6.1.110: dTDP-4-dehydro-2,3,6-trideoxy-D-glucose 4-aminotransferase +EC 2.6.1.111: 3-aminobutanoyl-CoA transaminase +EC 2.6.1.112: (S)-ureidoglycine—glyoxylate transaminase +EC 2.6.1.113: putrescine—pyruvate transaminase +EC 2.6.1.114: 8-demethyl-8-aminoriboflavin-5′-phosphate synthase +EC 2.6.1.115: 5-hydroxydodecatetraenal 1-aminotransferase +EC 2.6.1.116: 6-aminohexanoate aminotransferase +EC 2.6.1.117: L-glutamine—4-(methylsulfanyl)-2-oxobutanoate aminotransferase +EC 2.6.1.118: [amino-group carrier protein]-γ-(L-lysyl)-L-glutamate aminotransferase +EC 2.6.1.119: vanillin aminotransferase + +=== EC 2.6.2: Amidinotransferases (deleted sub-subclass) === +EC 2.6.2.1: now EC 2.1.4.1 glycine amidinotransferase + +=== EC 2.6.3: Oximinotransferases === +EC 2.6.3.1: oximinotransferase + +=== EC 2.6.99: Transferring Other Nitrogenous Groups === +EC 2.6.99.1: dATP(dGTP)—DNA purinetransferase +EC 2.6.99.2: pyridoxine 5′-phosphate synthase +EC 2.6.99.3: O-ureido-L-serine synthase +EC 2.6.99.4: Now EC 2.3.1.234, N6-L-threonylcarbamoyladenine synthase. + +== EC 2.7: Transferring Phosphorus-Containing Groups == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-11.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-11.md new file mode 100644 index 000000000..cfb8934c6 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-11.md @@ -0,0 +1,244 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 12/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.7.1: Phosphotransferases with an alcohol group as acceptor === +EC 2.7.1.1: hexokinase +EC 2.7.1.2: glucokinase +EC 2.7.1.3: ketohexokinase +EC 2.7.1.4: fructokinase +EC 2.7.1.5: rhamnulokinase +EC 2.7.1.6: galactokinase +EC 2.7.1.7: mannokinase +EC 2.7.1.8: glucosamine kinase +EC 2.7.1.9: deleted +EC 2.7.1.10: phosphoglucokinase +EC 2.7.1.11: 6-phosphofructokinase +EC 2.7.1.12: gluconokinase +EC 2.7.1.13: dehydrogluconokinase +EC 2.7.1.14: sedoheptulokinase +EC 2.7.1.15: ribokinase +EC 2.7.1.16: ribulokinase +EC 2.7.1.17: xylulokinase +EC 2.7.1.18: phosphoribokinase +EC 2.7.1.19: phosphoribulokinase +EC 2.7.1.20: adenosine kinase +EC 2.7.1.21: thymidine kinase +EC 2.7.1.22: ribosylnicotinamide kinase +EC 2.7.1.23: NAD+ kinase +EC 2.7.1.24: dephospho-CoA kinase +EC 2.7.1.25: adenylyl-sulfate kinase +EC 2.7.1.26: riboflavin kinase +EC 2.7.1.27: erythritol kinase (D-erythritol 4-phosphate-forming) +EC 2.7.1.28: triokinase +EC 2.7.1.29: glycerone kinase +EC 2.7.1.30: glycerol kinase +EC 2.7.1.31: glycerate kinase +EC 2.7.1.32: choline kinase +EC 2.7.1.33: pantothenate kinase +EC 2.7.1.34: pantetheine kinase +EC 2.7.1.35: pyridoxal kinase +EC 2.7.1.36: mevalonate kinase +EC 2.7.1.37: now divided into EC 2.7.11.1, EC 2.7.11.8, EC 2.7.11.9, EC 2.7.11.10, EC 2.7.11.11, EC 2.7.11.12, EC 2.7.11.13, EC 2.7.11.21, EC 2.7.11.22, EC 2.7.11.24, EC 2.7.11.25, EC 2.7.11.30 and EC 2.7.12.1 +EC 2.7.1.38: now EC 2.7.11.19, phosphorylase kinase +EC 2.7.1.39: homoserine kinase +EC 2.7.1.40: pyruvate kinase +EC 2.7.1.41: glucose-1-phosphate phosphodismutase +EC 2.7.1.42: riboflavin phosphotransferase +EC 2.7.1.43: glucuronokinase +EC 2.7.1.44: galacturonokinase +EC 2.7.1.45: 2-dehydro-3-deoxygluconokinase +EC 2.7.1.46: L-arabinokinase +EC 2.7.1.47: D-ribulokinase +EC 2.7.1.48: uridine kinase +EC 2.7.1.49: hydroxymethylpyrimidine kinase +EC 2.7.1.50: hydroxyethylthiazole kinase +EC 2.7.1.51: L-fuculokinase +EC 2.7.1.52: fucokinase +EC 2.7.1.53: L-xylulokinase +EC 2.7.1.54: D-arabinokinase +EC 2.7.1.55: allose kinase +EC 2.7.1.56: 1-phosphofructokinase +EC 2.7.1.57: deleted +EC 2.7.1.58: 2-dehydro-3-deoxygalactonokinase +EC 2.7.1.59: N-acetylglucosamine kinase +EC 2.7.1.60: N-acylmannosamine kinase +EC 2.7.1.61: acyl-phosphate—hexose phosphotransferase +EC 2.7.1.62: Phosphoramidate-hexose phosphotransferase +EC 2.7.1.63: polyphosphate—glucose phosphotransferase +EC 2.7.1.64: inositol 3-kinase +EC 2.7.1.65: scyllo-inosamine 4-kinase +EC 2.7.1.66: undecaprenol kinase +EC 2.7.1.67: 1-phosphatidylinositol 4-kinase +EC 2.7.1.68: 1-phosphatidylinositol-4-phosphate 5-kinase +EC 2.7.1.69: now covered by EC 2.7.1.191, EC 2.7.1.192, EC 2.7.1.193, EC 2.7.1.194, EC 2.7.1.195, EC 2.7.1.196, EC 2.7.1.197, EC 2.7.1.198, EC 2.7.1.199, EC 2.7.1.200 EC 2.7.1.20, EC 2.7.1.202, EC 2.7.1.203, EC 2.7.1.204, EC 2.7.1.205, EC 2.7.1.206, EC 2.7.1.207 and EC 2.7.1.208 +EC 2.7.1.70: Now included in EC 2.7.11.1, non-specific serine/threonine protein kinase +EC 2.7.1.71: shikimate kinase +EC 2.7.1.72: streptomycin 6-kinase +EC 2.7.1.73: inosine kinase +EC 2.7.1.74: deoxycytidine kinase +EC 2.7.1.75: Now EC 2.7.1.21 thymidine kinase +EC 2.7.1.76: deoxyadenosine kinase +EC 2.7.1.77: nucleoside phosphotransferase +EC 2.7.1.78: polynucleotide 5′-hydroxyl-kinase +EC 2.7.1.79: diphosphate—glycerol phosphotransferase +EC 2.7.1.80: diphosphate—serine phosphotransferase +EC 2.7.1.81: hydroxylysine kinase +EC 2.7.1.82: ethanolamine kinase +EC 2.7.1.83: pseudouridine kinase +EC 2.7.1.84: alkylglycerone kinase +EC 2.7.1.85: β-glucoside kinase +EC 2.7.1.86: NADH kinase +EC 2.7.1.87: streptomycin 3′′-kinase +EC 2.7.1.88: dihydrostreptomycin-6-phosphate 3′α-kinase +EC 2.7.1.89: thiamine kinase +EC 2.7.1.90: diphosphate—fructose-6-phosphate 1-phosphotransferase +EC 2.7.1.91: sphinganine kinase +EC 2.7.1.92: 5-dehydro-2-deoxygluconokinase +EC 2.7.1.93: alkylglycerol kinase +EC 2.7.1.94: acylglycerol kinase +EC 2.7.1.95: kanamycin kinase +EC 2.7.1.96: deleted, Now included with EC 2.7.1.86 NADH kinase +EC 2.7.1.97: deleted, Identical with EC 2.7.11.14, rhodopsin kinase +EC 2.7.1.98: deleted +EC 2.7.1.99: Now EC 2.7.11.2, [pyruvate dehydrogenase (acetyl-transferring)] kinase +EC 2.7.1.100: S-methyl-5-thioribose kinase +EC 2.7.1.101: tagatose kinase +EC 2.7.1.102: hamamelose kinase +EC 2.7.1.103: viomycin kinase +EC 2.7.1.104: Now EC 2.7.99.1, triphosphate—protein phosphotransferase +EC 2.7.1.105: 6-phosphofructo-2-kinase +EC 2.7.1.106: glucose-1,6-bisphosphate synthase +EC 2.7.1.107: diacylglycerol kinase +EC 2.7.1.108: dolichol kinase +EC 2.7.1.109: Now EC 2.7.11.31, [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase +EC 2.7.1.110: Now EC 2.7.11.3, dephospho-(reductase kinase) kinase +EC 2.7.1.111: Now listed as EC 2.7.11.27, [acetyl-CoA carboxylase] kinase +EC 2.7.1.112: Now EC 2.7.10.2, non-specific protein-tyrosine kinase +EC 2.7.1.113: deoxyguanosine kinase +EC 2.7.1.114: AMP—thymidine kinase +EC 2.7.1.115: Now EC 2.7.11.4, (3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) kinase +EC 2.7.1.116: Now EC 2.7.11.5, [isocitrate dehydrogenase (NADP+)] kinase +EC 2.7.1.117: Now EC 2.7.11.18, myosin-light-chain kinase +EC 2.7.1.118: ADP—thymidine kinase +EC 2.7.1.119: hygromycin-B 7′′-O-kinase +EC 2.7.1.120: Now EC 2.7.11.17, Ca2+/calmodulin-dependent protein kinase +EC 2.7.1.121: phosphoenolpyruvate—glycerone phosphotransferase +EC 2.7.1.122: xylitol kinase +EC 2.7.1.123: Now EC 2.7.11.17, Ca2+/calmodulin-dependent protein kinase +EC 2.7.1.124: Now EC 2.7.11.6, [tyrosine 3-monooxygenase] kinase +EC 2.7.1.125: Now EC 2.7.11.14, rhodopsin kinase +EC 2.7.1.126: Now EC 2.7.11.15, β-adrenergic-receptor kinase +EC 2.7.1.127: inositol-trisphosphate 3-kinase +EC 2.7.1.128: Now EC 2.7.11.27, [acetyl-CoA carboxylase] kinase +EC 2.7.1.129: Now EC 2.7.11.7, myosin-heavy-chain kinase +EC 2.7.1.130: tetraacyldisaccharide 4′-kinase +EC 2.7.1.131: Now EC 2.7.11.29, low-density-lipoprotein receptor kinase +EC 2.7.1.132: Now EC 2.7.11.28, tropomyosin kinase +EC 2.7.1.133: Now included with EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase +EC 2.7.1.134: inositol-tetrakisphosphate 1-kinase +EC 2.7.1.135: Now EC 2.7.11.26, tau-protein kinase +EC 2.7.1.136: macrolide 2′-kinase +EC 2.7.1.137: phosphatidylinositol 3-kinase +EC 2.7.1.138: ceramide kinase +EC 2.7.1.139: Now included with EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase +EC 2.7.1.140: inositol-tetrakisphosphate 5-kinase +EC 2.7.1.141: Now EC 2.7.11.23, [RNA-polymerase]-subunit kinase +EC 2.7.1.142: glycerol-3-phosphate—glucose phosphotransferase +EC 2.7.1.143: diphosphate-purine nucleoside kinase +EC 2.7.1.144: tagatose-6-phosphate kinase +EC 2.7.1.145: deoxynucleoside kinase +EC 2.7.1.146: ADP-dependent phosphofructokinase +EC 2.7.1.147: ADP-dependent glucokinase +EC 2.7.1.148: 4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol kinase +EC 2.7.1.149: 1-phosphatidylinositol-5-phosphate 4-kinase +EC 2.7.1.150: 1-phosphatidylinositol-3-phosphate 5-kinase +EC 2.7.1.151: inositol-polyphosphate multikinase +EC 2.7.1.152: Now EC 2.7.4.21, inositol-hexakisphosphate kinase +EC 2.7.1.153: phosphatidylinositol-4,5-bisphosphate 3-kinase +EC 2.7.1.154: phosphatidylinositol-4-phosphate 3-kinase +EC 2.7.1.155: Now EC 2.7.4.24, diphosphoinositol-pentakisphosphate kinase +EC 2.7.1.156: adenosylcobinamide kinase +EC 2.7.1.157: N-acetylgalactosamine kinase +EC 2.7.1.158: inositol-pentakisphosphate 2-kinase +EC 2.7.1.159: inositol-1,3,4-trisphosphate 5/6-kinase +EC 2.7.1.160: 2′-phosphotransferase +EC 2.7.1.161: CTP-dependent riboflavin kinase +EC 2.7.1.162: N-acetylhexosamine 1-kinase +EC 2.7.1.163: hygromycin B 4-O-kinase +EC 2.7.1.164: O-phosphoseryl-tRNASec kinase +EC 2.7.1.165: glycerate 2-kinase +EC 2.7.1.166: 3-deoxy-D-manno-octulosonic acid kinase +EC 2.7.1.167: D-glycero-β-D-manno-heptose-7-phosphate kinase +EC 2.7.1.168: D-glycero-α-D-manno-heptose-7-phosphate kinase +EC 2.7.1.169: pantoate kinase +EC 2.7.1.170: anhydro-N-acetylmuramic acid kinase +EC 2.7.1.171: protein-fructosamine 3-kinase +EC 2.7.1.172: protein-ribulosamine 3-kinase +EC 2.7.1.173: nicotinate riboside kinase +EC 2.7.1.174: diacylglycerol kinase (CTP dependent) +EC 2.7.1.175: maltokinase +EC 2.7.1.176: UDP-N-acetylglucosamine kinase +EC 2.7.1.177: L-threonine kinase +EC 2.7.1.178: 2-dehydro-3-deoxyglucono/galactono-kinase +EC 2.7.1.179: kanosamine kinase +EC 2.7.1.180: FAD:protein FMN transferase +EC 2.7.1.181: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol kinase +EC 2.7.1.182: phytol kinase +EC 2.7.1.183: glycoprotein-mannosyl O6-kinase +EC 2.7.1.184: sulfofructose kinase +EC 2.7.1.185: mevalonate 3-kinase +EC 2.7.1.186: mevalonate-3-phosphate 5-kinase +EC 2.7.1.187: acarbose 7IV-phosphotransferase +EC 2.7.1.188: 2-epi-5-epi-valiolone 7-kinase +EC 2.7.1.189: autoinducer-2 kinase +EC 2.7.1.190: aminoglycoside 2′′-phosphotransferase +EC 2.7.1.191: protein-N π-phosphohistidine—D-mannose phosphotransferase +EC 2.7.1.192: protein-N π-phosphohistidine—N-acetylmuramate phosphotransferase +EC 2.7.1.193: protein-N π-phosphohistidine—N-acetyl-D-glucosamine phosphotransferase +EC 2.7.1.194: protein-N π-phosphohistidine—L-ascorbate phosphotransferase +EC 2.7.1.195: protein-N π-phosphohistidine—2-O-α-mannosyl-D-glycerate phosphotransferase +EC 2.7.1.196: protein-N π-phosphohistidine—N,N′-diacetylchitobiose phosphotransferase +EC 2.7.1.197: protein-Nπ'-phosphohistidine—D-mannitol phosphotransferase +EC 2.7.1.198: protein-N π-phosphohistidine—D-sorbitol phosphotransferase +EC 2.7.1.199: protein-N π-phosphohistidine—D-glucose phosphotransferase +EC 2.7.1.200: protein-N π-phosphohistidine—galactitol phosphotransferase +EC 2.7.1.201: protein-N π-phosphohistidine—trehalose phosphotransferase +EC 2.7.1.202: protein-N π-phosphohistidine—D-fructose phosphotransferase +EC 2.7.1.203: protein-N π-phosphohistidine—D-glucosaminate phosphotransferase +EC 2.7.1.204: protein-N π-phosphohistidine—D-galactose phosphotransferase +EC 2.7.1.205: protein-N π-phosphohistidine—cellobiose phosphotransferase +EC 2.7.1.206: protein-N π-phosphohistidine—L-sorbose phosphotransferase +EC 2.7.1.207: protein-N π-phosphohistidine—lactose phosphotransferase +EC 2.7.1.208: protein-N π-phosphohistidine—maltose phosphotransferase +EC 2.7.1.209: L-erythrulose 1-kinase +EC 2.7.1.210: D-erythrulose 4-kinase +EC 2.7.1.211: protein-N π-phosphohistidine—sucrose phosphotransferase +EC 2.7.1.212: α-D-ribose-1-phosphate 5-kinase (ADP) +EC 2.7.1.213: cytidine kinase +EC 2.7.1.214: C7-cyclitol 7-kinase +EC 2.7.1.215: erythritol kinase (D-erythritol 1-phosphate-forming) +EC 2.7.1.216: farnesol kinase +EC 2.7.1.217: 3-dehydrotetronate 4-kinase +EC 2.7.1.218: fructoselysine 6-kinase +EC 2.7.1.219: D-threonate 4-kinase +EC 2.7.1.220: D-erythronate 4-kinase +EC 2.7.1.221: N-acetylmuramate 1-kinase +EC 2.7.1.222: 4-hydroxytryptamine kinase +EC 2.7.1.223: aminoimidazole riboside kinase +EC 2.7.1.224: cytidine diphosphoramidate kinase +EC 2.7.1.225: L-serine kinase (ATP) +EC 2.7.1.226: L-serine kinase (ADP) +EC 2.7.1.227: inositol phosphorylceramide synthase +EC 2.7.1.228: mannosyl-inositol-phosphoceramide inositolphosphotransferase +EC 2.7.1.229: deoxyribokinase +EC 2.7.1.230: amicoumacin kinase +EC 2.7.1.231: 3-oxoisoapionate kinase +EC 2.7.1.232: levoglucosan kinase +EC 2.7.1.233: apulose kinase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-12.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-12.md new file mode 100644 index 000000000..b6fc5b578 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-12.md @@ -0,0 +1,198 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 13/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.7.2: Phosphotransferases with a carboxy group as acceptor === +EC 2.7.2.1: acetate kinase +EC 2.7.2.2: carbamate kinase +EC 2.7.2.3: phosphoglycerate kinase +EC 2.7.2.4: aspartate kinase +EC 2.7.2.5: Now EC 6.3.4.16, carbamoyl-phosphate synthase (ammonia) +EC 2.7.2.6: formate kinase +EC 2.7.2.7: butyrate kinase +EC 2.7.2.8: acetylglutamate kinase +EC 2.7.2.9: Now EC 6.3.5.5, carbamoyl-phosphate synthase (glutamine-hydrolysing) +EC 2.7.2.10: phosphoglycerate kinase (GTP) +EC 2.7.2.11: glutamate 5-kinase +EC 2.7.2.12: acetate kinase (diphosphate) +EC 2.7.2.13: Now known to be due to the activities of EC 6.1.1.17, glutamate—tRNA ligase, EC 1.2.1.70, glutamyl-tRNA reductase and EC 5.4.3.8 glutamate-1-semialdehyde 2,1-aminomutase +EC 2.7.2.14: branched-chain-fatty-acid kinase +EC 2.7.2.15: propionate kinase +EC 2.7.2.16: 2-phosphoglycerate kinase +EC 2.7.2.17: [amino-group carrier protein]-L-2-aminoadipate 6-kinase +EC 2.7.2.18: fatty acid kinase + +=== EC 2.7.3: Phosphotransferases with a nitrogenous group as acceptor === +EC 2.7.3.1: guanidinoacetate kinase +EC 2.7.3.2: creatine kinase +EC 2.7.3.3: arginine kinase +EC 2.7.3.4: taurocyamine kinase +EC 2.7.3.5: lombricine kinase +EC 2.7.3.6: hypotaurocyamine kinase +EC 2.7.3.7: opheline kinase +EC 2.7.3.8: ammonia kinase +EC 2.7.3.9: phosphoenolpyruvate—protein phosphotransferase +EC 2.7.3.10: agmatine kinase +EC 2.7.3.11: now EC 2.7.13.1, protein-histidine pros-kinase +EC 2.7.3.12: now EC 2.7.13.2, protein-histidine tele-kinase +EC 2.7.3.13: glutamine kinase + +=== EC 2.7.4: Phosphotransferases with a phosphate group as acceptor === +EC 2.7.4.1: ATP-polyphosphate phosphotransferase +EC 2.7.4.2: phosphomevalonate kinase +EC 2.7.4.3: adenylate kinase +EC 2.7.4.4: nucleoside-phosphate kinase +EC 2.7.4.5: deleted, now included with EC 2.7.4.14 cytidylate kinase +EC 2.7.4.6: nucleoside-diphosphate kinase +EC 2.7.4.7: phosphomethylpyrimidine kinase +EC 2.7.4.8: guanylate kinase +EC 2.7.4.9: dTMP kinase +EC 2.7.4.10: nucleoside-triphosphate—adenylate kinase +EC 2.7.4.11: (deoxy)adenylate kinase +EC 2.7.4.12: T2-induced deoxynucleotide kinase +EC 2.7.4.13: (deoxy)nucleoside-phosphate kinase +EC 2.7.4.14: cytidylate kinase +EC 2.7.4.15: thiamine-diphosphate kinase +EC 2.7.4.16: thiamine-phosphate kinase +EC 2.7.4.17: 3-phosphoglyceroyl-phosphate—polyphosphate phosphotransferase +EC 2.7.4.18: farnesyl-diphosphate kinase +EC 2.7.4.19: 5-methyldeoxycytidine-5′-phosphate kinase +EC 2.7.4.20: dolichyl-diphosphate—polyphosphate phosphotransferase +EC 2.7.4.21: inositol-hexakisphosphate kinase +EC 2.7.4.22: UMP kinase +EC 2.7.4.23: ribose 1,5-bisphosphate phosphokinase +EC 2.7.4.24: diphosphoinositol-pentakisphosphate kinase +EC 2.7.4.25: (d)CMP kinase +EC 2.7.4.26: isopentenyl phosphate kinase +EC 2.7.4.27: [pyruvate, phosphate dikinase]-phosphate phosphotransferase +EC 2.7.4.28: [pyruvate, water dikinase]-phosphate phosphotransferase +EC 2.7.4.29: Kdo2-lipid A phosphotransferase +EC 2.7.4.30: Now EC 2.7.8.43, lipid A phosphoethanolamine transferase +EC 2.7.4.31: [[[5-(aminomethyl)furan-3-yl]methyl phosphate kinase]] +EC 2.7.4.32: farnesyl phosphate kinase +EC 2.7.4.33: AMP-polyphosphate phosphotransferase +EC 2.7.4.34: GDP-polyphosphate phosphotransferase + +=== EC 2.7.5: Phosphotransferases with regeneration of donors, apparently catalysing intramolecular transfers === +Deleted sub-subclass + +=== EC 2.7.6: Diphosphotransferases === +EC 2.7.6.1: ribose-phosphate diphosphokinase +EC 2.7.6.2: thiamine diphosphokinase +EC 2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase +EC 2.7.6.4: nucleotide diphosphokinase +EC 2.7.6.5: GTP diphosphokinase + +=== EC 2.7.7: Nucleotidyltransferases === +EC 2.7.7.1: nicotinamide-nucleotide adenylyltransferase +EC 2.7.7.2: FAD synthase +EC 2.7.7.3: pantetheine-phosphate adenylyltransferase +EC 2.7.7.4: sulfate adenylyltransferase +EC 2.7.7.5: sulfate adenylyltransferase (ADP) +EC 2.7.7.6: DNA-directed RNA polymerase +EC 2.7.7.7: DNA-directed DNA polymerase +EC 2.7.7.8: polyribonucleotide nucleotidyltransferase +EC 2.7.7.9: UTP—glucose-1-phosphate uridylyltransferase +EC 2.7.7.10: UTP—hexose-1-phosphate uridylyltransferase +EC 2.7.7.11: UTP—xylose-1-phosphate uridylyltransferase +EC 2.7.7.12: UDP-glucose—hexose-1-phosphate uridylyltransferase +EC 2.7.7.13: mannose-1-phosphate guanylyltransferase +EC 2.7.7.14: ethanolamine-phosphate cytidylyltransferase +EC 2.7.7.15: choline-phosphate cytidylyltransferase +EC 2.7.7.16: Now EC 4.6.1.18, pancreatic ribonuclease +EC 2.7.7.17: Now EC 4.6.1.19, ribonuclease T2 +EC 2.7.7.18: nicotinate-nucleotide adenylyltransferase +EC 2.7.7.19: polynucleotide adenylyltransferase +EC 2.7.7.20: deleted (identical with EC 2.7.7.72, CCA tRNA nucleotidyltransferase +EC 2.7.7.21: Now EC 2.7.7.72, CCA tRNA nucleotidyltransferase +EC 2.7.7.22: mannose-1-phosphate guanylyltransferase (GDP) +EC 2.7.7.23: UDP-N-acetylglucosamine diphosphorylase +EC 2.7.7.24: glucose-1-phosphate thymidylyltransferase +EC 2.7.7.25: Now EC 2.7.7.72, CCA tRNA nucleotidyltransferase +EC 2.7.7.26: Now EC 4.6.1.24, ribonuclease T1 +EC 2.7.7.27: glucose-1-phosphate adenylyltransferase +EC 2.7.7.28: nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase +EC 2.7.7.29: [[identical to EC 2.7.7.28, ((nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase))|identical to EC 2.7.7.28, nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase]] +EC 2.7.7.30: fucose-1-phosphate guanylyltransferase +EC 2.7.7.31: DNA nucleotidylexotransferase +EC 2.7.7.32: galactose-1-phosphate thymidylyltransferase +EC 2.7.7.33: glucose-1-phosphate cytidylyltransferase +EC 2.7.7.34: glucose-1-phosphate guanylyltransferase +EC 2.7.7.35: ribose-5-phosphate adenylyltransferase +EC 2.7.7.36: aldose-1-phosphate adenylyltransferase +EC 2.7.7.37: aldose-1-phosphate nucleotidyltransferase +EC 2.7.7.38: 3-deoxy-manno-octulosonate cytidylyltransferase +EC 2.7.7.39: glycerol-3-phosphate cytidylyltransferase +EC 2.7.7.40: D-ribitol-5-phosphate cytidylyltransferase +EC 2.7.7.41: phosphatidate cytidylyltransferase +EC 2.7.7.42: [glutamine synthetase] adenylyltransferase +EC 2.7.7.43: N-acylneuraminate cytidylyltransferase +EC 2.7.7.44: glucuronate-1-phosphate uridylyltransferase +EC 2.7.7.45: guanosine-triphosphate guanylyltransferase +EC 2.7.7.46: gentamicin 2′′-nucleotidyltransferase +EC 2.7.7.47: streptomycin 3′′-adenylyltransferase +EC 2.7.7.48: RNA-directed RNA polymerase +EC 2.7.7.49: RNA-directed DNA polymerase +EC 2.7.7.50: mRNA guanylyltransferase +EC 2.7.7.51: adenylylsulfate—ammonia adenylyltransferase +EC 2.7.7.52: RNA uridylyltransferase +EC 2.7.7.53: ATP adenylyltransferase +EC 2.7.7.54: The activity is part of EC 6.3.2.40, cyclopeptine synthase +EC 2.7.7.55: The activity is part of EC 6.3.2.40, cyclopeptine synthase +EC 2.7.7.56: tRNA nucleotidyltransferase +EC 2.7.7.57: N-methylphosphoethanolamine cytidylyltransferase +EC 2.7.7.58: Now included in EC 6.2.1.71, [[2,3-dihydroxybenzoate[aryl-carrier protein] ligase]] +EC 2.7.7.59: [protein-PII] uridylyltransferase +EC 2.7.7.60: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase +EC 2.7.7.61: citrate lyase holo-[acyl-carrier protein] synthase +EC 2.7.7.62: adenosylcobinamide-phosphate guanylyltransferase +EC 2.7.7.63: Now EC 6.3.1.20, lipoate—protein ligase +EC 2.7.7.64: UTP-monosaccharide-1-phosphate uridylyltransferase +EC 2.7.7.65: diguanylate cyclase +EC 2.7.7.66: malonate decarboxylase holo-[acyl-carrier protein] synthase +EC 2.7.7.67: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase +EC 2.7.7.68: 2-phospho-L-lactate guanylyltransferase +EC 2.7.7.69: GDP-L-galactose/GDP-D-glucose: hexose 1-phosphate guanylyltransferase +EC 2.7.7.70: D-glycero-β-D-manno-heptose 1-phosphate adenylyltransferase +EC 2.7.7.71: D-glycero-α-D-manno-heptose 1-phosphate guanylyltransferase +EC 2.7.7.72: CCA tRNA nucleotidyltransferase +EC 2.7.7.73: sulfur carrier protein ThiS adenylyltransferase +EC 2.7.7.74: 1L-myo-inositol 1-phosphate cytidylyltransferase +EC 2.7.7.75: molybdopterin adenylyltransferase +EC 2.7.7.76: molybdenum cofactor cytidylyltransferase +EC 2.7.7.77: molybdenum cofactor guanylyltransferase +EC 2.7.7.78: GDP-D-glucose phosphorylase +EC 2.7.7.79: tRNAHis guanylyltransferase +EC 2.7.7.80: molybdopterin-synthase adenylyltransferase +EC 2.7.7.81: pseudaminic acid cytidylyltransferase +EC 2.7.7.82: CMP-N,N′-diacetyllegionaminic acid synthase +EC 2.7.7.83: UDP-N-acetylgalactosamine diphosphorylase +EC 2.7.7.84: diadenylate cyclase +EC 2.7.7.85: 2′-5′ oligoadenylate synthase +EC 2.7.7.86: cyclic GMP-AMP synthase +EC 2.7.7.87: L-threonylcarbamoyladenylate synthase +EC 2.7.7.88: GDP polyribonucleotidyltransferase +EC 2.7.7.89: [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase +EC 2.7.7.90: 8-amino-3,8-dideoxy-''manno''-octulosonate cytidylyltransferase +EC 2.7.7.91: valienol-1-phosphate guanylyltransferase +EC 2.7.7.92: 3-deoxy-D-glycero-D-galacto-nonulopyranosonate cytidylyltransferase +EC 2.7.7.93: phosphonoformate cytidylyltransferase +EC 2.7.7.94: Now EC 6.2.1.51, 4-hydroxyphenylalkanoate adenylyltransferase FadD29 +EC 2.7.7.95: Now EC 6.2.1.49, long-chain fatty acid adenylyltransferase FadD28 +EC 2.7.7.96: ADP-D-ribose pyrophosphorylase +EC 2.7.7.97: 3-hydroxy-4-methylanthranilate adenylyltransferase +EC 2.7.7.98: Now EC 6.2.1.50, 4-hydroxybenzoate adenylyltransferase FadD22 +EC 2.7.7.99: N-acetyl-α-D-muramate 1-phosphate uridylyltransferase +EC 2.7.7.100: SAMP-activating enzyme +EC 2.7.7.101: DNA primase DnaG +EC 2.7.7.102: DNA primase AEP +EC 2.7.7.103: L-glutamine-phosphate cytidylyltransferase +EC 2.7.7.104: 2-hydroxyethylphosphonate cytidylyltransferase +EC 2.7.7.105: phospho''enol''pyruvate guanylyltransferase +EC 2.7.7.106: 3-phospho-D-glycerate guanylyltransferase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-13.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-13.md new file mode 100644 index 000000000..ad45fba5e --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-13.md @@ -0,0 +1,235 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 14/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.7.8: Transferases for other substituted phosphate groups === +EC 2.7.8.1: diacylglycerol ethanolaminephosphotransferase +EC 2.7.8.2: diacylglycerol cholinephosphotransferase +EC 2.7.8.3: ceramide cholinephosphotransferase +EC 2.7.8.4: serine ethanolaminephosphotransferase +EC 2.7.8.5: CDP-diacylglycerol—glycerol-3-phosphate 1-phosphatidyltransferase +EC 2.7.8.6: undecaprenyl-phosphate galactose phosphotransferase +EC 2.7.8.7: holo-[acyl-carrier-protein] synthase +EC 2.7.8.8: CDP-diacylglycerol—serine O-phosphatidyltransferase +EC 2.7.8.9: phosphomannan mannosephosphotransferase +EC 2.7.8.10: sphingosine cholinephosphotransferase +EC 2.7.8.11: CDP-diacylglycerol—inositol 3-phosphatidyltransferase +EC 2.7.8.12: CDP-glycerol glycerophosphotransferase +EC 2.7.8.13: phospho-N-acetylmuramoyl-pentapeptide-transferase +EC 2.7.8.14: CDP-ribitol ribitolphosphotransferase +EC 2.7.8.15: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase +EC 2.7.8.16: deleted, now included with EC 2.7.8.2 diacylglycerol cholinephosphotransferase +EC 2.7.8.17: UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase +EC 2.7.8.18: UDP-galactose—UDP-N-acetylglucosamine galactose phosphotransferase +EC 2.7.8.19: UDP-glucose—glycoprotein glucose phosphotransferase +EC 2.7.8.20: phosphatidylglycerol—membrane-oligosaccharide glycerophosphotransferase +EC 2.7.8.21: membrane-oligosaccharide glycerophosphotransferase +EC 2.7.8.22: 1-alkenyl-2-acylglycerol choline phosphotransferase +EC 2.7.8.23: carboxyvinyl-carboxyphosphonate phosphorylmutase +EC 2.7.8.24: CDP-diacylglycerol—choline O-phosphatidyltransferase +EC 2.7.8.25: Now EC 2.4.2.52, triphosphoribosyl-dephospho-CoA synthase +EC 2.7.8.26: adenosylcobinamide-GDP ribazoletransferase +EC 2.7.8.27: sphingomyelin synthase +EC 2.7.8.28: 2-phospho-L-lactate transferase +EC 2.7.8.29: L-serine-phosphatidylethanolamine phosphatidyltransferase +EC 2.7.8.30: Now EC 2.4.2.53, undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase +EC 2.7.8.31: undecaprenyl-phosphate glucose phosphotransferase +EC 2.7.8.32: 3-O-α-D-mannopyranosyl-α-D-mannopyranose xylosylphosphotransferase +EC 2.7.8.33: UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase +EC 2.7.8.34: CDP-L-myo-inositol myo-inositolphosphotransferase +EC 2.7.8.35: UDP-N-acetylglucosamine—decaprenyl-phosphate N-acetylglucosaminephosphotransferase +EC 2.7.8.36: undecaprenyl phosphate N,N′-diacetylbacillosamine 1-phosphate transferase +EC 2.7.8.37: α-D-ribose 1-methylphosphonate 5-triphosphate synthase +EC 2.7.8.38: archaetidylserine synthase +EC 2.7.8.39: archaetidylinositol phosphate synthase +EC 2.7.8.40: UDP-N-acetylgalactosamine-undecaprenyl-phosphate N-acetylgalactosaminephosphotransferase +EC 2.7.8.41: cardiolipin synthase (CMP-forming) +EC 2.7.8.42: Kdo2-lipid A phosphoethanolamine 7′′-transferase +EC 2.7.8.43: lipid A phosphoethanolamine transferase +EC 2.7.8.44: teichoic acid glycerol-phosphate primase +EC 2.7.8.45: teichoic acid glycerol-phosphate transferase +EC 2.7.8.46: teichoic acid ribitol-phosphate primase +EC 2.7.8.47: teichoic acid ribitol-phosphate polymerase + +=== EC 2.7.9: Phosphotransferases with paired acceptors (dikinases) === +EC 2.7.9.1: pyruvate, phosphate dikinase +EC 2.7.9.2: pyruvate, water dikinase +EC 2.7.9.3: selenide, water dikinase +EC 2.7.9.4: α-glucan, water dikinase +EC 2.7.9.5: phosphoglucan, water dikinase +EC 2.7.9.6: rifampicin phosphotransferase + +=== EC 2.7.10: Protein-tyrosine kinases === +EC 2.7.10.1: receptor protein-tyrosine kinase +EC 2.7.10.2: non-specific protein-tyrosine kinase + +=== EC 2.7.11: Protein-serine/threonine kinases === +EC 2.7.11.1: non-specific serine/threonine protein kinase +EC 2.7.11.2: [pyruvate dehydrogenase (acetyl-transferring)] kinase +EC 2.7.11.3: dephospho-(reductase kinase) kinase +EC 2.7.11.4: (3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) kinase +EC 2.7.11.5: [isocitrate dehydrogenase (NADP+)] kinase +EC 2.7.11.6: [tyrosine 3-monooxygenase] kinase +EC 2.7.11.7: myosin-heavy-chain kinase +EC 2.7.11.8: Fas-activated serine/threonine kinase +EC 2.7.11.9: Goodpasture-antigen-binding protein kinase +EC 2.7.11.10: IkB kinase +EC 2.7.11.11: cAMP-dependent protein kinase +EC 2.7.11.12: cGMP-dependent protein kinase +EC 2.7.11.13: protein kinase C +EC 2.7.11.14: rhodopsin kinase +EC 2.7.11.15: β-adrenergic-receptor kinase +EC 2.7.11.16: G-protein-coupled receptor kinase +EC 2.7.11.17: Ca2+/calmodulin-dependent protein kinase +EC 2.7.11.18: myosin-light-chain kinase +EC 2.7.11.19: phosphorylase kinase +EC 2.7.11.20: elongation factor 2 kinase +EC 2.7.11.21: polo kinase +EC 2.7.11.22: cyclin-dependent kinase +EC 2.7.11.23: [RNA-polymerase]-subunit kinase +EC 2.7.11.24: mitogen-activated protein kinase +EC 2.7.11.25: mitogen-activated protein kinase kinase kinase +EC 2.7.11.26: tau-protein kinase +EC 2.7.11.27: [acetyl-CoA carboxylase] kinase +EC 2.7.11.28: tropomyosin kinase +EC 2.7.11.29: low-density-lipoprotein receptor kinase +EC 2.7.11.30: receptor protein serine/threonine kinase +EC 2.7.11.31: [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase +EC 2.7.11.32: [pyruvate, phosphate dikinase] kinase +EC 2.7.11.33: [pyruvate, water dikinase] kinase + +=== EC 2.7.12: Dual-specificity kinases (those acting on Ser/Thr and Tyr residues) === +EC 2.7.12.1: dual-specificity kinase +EC 2.7.12.2: mitogen-activated protein kinase kinase + +=== EC 2.7.13: Protein-histidine kinases === +EC 2.7.13.1: protein-histidine pros-kinase +EC 2.7.13.2: protein-histidine tele-kinase +EC 2.7.13.3: histidine kinase + +=== EC 2.7.14: Protein-arginine kinases === +EC 2.7.14.1: protein arginine kinase + +=== EC 2.7.99: Other protein kinases === +EC 2.7.99.1: triphosphate—protein phosphotransferase + +== EC 2.8: Transferring Sulfur-Containing Groups == + +=== EC 2.8.1: Sulfurtransferases === +EC 2.8.1.1: thiosulfate sulfurtransferase +EC 2.8.1.2: 3-mercaptopyruvate sulfurtransferase +EC 2.8.1.3: thiosulfate—thiol sulfurtransferase +EC 2.8.1.4: tRNA sulfurtransferase +EC 2.8.1.5: thiosulfate—dithiol sulfurtransferase +EC 2.8.1.6: biotin synthase +EC 2.8.1.7: cysteine desulfurase +EC 2.8.1.8: lipoyl synthase +EC 2.8.1.9: molybdenum cofactor sulfurtransferase +EC 2.8.1.10: thiazole synthase +EC 2.8.1.11: molybdopterin synthase sulfurtransferase +EC 2.8.1.12: molybdopterin synthase +EC 2.8.1.13: tRNA-uridine 2-sulfurtransferase +EC 2.8.1.14: tRNA-5-taurinomethyluridine 2-sulfurtransferase +EC 2.8.1.15: tRNA-5-methyluridine54 2-sulfurtransferase +EC 2.8.1.16: L-aspartate semialdehyde sulfurtransferase + +=== EC 2.8.2: Sulfotransferases === +EC 2.8.2.1: aryl sulfotransferase +EC 2.8.2.2: alcohol sulfotransferase +EC 2.8.2.3: amine sulfotransferase +EC 2.8.2.4: estrone sulfotransferase +EC 2.8.2.5: chondroitin 4-sulfotransferase +EC 2.8.2.6: choline sulfotransferase +EC 2.8.2.7: UDP-N-acetylgalactosamine-4-sulfate sulfotransferase +EC 2.8.2.8: [heparan sulfate]-glucosamine N-sulfotransferase +EC 2.8.2.9: tyrosine-ester sulfotransferase +EC 2.8.2.10: Renilla-luciferin sulfotransferase +EC 2.8.2.11: galactosylceramide sulfotransferase +EC 2.8.2.12: deleted, identical to EC 2.8.2.8, [heparan sulfate]-glucosamine N-sulfotransferase +EC 2.8.2.13: psychosine sulfotransferase +EC 2.8.2.14: bile salt sulfotransferase +EC 2.8.2.15: steroid sulfotransferase +EC 2.8.2.16: thiol sulfotransferase +EC 2.8.2.17: chondroitin 6-sulfotransferase +EC 2.8.2.18: cortisol sulfotransferase +EC 2.8.2.19: triglucosylalkylacylglycerol sulfotransferase +EC 2.8.2.20: protein-tyrosine sulfotransferase +EC 2.8.2.21: keratan sulfotransferase +EC 2.8.2.22: aryl-sulfate sulfotransferase +EC 2.8.2.23: [heparan sulfate]-glucosamine 3-sulfotransferase 1 +EC 2.8.2.24: desulfoglucosinolate sulfotransferase +EC 2.8.2.25: flavonol 3-sulfotransferase +EC 2.8.2.26: quercetin-3-sulfate 3′-sulfotransferase +EC 2.8.2.27: quercetin-3-sulfate 4′-sulfotransferase +EC 2.8.2.28: quercetin-3,3′-bissulfate 7-sulfotransferase +EC 2.8.2.29: [heparan sulfate]-glucosamine 3-sulfotransferase 2 +EC 2.8.2.30: [heparan sulfate]-glucosamine 3-sulfotransferase 3 +EC 2.8.2.31: petromyzonol sulfotransferase +EC 2.8.2.32: scymnol sulfotransferase +EC 2.8.2.33: N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase +EC 2.8.2.34: glycochenodeoxycholate sulfotransferase +EC 2.8.2.35: dermatan 4-sulfotransferase +EC 2.8.2.36: desulfo-A47934 sulfotransferase +EC 2.8.2.37: trehalose 2-sulfotransferase +EC 2.8.2.38: aliphatic desulfoglucosinolate sulfotransferase +EC 2.8.2.39: hydroxyjasmonate sulfotransferase +EC 2.8.2.40: ω-hydroxy-β-dihydromenaquinone-9 sulfotransferase + +=== EC 2.8.3: CoA-transferases === +EC 2.8.3.1: propionate CoA-transferase +EC 2.8.3.2: oxalate CoA-transferase +EC 2.8.3.3: malonate CoA-transferase +EC 2.8.3.4: deleted +EC 2.8.3.5: 3-oxoacid CoA-transferase +EC 2.8.3.6: 3-oxoadipate CoA-transferase +EC 2.8.3.7: The activity is due to two enzymes, EC 2.8.3.22, succinyl-CoA—L-malate CoA-transferase and EC 2.8.3.20, succinyl-CoA—Dcitramalate CoA-transferase +EC 2.8.3.8: acetate CoA-transferase +EC 2.8.3.9: butyrate—acetoacetate CoA-transferase +EC 2.8.3.10: citrate CoA-transferase +EC 2.8.3.11: citramalate CoA-transferase +EC 2.8.3.12: glutaconate CoA-transferase +EC 2.8.3.13: succinate—hydroxymethylglutarate CoA-transferase +EC 2.8.3.14: 5-hydroxypentanoate CoA-transferase +EC 2.8.3.15: succinyl-CoA:(R)-benzylsuccinate CoA-transferase +EC 2.8.3.16: formyl-CoA transferase +EC 2.8.3.17: cinnamoyl-CoA:phenyllactate CoA-transferase +EC 2.8.3.18: succinyl-CoA:acetate CoA-transferase +EC 2.8.3.19: CoA:oxalate CoA-transferase +EC 2.8.3.20: succinyl-CoA—D-citramalate CoA-transferase +EC 2.8.3.21: L-carnitine CoA-transferase +EC 2.8.3.22: succinyl-CoA—L-malate CoA-transferase +EC 2.8.3.23: caffeate CoA-transferase +EC 2.8.3.24: (''R'')-2-hydroxy-4-methylpentanoate CoA-transferase +EC 2.8.3.25: bile acid CoA-transferase +EC 2.8.3.26: succinyl-CoA:mesaconate CoA transferase + +=== EC 2.8.4: Transferring alkylthio groups === +EC 2.8.4.1: coenzyme-B sulfoethylthiotransferase +EC 2.8.4.2: arsenate-mycothiol transferase +EC 2.8.4.3: tRNA-2-methylthio-N6-dimethylallyladenosine synthase +EC 2.8.4.4: [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase +EC 2.8.4.5: tRNA (N6-L-threonylcarbamoyladenosine37-C2)-methylthiotransferase + +=== EC 2.8.5: Thiosulfotransferases === +EC 2.8.5.1: S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent) +EC 2.8.5.2: L-cysteine S-thiosulfotransferase + +== EC 2.9: Transferring Selenium-Containing Groups == + +=== EC 2.9.1: Selenotransferases === +EC 2.9.1.1: L-seryl-tRNASec selenium transferase +EC 2.9.1.2: O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase +EC 2.9.1.3: tRNA 2-selenouridine synthase + +== EC 2.10: Transferring molybdenum- or tungsten-containing groups == + +=== EC 2.10.1: Molybdenumtransferases or tungstentransferases with sulfide groups as acceptors === +EC 2.10.1.1: molybdopterin molybdotransferase + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-2.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-2.md new file mode 100644 index 000000000..7737f8294 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-2.md @@ -0,0 +1,31 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 3/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +Now known to have the activity of EC 2.1.1.359, [histone H3]-lysine36 N-trimethyltransferase. EC 2.1.1.359: [histone H3]-lysine36 N-trimethyltransferase +EC 2.1.1.360: [histone H3]-lysine79 N-trimethyltransferase +EC 2.1.1.361: [histone H4]-lysine20 N-methyltransferase +EC 2.1.1.362: [histone H4]-N-methyl-L-lysine20 N-methyltransferase +EC 2.1.1.363: pre-sodorifen synthase +EC 2.1.1.364: [histone H3]-lysine4 N-methyltransferase +EC 2.1.1.365: MMP 1-O-methyltransferase +EC 2.1.1.366: [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase +EC 2.1.1.367: [histone H3]-lysine9 N-methyltransferase +EC 2.1.1.368: [histone H3]-lysine9 N-dimethyltransferase +EC 2.1.1.369: [histone H3]-lysine27 N-methyltransferase +EC 2.1.1.370: [histone H3]-lysine4 N-dimethyltransferase +EC 2.1.1.371: [histone H3]-lysine27 N-dimethyltransferase +EC 2.1.1.372: [histone H4]-lysine20 N-trimethyltransferase +EC 2.1.1.373: 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase +EC 2.1.1.374: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase +EC 2.1.1.375: NNS virus cap methyltransferase +EC 2.1.1.376: glycine betaine—corrinoid protein Co-methyltransferase +EC 2.1.1.377: [methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase +EC 2.1.1.378: [methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase +EC 2.1.1.379: [methyl coenzyme M reductase]-L-arginine C-5-methyltransferase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-3.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-3.md new file mode 100644 index 000000000..410c7baba --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-3.md @@ -0,0 +1,69 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 4/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.1.2: Hydroxymethyl-, Formyl- and Related Transferases === +EC 2.1.2.1: glycine hydroxymethyltransferase +EC 2.1.2.2: phosphoribosylglycinamide formyltransferase 1 +EC 2.1.2.3: phosphoribosylaminoimidazolecarboxamide formyltransferase +EC 2.1.2.4: glycine formimidoyltransferase +EC 2.1.2.5: glutamate formiminotransferase +EC 2.1.2.6: deleted, included in EC 2.1.2.5 +EC 2.1.2.7: D-alanine 2-hydroxymethyltransferase +EC 2.1.2.8: deoxycytidylate 5-hydroxymethyltransferase +EC 2.1.2.9: methionyl-tRNA formyltransferase +EC 2.1.2.10: aminomethyltransferase +EC 2.1.2.11: 3-methyl-2-oxobutanoate hydroxymethyltransferase +EC 2.1.2.12: now EC 2.1.1.74 +EC 2.1.2.13: UDP-4-amino-4-deoxy-L-arabinose formyltransferase +EC 2.1.2.14: GDP-perosamine N-formyltransferase + +=== EC 2.1.3: Carboxy- and Carbamoyltransferases === +EC 2.1.3.1: methylmalonyl-CoA carboxytransferase +EC 2.1.3.2: aspartate carbamoyltransferase +EC 2.1.3.3: ornithine carbamoyltransferase +EC 2.1.3.4: deleted +EC 2.1.3.5: oxamate carbamoyltransferase +EC 2.1.3.6: putrescine carbamoyltransferase +EC 2.1.3.7: 3-hydroxymethylcephem carbamoyltransferase +EC 2.1.3.8: lysine carbamoyltransferase +EC 2.1.3.9: N-acetylornithine carbamoyltransferase +EC 2.1.3.10: malonyl-S-ACP:biotin-protein carboxyltransferase +EC 2.1.3.11: N-succinylornithine carbamoyltransferase +EC 2.1.3.13: [[The enzyme has been replaced by EC 6.1.2.2]] +EC 2.1.3.14: [[The enzyme has been replaced by EC 6.1.2.2]] +EC 2.1.3.15: acetyl-CoA carboxytransferase + +=== EC 2.1.4: Amidinotransferases === +EC 2.1.4.1: glycine amidinotransferase +EC 2.1.4.2: scyllo-inosamine-4-phosphate amidinotransferase +EC 2.1.4.3: L-arginine:L-lysine amidinotransferase + +=== EC 2.1.5: Methylenetransferases === +EC 2.1.5.1: sesamin methylene transferase + +== EC 2.2: Transferring Aldehyde or Ketonic Groups == + +=== EC 2.2.1: Transketolases and Transaldolases === +EC 2.2.1.1: transketolase +EC 2.2.1.2: transaldolase +EC 2.2.1.3: formaldehyde transketolase +EC 2.2.1.4: acetoin—ribose-5-phosphate transaldolase +EC 2.2.1.5: 2-hydroxy-3-oxoadipate synthase +EC 2.2.1.6: acetolactate synthase +EC 2.2.1.7: 1-deoxy-D-xylulose-5-phosphate synthase +EC 2.2.1.8: fluorothreonine transaldolase +EC 2.2.1.9: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase +EC 2.2.1.10: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase +EC 2.2.1.11: 6-deoxy-5-ketofructose 1-phosphate synthase +EC 2.2.1.12: 3-acetyloctanal synthase +EC 2.2.1.13: apulose-4-phosphate transketolase +EC 2.2.1.14: 6-deoxy-6-sulfo-D-fructose transaldolase + +== EC 2.3: Acyltransferases == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-4.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-4.md new file mode 100644 index 000000000..44fef2f36 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-4.md @@ -0,0 +1,315 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 5/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.3.1: Transferring groups other than amino-acyl groups === +EC 2.3.1.1: amino-acid N-acetyltransferase +EC 2.3.1.2: imidazole N-acetyltransferase +EC 2.3.1.3: glucosamine N-acetyltransferase +EC 2.3.1.4: glucosamine-phosphate N-acetyltransferase +EC 2.3.1.5: arylamine N-acetyltransferase +EC 2.3.1.6: choline O-acetyltransferase +EC 2.3.1.7: carnitine O-acetyltransferase +EC 2.3.1.8: phosphate acetyltransferase +EC 2.3.1.9: acetyl-CoA C-acetyltransferase +EC 2.3.1.10: hydrogen-sulfide S-acetyltransferase +EC 2.3.1.11: thioethanolamine S-acetyltransferase +EC 2.3.1.12: dihydrolipoyllysine-residue acetyltransferase +EC 2.3.1.13: glycine N-acyltransferase +EC 2.3.1.14: glutamine N-phenylacetyltransferase +EC 2.3.1.15: glycerol-3-phosphate O-acyltransferase +EC 2.3.1.16: acetyl-CoA C-acyltransferase +EC 2.3.1.17: aspartate N-acetyltransferase +EC 2.3.1.18: galactoside O-acetyltransferase +EC 2.3.1.19: phosphate butyryltransferase +EC 2.3.1.20: diacylglycerol O-acyltransferase +EC 2.3.1.21: carnitine O-palmitoyltransferase +EC 2.3.1.22: 2-acylglycerol O-acyltransferase +EC 2.3.1.23: 1-acylglycerophosphocholine O-acyltransferase +EC 2.3.1.24: sphingosine N-acyltransferase +EC 2.3.1.25: plasmalogen synthase +EC 2.3.1.26: sterol O-acyltransferase +EC 2.3.1.27: cortisol O-acetyltransferase +EC 2.3.1.28: chloramphenicol O-acetyltransferase +EC 2.3.1.29: glycine C-acetyltransferase +EC 2.3.1.30: serine O-acetyltransferase +EC 2.3.1.31: homoserine O-acetyltransferase +EC 2.3.1.32: lysine N-acetyltransferase +EC 2.3.1.33: histidine N-acetyltransferase +EC 2.3.1.34: D-tryptophan N-acetyltransferase +EC 2.3.1.35: glutamate N-acetyltransferase +EC 2.3.1.36: D-amino-acid N-acetyltransferase +EC 2.3.1.37: 5-aminolevulinate synthase +EC 2.3.1.38: [acyl-carrier-protein] S-acetyltransferase +EC 2.3.1.39: [acyl-carrier-protein] S-malonyltransferase +EC 2.3.1.40: acyl-[acyl-carrier-protein]—phospholipid O-acyltransferase +EC 2.3.1.41: β-ketoacyl-[acyl-carrier-protein] synthase I +EC 2.3.1.42: glycerone-phosphate O-acyltransferase +EC 2.3.1.43: phosphatidylcholine—sterol O-acyltransferase +EC 2.3.1.44: N-acetylneuraminate 4-O-acetyltransferase +EC 2.3.1.45: N-acetylneuraminate 7-O(or 9-O)-acetyltransferase +EC 2.3.1.46: homoserine O-succinyltransferase +EC 2.3.1.47: 8-amino-7-oxononanoate synthase +EC 2.3.1.48: histone acetyltransferase +EC 2.3.1.49: deacetyl-(citrate-(pro-3S)-lyase) S-acetyltransferase +EC 2.3.1.50: serine C-palmitoyltransferase +EC 2.3.1.51: 1-acylglycerol-3-phosphate O-acyltransferase +EC 2.3.1.52: 2-acylglycerol-3-phosphate O-acyltransferase +EC 2.3.1.53: phenylalanine N-acetyltransferase +EC 2.3.1.54: formate C-acetyltransferase +EC 2.3.1.55: [[identical to EC 2.3.1.82]] +EC 2.3.1.56: aromatic-hydroxylamine O-acetyltransferase +EC 2.3.1.57: diamine N-acetyltransferase +EC 2.3.1.58: 2,3-diaminopropionate N-oxalyltransferase +EC 2.3.1.59: gentamicin 2′-N-acetyltransferase +EC 2.3.1.60: gentamicin 3′-N-acetyltransferase +EC 2.3.1.61: dihydrolipoyllysine-residue succinyltransferase +EC 2.3.1.62: 2-acylglycerophosphocholine O-acyltransferase +EC 2.3.1.63: 1-alkylglycerophosphocholine O-acyltransferase +EC 2.3.1.64: agmatine N4-coumaroyltransferase +EC 2.3.1.65: bile acid-CoA:amino acid N-acyltransferase +EC 2.3.1.66: leucine N-acetyltransferase +EC 2.3.1.67: 1-alkylglycerophosphocholine O-acetyltransferase +EC 2.3.1.68: glutamine N-acyltransferase +EC 2.3.1.69: monoterpenol O-acetyltransferase +EC 2.3.1.70: deleted +EC 2.3.1.71: glycine N-benzoyltransferase +EC 2.3.1.72: indoleacetylglucose—inositol O-acyltransferase +EC 2.3.1.73: diacylglycerol—sterol O-acyltransferase +EC 2.3.1.74: chalcone synthase +EC 2.3.1.75: long-chain-alcohol O-fatty-acyltransferase +EC 2.3.1.76: retinol O-fatty-acyltransferase +EC 2.3.1.77: triacylglycerol—sterol O-acyltransferase +EC 2.3.1.78: heparan-α-glucosaminide N-acetyltransferase +EC 2.3.1.79: maltose O-acetyltransferase +EC 2.3.1.80: cysteine-S-conjugate N-acetyltransferase +EC 2.3.1.81: aminoglycoside 3-N-acetyltransferase +EC 2.3.1.82: aminoglycoside 6′-N-acetyltransferase +EC 2.3.1.83: phosphatidylcholine—dolichol O-acyltransferase +EC 2.3.1.84: alcohol O-acetyltransferase +EC 2.3.1.85: fatty-acid synthase system +EC 2.3.1.86: fatty-acyl-CoA synthase system +EC 2.3.1.87: aralkylamine N-acetyltransferase +EC 2.3.1.88: Now covered by EC 2.3.1.254, EC 2.3.1.255, EC 2.3.1.256, EC 2.3.1.257, EC 2.3.1.258 and EC 2.3.1.259 +EC 2.3.1.89: tetrahydrodipicolinate N-acetyltransferase +EC 2.3.1.90: β-glucogallin O-galloyltransferase +EC 2.3.1.91: sinapoylglucose—choline O-sinapoyltransferase +EC 2.3.1.92: sinapoylglucose—malate O-sinapoyltransferase +EC 2.3.1.93: 13-hydroxylupinine O-tigloyltransferase +EC 2.3.1.94: 6-deoxyerythronolide-B synthase +EC 2.3.1.95: trihydroxystilbene synthase +EC 2.3.1.96: glycoprotein N-palmitoyltransferase +EC 2.3.1.97: glycylpeptide N-tetradecanoyltransferase +EC 2.3.1.98: chlorogenate—glucarate O-hydroxycinnamoyltransferase +EC 2.3.1.99: quinate O-hydroxycinnamoyltransferase +EC 2.3.1.100: [myelin-proteolipid] O-palmitoyltransferase +EC 2.3.1.101: formyl|methanofuran—tetrahydromethanopterin N-formyltransferase +EC 2.3.1.102: N6-hydroxylysine O-acetyltransferase +EC 2.3.1.103: sinapoylglucose—sinapoylglucose O-sinapoyltransferase +EC 2.3.1.104: The activity is covered by EC 2.3.1.25 +EC 2.3.1.105: alkylglycerophosphate 2-O-acetyltransferase +EC 2.3.1.106: tartronate O-hydroxycinnamoyltransferase +EC 2.3.1.107: deacetylvindoline O-acetyltransferase +EC 2.3.1.108: α-tubulin N-acetyltransferase +EC 2.3.1.109: arginine N-succinyltransferase +EC 2.3.1.110: tyramine N-feruloyltransferase +EC 2.3.1.111: mycocerosate synthase +EC 2.3.1.112: D-tryptophan N-malonyltransferase +EC 2.3.1.113: anthranilate N-malonyltransferase +EC 2.3.1.114: 3,4-dichloroaniline N-malonyltransferase +EC 2.3.1.115: isoflavone-7-O-β-glucoside 6′′-O-malonyltransferase +EC 2.3.1.116: lavonol-3-O-β-glucoside O-malonyltransferase +EC 2.3.1.117: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase +EC 2.3.1.118: N-hydroxyarylamine O-acetyltransferase +EC 2.3.1.119: Now covered by EC 2.3.1.199, EC 1.1.1.330, EC 4.2.1.134 and EC 1.3.1.93 +EC 2.3.1.120: [[The reaction is due to EC 2.3.1.74]] +EC 2.3.1.121: 1-alkenylglycerophosphoethanolamine O-acyltransferase +EC 2.3.1.122: trehalose O-mycolyltransferase +EC 2.3.1.123: dolichol O-acyltransferase +EC 2.3.1.124: [[Already listed as EC 2.3.1.20]] +EC 2.3.1.125: 1-alkyl-2-acetylglycerol O-acyltransferase +EC 2.3.1.126: isocitrate O-dihydroxycinnamoyltransferase +EC 2.3.1.127: ornithine N-benzoyltransferase +EC 2.3.1.128: now classified as EC 2.3.1.266 and EC 2.3.1.267 +EC 2.3.1.129: acyl-[acyl-carrier-protein]—UDP-N-acetylglucosamine O-acyltransferase +EC 2.3.1.130: galactarate O-hydroxycinnamoyltransferase +EC 2.3.1.131: glucarate O-hydroxycinnamoyltransferase +EC 2.3.1.132: glucarolactone O-hydroxycinnamoyltransferase +EC 2.3.1.133: shikimate O-hydroxycinnamoyltransferase +EC 2.3.1.134: galactolipid O-acyltransferase +EC 2.3.1.135: phosphatidylcholine—retinol O-acyltransferase +EC 2.3.1.136: polysialic-acid O-acetyltransferase +EC 2.3.1.137: carnitine O-octanoyltransferase +EC 2.3.1.138: putrescine N-hydroxycinnamoyltransferase +EC 2.3.1.139: ecdysone O-acyltransferase +EC 2.3.1.140: rosmarinate synthase +EC 2.3.1.141: galactosylacylglycerol O-acyltransferase +EC 2.3.1.142: glycoprotein O-fatty-acyltransferase +EC 2.3.1.143: β-glucogallin—tetrakisgalloylglucose O-galloyltransferase +EC 2.3.1.144: anthranilate N-benzoyltransferase +EC 2.3.1.145: piperidine N-piperoyltransferase +EC 2.3.1.146: pinosylvin synthase +EC 2.3.1.147: glycerophospholipid arachidonoyl-transferase (CoA-independent) +EC 2.3.1.148: glycerophospholipid acyltransferase (CoA-dependent) +EC 2.3.1.149: platelet-activating factor acetyltransferase +EC 2.3.1.150: salutaridinol 7-O-acetyltransferase +EC 2.3.1.151: 2,3′,4,6-tetrahydroxybenzophenone synthase +EC 2.3.1.152: alcohol O-cinnamoyltransferase +EC 2.3.1.153: anthocyanin 5-(6′′′-hydroxycinnamoyltransferase) +EC 2.3.1.154: Now EC 2.3.1.176 +EC 2.3.1.155: acetyl-CoA C-myristoyltransferase +EC 2.3.1.156: phloroisovalerophenone synthase +EC 2.3.1.157: glucosamine-1-phosphate N-acetyltransferase +EC 2.3.1.158: phospholipid:diacylglycerol acyltransferase +EC 2.3.1.159: acridone synthase +EC 2.3.1.160: vinorine synthase +EC 2.3.1.161: lovastatin nonaketide synthase +EC 2.3.1.162: taxadien-5α-ol O-acetyltransferase +EC 2.3.1.163: 10-hydroxytaxane O-acetyltransferase +EC 2.3.1.164: isopenicillin-N N-acyltransferase +EC 2.3.1.165: 6-methylsalicylic acid synthase +EC 2.3.1.166: 2α-hydroxytaxane 2-O-benzoyltransferase +EC 2.3.1.167: 10-deacetylbaccatin III 10-O-acetyltransferase +EC 2.3.1.168: dihydrolipoyllysine-residue (2-methylpropanoyl)transferase +EC 2.3.1.169: CO-methylating acetyl-CoA synthase +EC 2.3.1.170: 6′-deoxychalcone synthase +EC 2.3.1.171: anthocyanin 6′′-O-malonyltransferase +EC 2.3.1.172: anthocyanin 5-O-glucoside 6′′′-O-malonyltransferase +EC 2.3.1.173: flavonol-3-O-triglucoside O-coumaroyltransferase +EC 2.3.1.174: 3-oxoadipyl-CoA thiolase +EC 2.3.1.175: deacetylcephalosporin-C acetyltransferase +EC 2.3.1.176: propanoyl-CoA C-acyltransferase +EC 2.3.1.177: 3,5-dihydroxybiphenyl synthase +EC 2.3.1.178: diaminobutyrate acetyltransferase +EC 2.3.1.179: β-ketoacyl-[acyl-carrier-protein] synthase II +EC 2.3.1.180: β-ketoacyl-[acyl-carrier-protein] synthase III +EC 2.3.1.181: lipoyl(octanoyl) transferase +EC 2.3.1.182: (R)-citramalate synthase +EC 2.3.1.183: phosphinothricin acetyltransferase +EC 2.3.1.184: acyl-homoserine-lactone synthase +EC 2.3.1.185: tropine acyltransferase +EC 2.3.1.186: pseudotropine acyltransferase +EC 2.3.1.187: acetyl-S-ACP:malonate ACP transferase +EC 2.3.1.188: ω-hydroxypalmitate O-feruloyl transferase +EC 2.3.1.189: mycothiol synthase +EC 2.3.1.190: acetoin dehydrogenase +EC 2.3.1.191: UDP-3-O-(3-hydroxyacyl)glucosamine N-acyltransferase +EC 2.3.1.192: glycine N-phenylacetyltransferase +EC 2.3.1.193: tRNAMetcytidine acetyltransferase +EC 2.3.1.194: acetoacetyl-CoA synthase +EC 2.3.1.195: (Z)-3-hexen-1-ol acetyltransferase +EC 2.3.1.196: benzyl alcohol O-benzoyltransferase +EC 2.3.1.197: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose 3-N-acetyltransferase +EC 2.3.1.198: glycerol-3-phosphate 2-O-acyltransferase +EC 2.3.1.199: very-long-chain 3-oxoacyl-CoA synthase +EC 2.3.1.200: lipoyl amidotransferase +EC 2.3.1.201: UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase +EC 2.3.1.202: UDP-4-amino-4,6-dideoxy-N-acetyl-β-L-altrosamine N-acetyltransferase +EC 2.3.1.203: UDP-N-acetylbacillosamine N-acetyltransferase +EC 2.3.1.204: octanoyl-[GcvH]:protein N-octanoyltransferase +EC 2.3.1.205: fumigaclavine B O-acetyltransferase +EC 2.3.1.206: 3,5,7-trioxododecanoyl-CoA synthase +EC 2.3.1.207: β-ketodecanoyl-[acyl-carrier-protein] synthase +EC 2.3.1.208: 4-hydroxycoumarin synthase +EC 2.3.1.209: dTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase +EC 2.3.1.210: dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase +EC 2.3.1.211: bisdemethoxycurcumin synthase +EC 2.3.1.212: benzalacetone synthase +EC 2.3.1.213: cyanidin 3-O-(6-O-glucosyl-2-O-xylosylgalactoside) 6′′′-O-hydroxycinnamoyltransferase +EC 2.3.1.214: pelargonidin 3-O-(6-caffeoylglucoside) 5-O-(6-O-malonylglucoside) 4′′′-malonyltransferase +EC 2.3.1.215: anthocyanidin 3-O-glucoside 6′′-O-acyltransferase +EC 2.3.1.216: 5,7-dihydroxy-2-methylchromone synthase +EC 2.3.1.217: curcumin synthase +EC 2.3.1.218: phenylpropanoylacetyl-CoA synthase +EC 2.3.1.219: demethoxycurcumin synthase +EC 2.3.1.220: 2,4,6-trihydroxybenzophenone synthase +EC 2.3.1.221: noranthrone synthase +EC 2.3.1.222: phosphate propanoyltransferase +EC 2.3.1.223: 3-oxo-5,6-didehydrosuberyl-CoA thiolase +EC 2.3.1.224: acetyl-CoA-benzylalcohol acetyltransferase +EC 2.3.1.225: protein S-acyltransferase +EC 2.3.1.226: carboxymethylproline synthase +EC 2.3.1.227: GDP-perosamine N-acetyltransferase +EC 2.3.1.228: isovaleryl-homoserine lactone synthase +EC 2.3.1.229: 4-coumaroyl-homoserine lactone synthase +EC 2.3.1.230: 2-heptyl-4(1H)-quinolone synthase +EC 2.3.1.231: tRNAPhe {7-[3-amino-3-(methoxycarbonyl)propyl]wyosine37 -N}-methoxycarbonyltransferase +EC 2.3.1.232: methanol O-anthraniloyltransferase +EC 2.3.1.233: 1,3,6,8-tetrahydroxynaphthalene synthase +EC 2.3.1.234: N6-L-threonylcarbamoyladenine synthase +EC 2.3.1.235: tetracenomycin F2 synthase +EC 2.3.1.236: 5-methylnaphthoic acid synthase +EC 2.3.1.237: neocarzinostatin naphthoate synthase +EC 2.3.1.238: monacolin J acid methylbutanoate transferase +EC 2.3.1.239: 10-deoxymethynolide synthase +EC 2.3.1.240: narbonolide synthase +EC 2.3.1.241: Kdo2-lipid IVA lauroyltransferase +EC 2.3.1.242: Kdo2-lipid IVA palmitoleoyltransferase +EC 2.3.1.243: lauroyl-Kdo2-lipid IVA myristoyltransferase +EC 2.3.1.244: 2-methylbutanoate polyketide synthase +EC 2.3.1.245: 3-hydroxy-5-phosphooxypentane-2,4-dione thiolase +EC 2.3.1.246: 3,5-dihydroxyphenylacetyl-CoA synthase +EC 2.3.1.247: 3-keto-5-aminohexanoate cleavage enzyme +EC 2.3.1.248: spermidine disinapoyl transferase +EC 2.3.1.249: spermidine dicoumaroyl transferase +EC 2.3.1.250: [Wnt protein] O-palmitoleoyl transferase +EC 2.3.1.251: lipid IVA palmitoyltransferase +EC 2.3.1.252: mycolipanoate synthase +EC 2.3.1.253: phloroglucinol synthase +EC 2.3.1.254: N-terminal methionine Nα-acetyltransferase NatB +EC 2.3.1.255: N-terminal amino-acid Nα-acetyltransferase NatA +EC 2.3.1.256: N-terminal methionine Nα-acetyltransferase NatC +EC 2.3.1.257: N-terminal L-serine Nα-acetyltransferase NatD +EC 2.3.1.258: N-terminal methionine Nα-acetyltransferase NatE +EC 2.3.1.259: N-terminal methionine Nα-acetyltransferase NatF +EC 2.3.1.260: tetracycline polyketide synthase +EC 2.3.1.261: (4-hydroxyphenyl)alkanoate synthase +EC 2.3.1.262: anthraniloyl-CoA anthraniloyltransferase +EC 2.3.1.263: 2-amino-4-oxopentanoate thiolase +EC 2.3.1.264: β-lysine N6-acetyltransferase +EC 2.3.1.265: phosphatidylinositol dimannoside acyltransferase +EC 2.3.1.266: [ribosomal protein S18]-alanine N-acetyltransferase +EC 2.3.1.267: [ribosomal protein S5]-alanine N-acetyltransferase +EC 2.3.1.268: ethanol O-acetyltransferase +EC 2.3.1.269: apolipoprotein N-acyltransferase +EC 2.3.1.270: lyso-ornithine lipid O-acyltransferase +EC 2.3.1.271: L-glutamate-5-semialdehyde N-acetyltransferase +EC 2.3.1.272: 2-acetylphloroglucinol acetyltransferase +EC 2.3.1.273: diglucosylglycerate octanoyltransferase +EC 2.3.1.274: phosphate acyltransferase +EC 2.3.1.275: acyl phosphate:glycerol-3-phosphate acyltransferase +EC 2.3.1.276: galactosamine-1-phosphate N-acetyltransferase +EC 2.3.1.277: 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase +EC 2.3.1.278: mycolipenoyl-CoA—2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase +EC 2.3.1.279: long-chain-acyl-CoA—trehalose acyltransferase +EC 2.3.1.280: (aminoalkyl)phosphonate N-acetyltransferase +EC 2.3.1.281: 5-hydroxydodecatetraenal polyketide synthase +EC 2.3.1.282: phenolphthiocerol/phthiocerol/phthiodiolone dimycocerosyl transferase +EC 2.3.1.283: 2′-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase +EC 2.3.1.284: 3′-(hydroxy)phthioceranyl-2′-palmitoyl(stearoyl)-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase +EC 2.3.1.285: (13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-acetyltransferase +EC 2.3.1.286: protein acetyllysine N-acetyltransferase +EC 2.3.1.287: phthioceranic/hydroxyphthioceranic acid synthase +EC 2.3.1.288: 2-O-sulfo trehalose long-chain-acyltransferase +EC 2.3.1.289: aureothin polyketide synthase system +EC 2.3.1.290: spectinabilin polyketide synthase system +EC 2.3.1.291: sphingoid base N-palmitoyltransferase +EC 2.3.1.292: (phenol)carboxyphthiodiolenone synthase +EC 2.3.1.293: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase I +EC 2.3.1.294: meromycolic acid 3-oxoacyl-(acyl carrier protein) synthase II +EC 2.3.1.295: mycoketide-CoA synthase +EC 2.3.1.296: ω-hydroxyceramide transacylase +EC 2.3.1.297: very-long-chain ceramide synthase +EC 2.3.1.298: ultra-long-chain ceramide synthase +EC 2.3.1.299: sphingoid base N-stearoyltransferase +EC 2.3.1.300: branched-chain β-ketoacyl-[acyl-carrier-protein] synthase +EC 2.3.1.301: mycobacterial β-ketoacyl-[acyl carrier protein] synthase III +EC 2.3.1.302: hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-hydroxycinnamoyltransferase +EC 2.3.1.303: α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und 2IV-O-acetyltransferase +EC 2.3.1.304: poly[(S)-3-hydroxyalkanoate] polymerase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-5.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-5.md new file mode 100644 index 000000000..d1455c3a3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-5.md @@ -0,0 +1,71 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 6/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.3.2: Aminoacyltransferases === +EC 2.3.2.1: D-glutamyltransferase +EC 2.3.2.2: γ-glutamyltransferase +EC 2.3.2.3: lysyltransferase +EC 2.3.2.4: Now classified as EC 4.3.2.9, γ-glutamylcyclotransferase +EC 2.3.2.5: glutaminyl-peptide cyclotransferase +EC 2.3.2.6: leucyltransferase +EC 2.3.2.7: aspartyltransferase +EC 2.3.2.8: arginyltransferase +EC 2.3.2.9: agaritine γ-glutamyltransferase +EC 2.3.2.10: UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase +EC 2.3.2.11: alanylphosphatidylglycerol synthase +EC 2.3.2.12: peptidyltransferase +EC 2.3.2.13: protein-glutamine g-glutamyltransferase +EC 2.3.2.14: D-alanine γ-glutamyltransferase +EC 2.3.2.15: glutathione γ-glutamylcysteinyltransferase +EC 2.3.2.16: lipid II:glycine glycyltransferase +EC 2.3.2.17: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase +EC 2.3.2.18: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase +EC 2.3.2.19: ribostamycin:4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoate transferase +EC 2.3.2.20: cyclo(L-leucyl-L-phenylalanyl) synthase +EC 2.3.2.21: cyclo(L-tyrosyl-L-tyrosyl) synthase +EC 2.3.2.22: cyclo(L-leucyl-L-leucyl) synthase +EC 2.3.2.23: E2 ubiquitin-conjugating enzyme +EC 2.3.2.24: (E3-independent) E2 ubiquitin-conjugating enzyme +EC 2.3.2.25: N-terminal E2 ubiquitin-conjugating enzyme +EC 2.3.2.26: HECT-type E3 ubiquitin transferase +EC 2.3.2.27: RING-type E3 ubiquitin transferase +EC 2.3.2.28: L-allo-isoleucyltransferase +EC 2.3.2.29: aspartate/glutamate leucyltransferase +EC 2.3.2.30: L-ornithine Nα-acyltransferase +EC 2.3.2.31: RBR-type E3 ubiquitin transferase +EC 2.3.2.32: cullin-RING-type E3 NEDD8 transferase +EC 2.3.2.33: RCR-type E3 ubiquitin transferase +EC 2.3.2.34: E2 NEDD8-conjugating enzyme +EC 2.3.2.35: capsaicin synthase +EC 2.3.2.36: RING-type E3 ubiquitin transferase (cysteine targeting) + +=== EC 2.3.3: Acyl groups converted into alkyl on transfer === +EC 2.3.3.1: citrate (Si)-synthase +EC 2.3.3.2: decylcitrate synthase +EC 2.3.3.3: citrate (Re)-synthase +EC 2.3.3.4: decylhomocitrate synthase +EC 2.3.3.5: 2-methylcitrate synthase +EC 2.3.3.6: 2-ethylmalate synthase +EC 2.3.3.7: 3-ethylmalate synthase +EC 2.3.3.8: ATP citrate synthase +EC 2.3.3.9: malate synthase +EC 2.3.3.10: hydroxymethylglutaryl-CoA synthase +EC 2.3.3.11: 2-hydroxyglutarate synthase +EC 2.3.3.12: 3-propylmalate synthase +EC 2.3.3.13: 2-isopropylmalate synthase +EC 2.3.3.14: homocitrate synthase +EC 2.3.3.15: sulfoacetaldehyde acetyltransferase +EC 2.3.3.16: citrate synthase (unknown stereospecificity) +EC 2.3.3.17: methylthioalkylmalate synthase +EC 2.3.3.18: 2-phosphinomethylmalate synthase +EC 2.3.3.19: 2-phosphonomethylmalate synthase +EC 2.3.3.20: acyl-CoA:acyl-CoA alkyltransferase + +== EC 2.4: Glycosyltransferases == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-6.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-6.md new file mode 100644 index 000000000..d81631ad3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-6.md @@ -0,0 +1,318 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 7/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.4.1: Hexosyltransferases === +EC 2.4.1.1: Glycogen phosphorylase +EC 2.4.1.2: dextrin dextranase +EC 2.4.1.3: deleted, included in EC 2.4.1.25 +EC 2.4.1.4: amylosucrase +EC 2.4.1.5: dextransucrase +EC 2.4.1.6: deleted +EC 2.4.1.7: sucrose phosphorylase +EC 2.4.1.8: maltose phosphorylase +EC 2.4.1.9: inulosucrase +EC 2.4.1.10: levansucrase +EC 2.4.1.11: glycogen(starch) synthase +EC 2.4.1.12: cellulose synthase (UDP-forming) +EC 2.4.1.13: sucrose synthase +EC 2.4.1.14: sucrose-phosphate synthase +EC 2.4.1.15: α,α-trehalose-phosphate synthase (UDP-forming) +EC 2.4.1.16: chitin synthase +EC 2.4.1.17: glucuronosyltransferase +EC 2.4.1.18: ,4-α-glucan branching enzyme +EC 2.4.1.19: cyclomaltodextrin glucanotransferase +EC 2.4.1.20: cellobiose phosphorylase +EC 2.4.1.21: starch synthase +EC 2.4.1.22: lactose synthase +EC 2.4.1.23: sphingosine β-galactosyltransferase +EC 2.4.1.24: 1,4-α-glucan 6-α-glucosyltransferase +EC 2.4.1.25: 4-α-glucanotransferase +EC 2.4.1.26: DNA α-glucosyltransferase +EC 2.4.1.27: DNA β-glucosyltransferase +EC 2.4.1.28: glucosyl-DNA β-glucosyltransferase +EC 2.4.1.29: cellulose synthase (GDP-forming) +EC 2.4.1.30: 1,3-β-oligoglucan phosphorylase +EC 2.4.1.31: laminaribiose phosphorylase +EC 2.4.1.32: glucomannan 4-β-mannosyltransferase +EC 2.4.1.33: mannuronan synthase +EC 2.4.1.34: 1,3-β-glucan synthase +EC 2.4.1.35: phenol β-glucosyltransferase +EC 2.4.1.36: α,α-trehalose-phosphate synthase (GDP-forming) +EC 2.4.1.37: fucosylgalactoside 3-α-galactosyltransferase +EC 2.4.1.38: β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase +EC 2.4.1.39: steroid N-acetylglucosaminyltransferase +EC 2.4.1.40: glycoprotein-fucosylgalactoside α-N-acetylgalactosaminyltransferase +EC 2.4.1.41: polypeptide N-acetylgalactosaminyltransferase +EC 2.4.1.42: deleted, included in EC 2.4.1.17 +EC 2.4.1.43: polygalacturonate 4-α-galacturonosyltransferase +EC 2.4.1.44: lipopolysaccharide 3-α-galactosyltransferase +EC 2.4.1.45: now included with EC 2.4.1.47, N-acylsphingosine galactosyltransferase +EC 2.4.1.46: monogalactosyldiacylglycerol synthase +EC 2.4.1.47: N-acylsphingosine galactosyltransferase +EC 2.4.1.48: heteroglycan α-mannosyltransferase +EC 2.4.1.49: cellodextrin phosphorylase +EC 2.4.1.50: procollagen galactosyltransferase +EC 2.4.1.51: now covered by EC 2.4.1.101, EC 2.4.1.143, EC 2.4.1.144 and EC 2.4.1.145 +EC 2.4.1.52: poly(glycerol-phosphate) α-glucosyltransferase +EC 2.4.1.53: poly(ribitol-phosphate) β-glucosyltransferase +EC 2.4.1.54: undecaprenyl-phosphate mannosyltransferase +EC 2.4.1.55: Now EC 2.7.8.14, CDP-ribitol ribitolphosphotransferase +EC 2.4.1.56: lipopolysaccharide N-acetylglucosaminyltransferase +EC 2.4.1.57: Newer studies have shown that this is catalysed by two independent activities now covered by EC 2.4.1.345, phosphatidyl-myo-inositol α-mannosyl transferase and EC 2.4.1.346, phosphatidyl-myo-inositol dimannoside synthase +EC 2.4.1.58: lipopolysaccharide glucosyltransferase I +EC 2.4.1.59: deleted, included in EC 2.4.1.17 +EC 2.4.1.60: CDP-abequose:α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase +EC 2.4.1.61: deleted, included in EC 2.4.1.17 +EC 2.4.1.62: ganglioside galactosyltransferase +EC 2.4.1.63: linamarin synthase +EC 2.4.1.64: α,α-trehalose phosphorylase +EC 2.4.1.65: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase +EC 2.4.1.66: procollagen glucosyltransferase +EC 2.4.1.67: galactinol—raffinose galactosyltransferase +EC 2.4.1.68: glycoprotein 6-α-L-fucosyltransferase +EC 2.4.1.69: type 1 galactoside α-(1,2)-fucosyltransferase +EC 2.4.1.70: poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase +EC 2.4.1.71: arylamine glucosyltransferase +EC 2.4.1.72: now EC 2.4.2.24, 1,4-β-D-xylan synthase +EC 2.4.1.73: lipopolysaccharide glucosyltransferase II +EC 2.4.1.74: glycosaminoglycan galactosyltransferase +EC 2.4.1.75: deleted entry, insufficient evidence to conclude that this is a different enzyme from EC 2.4.1.43 +EC 2.4.1.76: deleted, included in EC 2.4.1.17 +EC 2.4.1.77: deleted, included in EC 2.4.1.17 +EC 2.4.1.78: phosphopolyprenol glucosyltransferase +EC 2.4.1.79: globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase +EC 2.4.1.80: ceramide glucosyltransferase +EC 2.4.1.81: flavone 7-O-β-glucosyltransferase +EC 2.4.1.82: galactinol—sucrose galactosyltransferase +EC 2.4.1.83: dolichyl-phosphate β-D -mannosyltransferase +EC 2.4.1.84: deleted, included in EC 2.4.1.17 +EC 2.4.1.85: cyanohydrin β-glucosyltransferase +EC 2.4.1.86: N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase +EC 2.4.1.87: N-acetyllactosaminide 3-α-galactosyltransferase +EC 2.4.1.88: globoside α-N-acetylgalactosaminyltransferase +EC 2.4.1.89: deleted, included in EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase +EC 2.4.1.90: N-acetyllactosamine synthase +EC 2.4.1.91: flavonol 3-O-glucosyltransferase +EC 2.4.1.92: (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase +EC 2.4.1.93: Now EC 4.2.2.18, inulin fructotransferase (DFA-III-forming) +EC 2.4.1.94: protein N-acetylglucosaminyltransferase +EC 2.4.1.95: bilirubin-glucuronoside glucuronosyltransferase +EC 2.4.1.96: sn-glycerol-3-phosphate 1-galactosyltransferase +EC 2.4.1.97: 1,3-β-D-glucan phosphorylase +EC 2.4.1.98: deleted, Now included with EC 2.4.1.90, N-acetyllactosamine synthase +EC 2.4.1.99: sucrose:sucrose fructosyltransferase +EC 2.4.1.100: 2,1-fructan:2,1-fructan 1-fructosyltransferase +EC 2.4.1.101: α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase +EC 2.4.1.102: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase +EC 2.4.1.103: alizarin 2-β-glucosyltransferase +EC 2.4.1.104: o-dihydroxycoumarin 7-O-glucosyltransferase +EC 2.4.1.105: vitexin β-glucosyltransferase +EC 2.4.1.106: isovitexin β-glucosyltransferase +EC 2.4.1.107: deleted, now included with EC 2.4.1.17, glucuronosyltransferase +EC 2.4.1.108: deleted, now included with EC 2.4.1.17, glucuronosyltransferase +EC 2.4.1.109: dolichyl-phosphate-mannose—protein mannosyltransferase +EC 2.4.1.110: tRNA-queuosine β-mannosyltransferase +EC 2.4.1.111: coniferyl-alcohol glucosyltransferase +EC 2.4.1.112: The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase +EC 2.4.1.113: α-1,4-glucan-protein synthase (ADP-forming) +EC 2.4.1.114: 2-coumarate O-β-glucosyltransferase +EC 2.4.1.115: anthocyanidin 3-O-glucosyltransferase +EC 2.4.1.116: cyanidin 3-O-rutinoside 5-O-glucosyltransferase +EC 2.4.1.117: dolichyl-phosphate β-glucosyltransferase +EC 2.4.1.118: cytokinin 7-β-glucosyltransferase +EC 2.4.1.119: transferred to EC 2.4.99.18, dolichyl-diphosphooligosaccharideprotein glycotransferase +EC 2.4.1.120: sinapate 1-glucosyltransferase +EC 2.4.1.121: indole-3-acetate β-glucosyltransferase +EC 2.4.1.122: N-acetylgalactosaminide β-1,3-galactosyltransferase +EC 2.4.1.123: inositol 3-α-galactosyltransferase +EC 2.4.1.124: Now EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase +EC 2.4.1.125: sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase +EC 2.4.1.126: hydroxycinnamate 4-β-glucosyltransferase +EC 2.4.1.127: monoterpenol β-glucosyltransferase +EC 2.4.1.128: scopoletin glucosyltransferase +EC 2.4.1.129: peptidoglycan glycosyltransferase +EC 2.4.1.130: Now covered by EC 2.4.1.258, EC 2.4.1.259, EC 2.4.1.260 and EC 2.4.1.261 +EC 2.4.1.131: GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase +EC 2.4.1.132: GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase +EC 2.4.1.133: xylosylprotein 4-β-galactosyltransferase +EC 2.4.1.134: galactosylxylosylprotein 3-β-galactosyltransferase +EC 2.4.1.135: galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase +EC 2.4.1.136: gallate 1-β-glucosyltransferase +EC 2.4.1.137: sn-glycerol-3-phosphate 2-α-galactosyltransferase +EC 2.4.1.138: mannotetraose 2-α-N-acetylglucosaminyltransferase +EC 2.4.1.139: maltose synthase +EC 2.4.1.140: alternansucrase +EC 2.4.1.141: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase +EC 2.4.1.142: chitobiosyldiphosphodolichol β-mannosyltransferase +EC 2.4.1.143: α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase +EC 2.4.1.144: β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase +EC 2.4.1.145: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase +EC 2.4.1.146: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase +EC 2.4.1.147: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase +EC 2.4.1.148: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase +EC 2.4.1.149: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase +EC 2.4.1.150: N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase +EC 2.4.1.151: now included with EC 2.4.1.87 N-acetyllactosaminide 3-α-galactosyltransferase +EC 2.4.1.152: 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase +EC 2.4.1.153: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminyltransferase +EC 2.4.1.154: [[identical to EC 2.4.1.79, ((galactosylgalactosylglucosylceramide b-D-acetylgalactosaminyltransferase|globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase))|identical to EC 2.4.1.79, globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase]] +EC 2.4.1.155: α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase +EC 2.4.1.156: indolylacetyl-myo-inositol galactosyltransferase +EC 2.4.1.157: 1,2-diacylglycerol 3-glucosyltransferase, now classified as EC 2.4.1.336, monoglucosyldiacylglycerol synthase, and EC 2.4.1.337, 1,2-diacylglycerol 3-α-glucosyltransferase +EC 2.4.1.158: 13-hydroxydocosanoate 13-β-glucosyltransferase +EC 2.4.1.159: flavonol-3-O-glucoside L-rhamnosyltransferase +EC 2.4.1.160: pyridoxine 5′-O-β-D-glucosyltransferase +EC 2.4.1.161: oligosaccharide 4-α-D-glucosyltransferase +EC 2.4.1.162: aldose β-D-fructosyltransferase +EC 2.4.1.163: now included in EC 2.4.1.149, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase +EC 2.4.1.164: now included with EC 2.4.1.150, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase +EC 2.4.1.165: N-acetylneuraminylgalactosylglucosylceramide β-1,4-N-acetylgalactosaminyltransferase +EC 2.4.1.166: raffinose—raffinose α-galactosyltransferase +EC 2.4.1.167: sucrose 6F-α-galactosyltransferase +EC 2.4.1.168: xyloglucan 4-glucosyltransferase +EC 2.4.1.169: now EC 2.4.2.39, xyloglucan 6-xylosyltransferase +EC 2.4.1.170: isoflavone 7-O-glucosyltransferase +EC 2.4.1.171: methyl-ONN-azoxymethanol β-D-glucosyltransferase +EC 2.4.1.172: salicyl-alcohol β-D-glucosyltransferase +EC 2.4.1.173: sterol 3β-glucosyltransferase +EC 2.4.1.174: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase +EC 2.4.1.175: glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase +EC 2.4.1.176: gibberellin β-D-glucosyltransferase +EC 2.4.1.177: cinnamate β-D-glucosyltransferase +EC 2.4.1.178: hydroxymandelonitrile glucosyltransferase +EC 2.4.1.179: lactosylceramide β-1,3-galactosyltransferase +EC 2.4.1.180: lipopolysaccharide N-acetylmannosaminouronosyltransferase +EC 2.4.1.181: hydroxyanthraquinone glucosyltransferase +EC 2.4.1.182: lipid-A-disaccharide synthase +EC 2.4.1.183: α-1,3-glucan synthase +EC 2.4.1.184: galactolipid galactosyltransferase +EC 2.4.1.185: flavanone 7-O-β-glucosyltransferase +EC 2.4.1.186: glycogenin glucosyltransferase +EC 2.4.1.187: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-β-D-mannosaminyltransferase +EC 2.4.1.188: N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase +EC 2.4.1.189: uteolin 7-O-glucuronosyltransferase +EC 2.4.1.190: luteolin-7-O-glucuronide 2′′-O-glucuronosyltransferase +EC 2.4.1.191: luteolin-7-O-diglucuronide 4′-O-glucuronosyltransferase +EC 2.4.1.192: nuatigenin 3β-glucosyltransferase +EC 2.4.1.193: sarsapogenin 3β-glucosyltransferase +EC 2.4.1.194: 4-hydroxybenzoate 4-O-β-D-glucosyltransferase +EC 2.4.1.195: N-hydroxythioamide S-β-glucosyltransferase +EC 2.4.1.196: nicotinate glucosyltransferase +EC 2.4.1.197: high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase +EC 2.4.1.198: phosphatidylinositol N-acetylglucosaminyltransferase +EC 2.4.1.199: β-mannosylphosphodecaprenol—mannooligosaccharide 6-mannosyltransferase +EC 2.4.1.200: now EC 4.2.2.17, inulin fructotransferase (DFA-I-forming) +EC 2.4.1.201: α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase +EC 2.4.1.202: 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase +EC 2.4.1.203: trans-zeatin O-β-D-glucosyltransferase +EC 2.4.1.204: now EC 2.4.2.40, zeatin O-β-D-xylosyltransferase +EC 2.4.1.205: galactogen 6β-galactosyltransferase +EC 2.4.1.206: lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase +EC 2.4.1.207: xyloglucan:xyloglucosyl transferase +EC 2.4.1.208: diglucosyl diacylglycerol synthase (1,2-linking) +EC 2.4.1.209: cis-p-coumarate glucosyltransferase +EC 2.4.1.210: limonoid glucosyltransferase +EC 2.4.1.211: 1,3-β-galactosyl-N-acetylhexosamine phosphorylase +EC 2.4.1.212: hyaluronan synthase +EC 2.4.1.213: glucosylglycerol-phosphate synthase +EC 2.4.1.214: glycoprotein 3-α-L-fucosyltransferase +EC 2.4.1.215: cis-zeatin O-β-D-glucosyltransferase +EC 2.4.1.216: trehalose 6-phosphate phosphorylase +EC 2.4.1.217: mannosyl-3-phosphoglycerate synthase +EC 2.4.1.218: hydroquinone glucosyltransferase +EC 2.4.1.219: vomilenine glucosyltransferase +EC 2.4.1.220: indoxyl-UDPG glucosyltransferase +EC 2.4.1.221: peptide-O-fucosyltransferase +EC 2.4.1.222: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase +EC 2.4.1.223: glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase +EC 2.4.1.224: glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase +EC 2.4.1.225: N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase +EC 2.4.1.226: N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase +EC 2.4.1.227: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase +EC 2.4.1.228: lactosylceramide 4-α-galactosyltransferase +EC 2.4.1.229: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase +EC 2.4.1.230: kojibiose phosphorylase +EC 2.4.1.231: α,α-trehalose phosphorylase (configuration-retaining) +EC 2.4.1.232: initiation-specific α-1,6-mannosyltransferase +EC 2.4.1.233: deleted: identical to EC 2.4.1.115, anthocyanidin 3-O-glucosyltransferase +EC 2.4.1.234: kaempferol 3-O-galactosyltransferase +EC 2.4.1.235: deleted: identical to EC 2.4.1.116, cyanidin 3-O-rutinoside 5-O-glucosyltransferase +EC 2.4.1.236: flavanone 7-O-glucoside 2′′-O-β-L-rhamnosyltransferase +EC 2.4.1.237: flavonol 7-O-β-glucosyltransferase +EC 2.4.1.238: delphinidin 3,5-di-O-glucoside 3′-O-glucosyltransferase +EC 2.4.1.239: flavonol-3-O-glucoside glucosyltransferase +EC 2.4.1.240: flavonol-3-O-glycoside glucosyltransferase +EC 2.4.1.241: flavonol-3-O-glycoside glucosyltransferase +EC 2.4.1.242: NDP-glucose—starch glucosyltransferase +EC 2.4.1.243: 6G-fructosyltransferase +EC 2.4.1.244: N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase +EC 2.4.1.245: α,α-trehalose synthase +EC 2.4.1.246: mannosylfructose-phosphate synthase +EC 2.4.1.247: β-D-galactosyl-(1→4)-L-rhamnose phosphorylase +EC 2.4.1.248: cycloisomaltooligosaccharide glucanotransferase +EC 2.4.1.249: delphinidin 3′,5′-O-glucosyltransferase +EC 2.4.1.250: D-inositol-3-phosphate glycosyltransferase +EC 2.4.1.251: GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 4-β-mannosyltransferase +EC 2.4.1.252: GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase +EC 2.4.1.253: baicalein 7-O-glucuronosyltransferase +EC 2.4.1.254: cyanidin-3-O-glucoside 2′′-O-glucuronosyltransferase +EC 2.4.1.255: protein O-GlcNAc transferase +EC 2.4.1.256: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase +EC 2.4.1.257: GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase +EC 2.4.1.258: dolichyl-P-Man:Man5GlcNAc2-PP-dolichol α-1,3-mannosyltransferase +EC 2.4.1.259: dolichyl-P-Man:Man6GlcNAc2-PP-dolichol α-1,2-mannosyltransferase +EC 2.4.1.260: dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase +EC 2.4.1.261: dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase +EC 2.4.1.262: soyasapogenol glucuronosyltransferase +EC 2.4.1.263: abscisate β-glucosyltransferase +EC 2.4.1.264: D-Man-α-(1→3)-D-Glc-β-(1→4)-DD-Glc-α-1-diphosphoundecaprenol 2-β-glucuronosyltransferase +EC 2.4.1.265: olichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase +EC 2.4.1.266: glucosyl-3-phosphoglycerate synthase +EC 2.4.1.267: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase +EC 2.4.1.268: glucosylglycerate synthase +EC 2.4.1.269: mannosylglycerate synthase +EC 2.4.1.270: mannosylglucosyl-3-phosphoglycerate synthase +EC 2.4.1.271: crocetin glucosyltransferase +EC 2.4.1.272: soyasapogenol B glucuronide galactosyltransferase +EC 2.4.1.273: soyasaponin III rhamnosyltransferase +EC 2.4.1.274: glucosylceramide β-1,4-galactosyltransferase +EC 2.4.1.275: neolactotriaosylceramide β-1,4-galactosyltransferase +EC 2.4.1.276: zeaxanthin glucosyltransferase +EC 2.4.1.277: glycosyltransferase DesVII +EC 2.4.1.278: desosaminyl transferase EryCIII +EC 2.4.1.279: nigerose phosphorylase +EC 2.4.1.280: N,N′-diacetylchitobiose phosphorylase +EC 2.4.1.281: 4-O-β-D-mannosyl-D-glucose phosphorylase +EC 2.4.1.282: 3-O-α-D-glucosyl-L-rhamnose phosphorylase +EC 2.4.1.283: 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase +EC 2.4.1.284: 2-deoxystreptamine glucosyltransferase +EC 2.4.1.285: UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase +EC 2.4.1.286: chalcone 4′-O-glucosyltransferase +EC 2.4.1.287: rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,4/1,5-galactofuranosyltransferase +EC 2.4.1.288: galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,5/1,6-galactofuranosyltransferase +EC 2.4.1.289: N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase +EC 2.4.1.290: N,N′-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase +EC 2.4.1.291: N-acetylgalactosamine-N,N′-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase +EC 2.4.1.292: GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase +EC 2.4.1.293: GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase +EC 2.4.1.294: cyanidin 3-O-galactosyltransferase +EC 2.4.1.295: anthocyanin 3-O-sambubioside 5-O-glucosyltransferase +EC 2.4.1.296: anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase +EC 2.4.1.297: anthocyanidin 3-O-glucoside 2′′-O-glucosyltransferase +EC 2.4.1.298: anthocyanidin 3-O-glucoside 5-O-glucosyltransferase +EC 2.4.1.299: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose) +EC 2.4.1.300: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose) +EC 2.4.1.301: 2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase +EC 2.4.1.302: L-demethylnoviosyl transferase +EC 2.4.1.303: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase +EC 2.4.1.304: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase +EC 2.4.1.305: UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase +EC 2.4.1.306: UDP-GalNAc:α-D-GalNAc-diphosphoundecaprenol α-1,3-N-acetylgalactosaminyltransferase +EC 2.4.1.307: UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-7.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-7.md new file mode 100644 index 000000000..f40d88605 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-7.md @@ -0,0 +1,88 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 8/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +Now included in EC 2.4.1.122, N-acetylgalactosaminide β-1,3-galactosyltransferase +EC 2.4.1.308: GDP-Fuc:β-D-Gal-1,3-α-D-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,2-fucosyltransferase +EC 2.4.1.309: UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase +EC 2.4.1.310: vancomycin aglycone glucosyltransferase +EC 2.4.1.311: chloroorienticin B synthase +EC 2.4.1.312: protein O-mannose β-1,4-N-acetylglucosaminyltransferase +EC 2.4.1.313: protein O-mannose β-1,3-N-acetylgalactosaminyltransferase +EC 2.4.1.314: ginsenoside Rd glucosyltransferase +EC 2.4.1.315: diglucosyl diacylglycerol synthase (1,6-linking) +EC 2.4.1.316: tylactone mycaminosyltransferase +EC 2.4.1.317: O-mycaminosyltylonolide 6-deoxyallosyltransferase +EC 2.4.1.318: demethyllactenocin mycarosyltransferase +EC 2.4.1.319: β-1,4-mannooligosaccharide phosphorylase +EC 2.4.1.320: 1,4-β-mannosyl-N-acetylglucosamine phosphorylase +EC 2.4.1.321: cellobionic acid phosphorylase +EC 2.4.1.322: devancosaminyl-vancomycin vancosaminetransferase +EC 2.4.1.323: 7-deoxyloganetic acid glucosyltransferase +EC 2.4.1.324: 7-deoxyloganetin glucosyltransferase +EC 2.4.1.325: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase +EC 2.4.1.326: aklavinone 7-L-rhodosaminyltransferase +EC 2.4.1.327: aclacinomycin-T 2-deoxy-L-fucose transferase +EC 2.4.1.328: erythronolide mycarosyltransferase +EC 2.4.1.329: sucrose 6F-phosphate phosphorylase +EC 2.4.1.330: β-D-glucosyl crocetin β-1,6-glucosyltransferase +EC 2.4.1.331: 8-demethyltetracenomycin C L-rhamnosyltransferase +EC 2.4.1.332: 1,2-α-glucosylglycerol phosphorylase +EC 2.4.1.333: 1,2-β-oligoglucan phosphorylase +EC 2.4.1.334: 1,3-α-oligoglucan phosphorylase +EC 2.4.1.335: dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase +EC 2.4.1.336: monoglucosyldiacylglycerol synthase +EC 2.4.1.337: 1,2-diacylglycerol 3-α-glucosyltransferase +EC 2.4.1.338: validoxylamine A glucosyltransferase +EC 2.4.1.339: β-1,2-mannobiose phosphorylase +EC 2.4.1.340: 1,2-β-oligomannan phosphorylase +EC 2.4.1.341: α-1,2-colitosyltransferase +EC 2.4.1.342: α-maltose-1-phosphate synthase +EC 2.4.1.343: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase +EC 2.4.1.344: type 2 galactoside α-(1,2)-fucosyltransferase +EC 2.4.1.345: phosphatidyl-myo-inositol α-mannosyltransferase +EC 2.4.1.346: phosphatidyl-myo-inositol dimannoside synthase +EC 2.4.1.347: α,α-trehalose-phosphate synthase (ADP-forming) +EC 2.4.1.348: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase +EC 2.4.1.349: mannosyl-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase +EC 2.4.1.350: mogroside IE synthase +EC 2.4.1.351: rhamnogalacturonan I rhamnosyltransferase +EC 2.4.1.352: glucosylglycerate phosphorylase +EC 2.4.1.353: sordaricin 6-deoxyaltrosyltransferase +EC 2.4.1.354: (R)-mandelonitrile β-glucosyltransferase +EC 2.4.1.355: poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase +EC 2.4.1.356: glucosyl-dolichyl phosphate glucuronosyltransferase +EC 2.4.1.357: phlorizin synthase +EC 2.4.1.358: acylphloroglucinol glucosyltransferase +EC 2.4.1.359: glucosylglycerol phosphorylase (configuration-retaining) +EC 2.4.1.360: 2-hydroxyflavanone C-glucosyltransferase +EC 2.4.1.361: GDP-mannose:di-myo-inositol-1,3′-phosphate β-1,2-mannosyltransferase +EC 2.4.1.362: α-(1→3) branching sucrase +EC 2.4.1.363: ginsenoside 20-O-glucosyltransferase +EC 2.4.1.364: protopanaxadiol-type ginsenoside 3-O-glucosyltransferase +EC 2.4.1.365: protopanaxadiol-type ginsenoside-3-O-glucoside 2′′-O-glucosyltransferase +EC 2.4.1.366: ginsenoside F1 6-O-glucosyltransferase +EC 2.4.1.367: ginsenoside 6-O-glucosyltransferase +EC 2.4.1.368: oleanolate 3-O-glucosyltransferase +EC 2.4.1.369: enterobactin C-glucosyltransferase +EC 2.4.1.370: inositol phosphorylceramide mannosyltransferase +EC 2.4.1.371: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosylpolymerase +EC 2.4.1.372: mutansucrase +EC 2.4.1.373: α-(1→2) branching sucrase +EC 2.4.1.374: β-1,2-mannooligosaccharide synthase +EC 2.4.1.375: rhamnogalacturonan I galactosyltransferase +EC 2.4.1.376: EGF-domain serine glucosyltransferase +EC 2.4.1.377: dTDP-Rha:α-D-Gal-diphosphoundecaprenol α-1,3-rhamnosyltransferase +EC 2.4.1.378: GDP-mannose:α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,4-mannosyltransferase +EC 2.4.1.379: GDP-Man:α-D-Gal-diphosphoundecaprenol α-1,3-mannosyltransferase +EC 2.4.1.380: GDP-Man:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-mannosyltransferase +EC 2.4.1.381: dTDP-Rha:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-rhamnosyltransferase +EC 2.4.1.382: CDP-abequose:α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase +EC 2.4.1.383: GDP-Man:α-L-Rha-(1→3)-α-D-Gal-PP-Und β-1,4-mannosyltransferase +EC 2.4.1.384: NDP-glycosyltransferase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-8.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-8.md new file mode 100644 index 000000000..17ef4a9ea --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-8.md @@ -0,0 +1,101 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 9/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.4.2: Pentosyltransferases === +EC 2.4.2.1: purine-nucleoside phosphorylase +EC 2.4.2.2: pyrimidine-nucleoside phosphorylase +EC 2.4.2.3: uridine phosphorylase +EC 2.4.2.4: thymidine phosphorylase +EC 2.4.2.5: nucleoside ribosyltransferase +EC 2.4.2.6: nucleoside deoxyribosyltransferase +EC 2.4.2.7: adenine phosphoribosyltransferase +EC 2.4.2.8: hypoxanthine phosphoribosyltransferase +EC 2.4.2.9: uracil phosphoribosyltransferase +EC 2.4.2.10: orotate phosphoribosyltransferase +EC 2.4.2.11: now EC 6.3.4.21 nicotinate phosphoribosyltransferase +EC 2.4.2.12: nicotinamide phosphoribosyltransferase +EC 2.4.2.13: now EC 2.5.1.6 methionine adenosyltransferase +EC 2.4.2.14: amidophosphoribosyltransferase +EC 2.4.2.15: guanosine phosphorylase +EC 2.4.2.16: urate-ribonucleotide phosphorylase +EC 2.4.2.17: ATP phosphoribosyltransferase +EC 2.4.2.18: anthranilate phosphoribosyltransferase +EC 2.4.2.19: nicotinate-nucleotide diphosphorylase (carboxylating) +EC 2.4.2.20: dioxotetrahydropyrimidine phosphoribosyltransferase +EC 2.4.2.21: nicotinate-nucleotide—dimethylbenzimidazole phosphoribosyltransferase +EC 2.4.2.22: xanthine phosphoribosyltransferase +EC 2.4.2.23: [[This activity has been shown to be catalysed by EC 2.4.2.2, ((pyrimidine-nucleoside phosphorylase)), EC 2.4.2.3, ((uridine phosphorylase)), and EC 2.4.2.4, ((thymidine phosphorylase)).|This activity has been shown to be catalysed by EC 2.4.2.2, pyrimidine-nucleoside phosphorylase, EC 2.4.2.3, uridine phosphorylase, and EC 2.4.2.4, thymidine phosphorylase.]] +EC 2.4.2.24: 1,4-β-D-xylan synthase +EC 2.4.2.25: flavone apiosyltransferase +EC 2.4.2.26: protein xylosyltransferase +EC 2.4.2.27: dTDP-dihydrostreptose—streptidine-6-phosphate dihydrostreptosyltransferase +EC 2.4.2.28: S-methyl-5′-thioadenosine phosphorylase +EC 2.4.2.29: tRNA-guanosine34 preQ1 transglycosylase +EC 2.4.2.30: NAD+ ADP-ribosyltransferase +EC 2.4.2.31: NAD+—protein-arginine ADP-ribosyltransferase +EC 2.4.2.32: dolichyl-phosphate D-xylosyltransferase +EC 2.4.2.33: dolichyl-xylosyl-phosphate—protein xylosyltransferase +EC 2.4.2.34: indolylacetylinositol arabinosyltransferase +EC 2.4.2.35: flavonol-3-O-glycoside xylosyltransferase +EC 2.4.2.36: NAD+—diphthamide ADP-ribosyltransferase +EC 2.4.2.37: NAD+ —dinitrogen-reductase ADP-D-ribosyltransferase +EC 2.4.2.38: glycoprotein 2-β-D-xylosyltransferase +EC 2.4.2.39: xyloglucan 6-xylosyltransferase +EC 2.4.2.40: zeatin O-β-D-xylosyltransferase +EC 2.4.2.41: xylogalacturonan β-1,3-xylosyltransferase +EC 2.4.2.42: UDP-D-xylose:β-D-glucoside α-1,3-D-xylosyltransferase +EC 2.4.2.43: lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase +EC 2.4.2.44: S-methyl-5′-thioinosine phosphorylase +EC 2.4.2.45: decaprenyl-phosphate phosphoribosyltransferase +EC 2.4.2.46: galactan 5-O-arabinofuranosyltransferase +EC 2.4.2.47: arabinofuranan 3-O-arabinosyltransferase +EC 2.4.2.48: tRNA-guanine15 transglycosylase +EC 2.4.2.49: neamine phosphoribosyltransferase +EC 2.4.2.50: cyanidin 3-O-galactoside 2′′-O-xylosyltransferase +EC 2.4.2.51: anthocyanidin 3-O-glucoside 2′′′-O-xylosyltransferase +EC 2.4.2.52: triphosphoribosyl-dephospho-CoA synthase +EC 2.4.2.53: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase +EC 2.4.2.54: β-ribofuranosylphenol 5′-phosphate synthase +EC 2.4.2.55: nicotinate D-ribonucleotide:phenol phospho-D-ribosyltransferase +EC 2.4.2.56: kaempferol 3-O-xylosyltransferase +EC 2.4.2.57: AMP phosphorylase +EC 2.4.2.58: hydroxyproline O-arabinosyltransferase +EC 2.4.2.59: sulfide-dependent adenosine diphosphate thiazole synthase +EC 2.4.2.60: cysteine-dependent adenosine diphosphate thiazole synthase +EC 2.4.2.61: α-dystroglycan β1,4-xylosyltransferase +EC 2.4.2.62: xylosyl α-1,3-xylosyltransferase +EC 2.4.2.63: EGF-domain serine xylosyltransferase +EC 2.4.2.64: tRNA-guanosine34 queuine transglycosylase + +=== EC 2.4.99: Transferring Other Glycosyl Groups === +EC 2.4.99.1: β-galactoside α-(2,6)-sialyltransferase +EC 2.4.99.2: β-D-galactosyl-(1→3)-N-acetyl-β-D-galactosaminide α-2,3-sialyltransferase +EC 2.4.99.3: α-N-acetylgalactosaminide α-2,6-sialyltransferase +EC 2.4.99.4: β-galactoside α-2,3-sialyltransferase +EC 2.4.99.5: galactosyldiacylglycerol α-2,3-sialyltransferase +EC 2.4.99.6: N-acetyllactosaminide α-2,3-sialyltransferase +EC 2.4.99.7: α-N-acetylneuraminyl-2,3-β-galactosyl-1,3-N-acetylgalactosaminide 6-α-sialyltransferase +EC 2.4.99.8: α-N-acetylneuraminate α-2,8-sialyltransferase +EC 2.4.99.9: lactosylceramide α-2,3-sialyltransferase +EC 2.4.99.10: Now included in EC 2.4.99.6, N-acetyllactosaminide α-2,3-sialyltransferase +EC 2.4.99.11: Now included with EC 2.4.99.1,β-galactoside α-(2,6)-sialyltransferase +EC 2.4.99.12: lipid IVA 3-deoxy-D-manno-octulosonic acid transferase +EC 2.4.99.13: (Kdo)-lipid IVA3-deoxy-D-manno-octulosonic acid transferase +EC 2.4.99.14: (Kdo)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase +EC 2.4.99.15: (Kdo)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase +EC 2.4.99.16: starch synthase (maltosyl-transferring) +EC 2.4.99.17: S-adenosylmethionine:tRNA ribosyltransferase-isomerase +EC 2.4.99.18: dolichyl-diphosphooligosaccharide—protein glycotransferase +EC 2.4.99.19: undecaprenyl-diphosphooligosaccharide—protein glycotransferase +EC 2.4.99.20: 2′-phospho-ADP-ribosyl cyclase/2′-phospho-cyclic-ADP-ribose transferase +EC 2.4.99.21: dolichyl-phosphooligosaccharide-protein glycotransferase +EC 2.4.99.22: N-acetylglucosaminide α-(2,6)-sialyltransferase + +== EC 2.5: Transferring Alkyl or Aryl Groups, Other than Methyl Groups == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-9.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-9.md new file mode 100644 index 000000000..1bb854f3a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)-9.md @@ -0,0 +1,166 @@ +--- +title: "List of EC numbers (EC 2)" +chunk: 10/14 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_2)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:06.752346+00:00" +instance: "kb-cron" +--- + +=== EC 2.5.1: Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date) === +EC 2.5.1.1: dimethylallyltranstransferase +EC 2.5.1.2: thiamine pyridinylase +EC 2.5.1.3: thiamine-phosphate diphosphorylase +EC 2.5.1.4: adenosylmethionine cyclotransferase +EC 2.5.1.5: galactose-6-sulfurylase +EC 2.5.1.6: methionine adenosyltransferase +EC 2.5.1.7: UDP-N-acetylglucosamine 1-carboxyvinyltransferase +EC 2.5.1.8: transferred to EC 2.5.1.75, tRNA dimethylallyltransferase +EC 2.5.1.9: riboflavin synthase +EC 2.5.1.10: (2E,6E)-farnesyl diphosphate synthase +EC 2.5.1.11: Now covered by EC 2.5.1.84 (all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]) and EC 2.5.1.85 (all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]) +EC 2.5.1.12: deleted, now included with EC 2.5.1.18 glutathione transferase +EC 2.5.1.13: deleted, now included with EC 2.5.1.18 glutathione transferase +EC 2.5.1.14: deleted, now included with EC 2.5.1.18 glutathione transferase +EC 2.5.1.15: dihydropteroate synthase +EC 2.5.1.16: spermidine synthase +EC 2.5.1.17: cob(I)yrinic acid a,c-diamide adenosyltransferase +EC 2.5.1.18: glutathione transferase +EC 2.5.1.19: 3-phosphoshikimate 1-carboxyvinyltransferase +EC 2.5.1.20: rubber cis-polyprenylcistransferase +EC 2.5.1.21: squalene synthase +EC 2.5.1.22: spermine synthase +EC 2.5.1.23: sym-norspermidine synthase +EC 2.5.1.24: discadenine synthase +EC 2.5.1.25: tRNA-uridine aminocarboxypropyltransferase +EC 2.5.1.26: alkylglycerone-phosphate synthase +EC 2.5.1.27: adenylate dimethylallyltransferase +EC 2.5.1.28: dimethylallylcistransferase +EC 2.5.1.29: farnesyltranstransferase +EC 2.5.1.30: trans-hexaprenyltranstransferase +EC 2.5.1.31: ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] +EC 2.5.1.32: 15-cis-phytoene synthase +EC 2.5.1.33: deleted, now covered by EC 2.5.1.82 hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] and EC 2.5.1.83 hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] +EC 2.5.1.34: tryptophan dimethylallyltransferase +EC 2.5.1.35: aspulvinone dimethylallyltransferase +EC 2.5.1.36: trihydroxypterocarpan dimethylallyltransferase +EC 2.5.1.37: Now EC 4.4.1.20, leukotriene-C4 synthase +EC 2.5.1.38: isonocardicin synthase +EC 2.5.1.39: 4-hydroxybenzoate polyprenyltransferase +EC 2.5.1.40: Now EC 4.2.3.9, aristolochene synthase +EC 2.5.1.41: phosphoglycerol geranylgeranyltransferase +EC 2.5.1.42: geranylgeranylglycerol-phosphate geranylgeranyltransferase +EC 2.5.1.43: nicotianamine synthase +EC 2.5.1.44: homospermidine synthase +EC 2.5.1.45: homospermidine synthase (spermidine-specific) +EC 2.5.1.46: deoxyhypusine synthase +EC 2.5.1.47: cysteine synthase +EC 2.5.1.48: cystathionine γ-synthase +EC 2.5.1.49: O-acetylhomoserine aminocarboxypropyltransferase +EC 2.5.1.50: zeatin 9-aminocarboxyethyltransferase +EC 2.5.1.51: β-pyrazolylalanine synthase +EC 2.5.1.52: L-mimosine synthase +EC 2.5.1.53: uracilylalanine synthase +EC 2.5.1.54: 3-deoxy-7-phosphoheptulonate synthase +EC 2.5.1.55: 3-deoxy-8-phosphooctulonate synthase +EC 2.5.1.56: N-acetylneuraminate synthase +EC 2.5.1.57: N-acylneuraminate-9-phosphate synthase +EC 2.5.1.58: protein farnesyltransferase +EC 2.5.1.59: protein geranylgeranyltransferase type I +EC 2.5.1.60: protein geranylgeranyltransferase type II +EC 2.5.1.61: hydroxymethylbilane synthase +EC 2.5.1.62: chlorophyll synthase +EC 2.5.1.63: adenosyl-fluoride synthase +EC 2.5.1.64: The reaction that was attributed to this enzyme is now known to be catalysed by two separate enzymes: EC 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase and EC 4.2.99.20 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase +EC 2.5.1.65: O-phosphoserine sulfhydrylase +EC 2.5.1.66: N2-(2-carboxyethyl)arginine synthase +EC 2.5.1.67: chrysanthemyl diphosphate synthase +EC 2.5.1.68: (2Z,6E)-farnesyl diphosphate synthase +EC 2.5.1.69: lavandulyl diphosphate synthase +EC 2.5.1.70: naringenin 8-dimethylallyltransferase +EC 2.5.1.71: leachianone-G 2′′-dimethylallyltransferase +EC 2.5.1.72: quinolinate synthase +EC 2.5.1.73: O-phospho-L-seryl-tRNA:Cys-tRNA synthase +EC 2.5.1.74: 1,4-dihydroxy-2-naphthoate polyprenyltransferase +EC 2.5.1.75: tRNA dimethylallyltransferase +EC 2.5.1.76: cysteate synthase +EC 2.5.1.77: Now EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-methylphenol transferase and EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. +EC 2.5.1.78: 6,7-dimethyl-8-ribityllumazine synthase +EC 2.5.1.79: thermospermine synthase +EC 2.5.1.80: 7-dimethylallyltryptophan synthase +EC 2.5.1.81: geranylfarnesyl diphosphate synthase +EC 2.5.1.82: hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] +EC 2.5.1.83: hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] +EC 2.5.1.84: all-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific) +EC 2.5.1.85: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] +EC 2.5.1.86: trans,polycis-decaprenyl diphosphate synthase +EC 2.5.1.87: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] +EC 2.5.1.88: trans,polycis-polyprenyl diphosphate synthase [(2Z,6E)-farnesyl diphosphate specific] +EC 2.5.1.89: tritrans,polycis-undecaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] +EC 2.5.1.90: all-trans-octaprenyl-diphosphate synthase +EC 2.5.1.91: all-trans-decaprenyl-diphosphate synthase +EC 2.5.1.92: (2Z,6Z)-farnesyl diphosphate synthase +EC 2.5.1.93: 4-hydroxybenzoate geranyltransferase +EC 2.5.1.94: adenozil-chloride synthase +EC 2.5.1.95: xanthan ketal pyruvate transferase +EC 2.5.1.96: 4,4′-diapophytoene synthase +EC 2.5.1.97: pseudaminic acid synthase +EC 2.5.1.98: Rhizobium leguminosarum exopolysaccharide glucosyl ketal-pyruvate-transferase +EC 2.5.1.99: [[The activity was an artifact caused by photoisomerization of the product of EC 2.5.1.32, ((phytoene synthase|15-cis-phytoene synthase))|The activity was an artifact caused by photoisomerization of the product of EC 2.5.1.32, 15-cis-phytoene synthase]] +EC 2.5.1.100: fumigaclavine A dimethylallyltransferase +EC 2.5.1.101: N,N′-diacetyllegionaminate synthase +EC 2.5.1.102: geranyl-pyrophosphate—olivetolic acid geranyltransferase +EC 2.5.1.103: presqualene diphosphate synthase +EC 2.5.1.104: N1-aminopropylagmatine synthase +EC 2.5.1.105: 7,8-dihydropterin-6-yl-methyl-4-(β-D-ribofuranosyl)aminobenzene 5′-phosphate synthase +EC 2.5.1.106: tryprostatin B synthase +EC 2.5.1.107: verruculogen prenyltransferase +EC 2.5.1.108: 2-(3-amino-3-carboxypropyl)histidine synthase +EC 2.5.1.109: brevianamide F prenyltransferase (deoxybrevianamide E-forming) +EC 2.5.1.110: 12α,13α-dihydroxyfumitremorgin C prenyltransferase +EC 2.5.1.111: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase +EC 2.5.1.112: adenylate dimethylallyltransferase (ADP/ATP-dependent) +EC 2.5.1.113: [[[CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase]] +EC 2.5.1.114: tRNAPhe (4-demethylwyosine37-C7) aminocarboxypropyltransferase +EC 2.5.1.115: homogentisate phytyltransferase +EC 2.5.1.116: homogentisate geranylgeranyltransferase +EC 2.5.1.117: homogentisate solanesyltransferase +EC 2.5.1.118: β-(isoxazolin-5-on-2-yl)-L-alanine synthase +EC 2.5.1.119: β-(isoxazolin-5-on-4-yl)-L-alanine synthase +EC 2.5.1.120: aminodeoxyfutalosine synthase +EC 2.5.1.121: 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase +EC 2.5.1.122: 4-O-dimethylallyl-L-tyrosine synthase +EC 2.5.1.123: flaviolin linalyltransferase +EC 2.5.1.124: 6-linalyl-2-O,3-dimethylflaviolin synthase +EC 2.5.1.125: 7-geranyloxy-5-hydroxy-2-methoxy-3-methylnaphthalene-1,4-dione synthase +EC 2.5.1.126: norspermine synthase +EC 2.5.1.127: caldopentamine synthase +EC 2.5.1.128: N4-bis(aminopropyl)spermidine synthase +EC 2.5.1.129: flavin prenyltransferase +EC 2.5.1.130: 2-carboxy-1,4-naphthoquinone phytyltransferase +EC 2.5.1.131: [[(4-{4-[2-(γ-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase]] +EC 2.5.1.132: 3-deoxy-D-glycero-D-galacto-nonulopyranosonate 9-phosphate synthase +EC 2.5.1.133: bacteriochlorophyll a synthase +EC 2.5.1.134: cystathionine β-synthase (O-acetyl-L-serine) +EC 2.5.1.135: validamine 7-phosphate valienyltransferase +EC 2.5.1.136: 2-acylphloroglucinol 4-prenyltransferase +EC 2.5.1.137: 2-acyl-4-prenylphloroglucinol 6-prenyltransferase +EC 2.5.1.138: coumarin 8-geranyltransferase +EC 2.5.1.139: umbelliferone 6-dimethylallyltransferase +EC 2.5.1.140: N-(2-amino-2-carboxyethyl)-L-glutamate synthase +EC 2.5.1.141: heme o synthase +EC 2.5.1.142: nerylneryl diphosphate synthase +EC 2.5.1.143: pyridinium-3,5-biscarboxylic acid mononucleotide synthase +EC 2.5.1.144: S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent) +EC 2.5.1.145: phosphatidylglycerol—prolipoprotein diacylglyceryl transferase +EC 2.5.1.146: [[3-geranyl-3-[(Z)-2-isocyanoethenyl]indole synthase]] +EC 2.5.1.147: 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-hydroxyphenyl transferase +EC 2.5.1.148: lycopaoctaene synthase +EC 2.5.1.149: lycopene elongase/hydratase (flavuxanthin-forming) +EC 2.5.1.150: lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming) +EC 2.5.1.151: alkylcobalamin dealkylase +EC 2.5.1.152: D-histidine 2-aminobutanoyltransferase +EC 2.5.1.153: adenosine tuberculosinyltransferase + +== EC 2.6: Transferring Nitrogenous Groups == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-0.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-0.md new file mode 100644 index 000000000..6692726b3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-0.md @@ -0,0 +1,167 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 1/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. + +== EC 3.1: Acting on Ester Bonds == + +=== EC 3.1.1: Carboxylic Ester Hydrolases === +EC 3.1.1.1: carboxylesterase +EC 3.1.1.2: arylesterase +EC 3.1.1.3: triacylglycerol lipase +EC 3.1.1.4: phospholipase A2 +EC 3.1.1.5: lysophospholipase +EC 3.1.1.6: acetylesterase +EC 3.1.1.7: acetylcholinesterase +EC 3.1.1.8: cholinesterase +EC 3.1.1.9: deleted, a side reaction of EC 3.1.1.8 cholinesterase +EC 3.1.1.10: tropinesterase +EC 3.1.1.11: pectinesterase +EC 3.1.1.12: deleted, identical with EC 3.1.1.1 carboxylesterase +EC 3.1.1.13: sterol esterase +EC 3.1.1.14: chlorophyllase +EC 3.1.1.15: L-arabinonolactonase +EC 3.1.1.16: deleted, mixture of EC 5.3.3.4 (muconolactone Δ-isomerase) and EC 3.1.1.24 (3-oxoadipate enol-lactonase) +EC 3.1.1.17: gluconolactonase +EC 3.1.1.18: deleted, now included with EC 3.1.1.17 gluconolactonase +EC 3.1.1.19: uronolactonase +EC 3.1.1.20: tannase +EC 3.1.1.21: deleted, now known to be catalysed by EC 3.1.1.1, carboxylesterase and EC 3.1.1.3, triacylglycerol lipase. +EC 3.1.1.22: hydroxybutyrate-dimer hydrolase +EC 3.1.1.23: acylglycerol lipase +EC 3.1.1.24: 3-oxoadipate enol-lactonase +EC 3.1.1.25: 1,4-lactonase +EC 3.1.1.26: galactolipase +EC 3.1.1.27: 4-pyridoxolactonase +EC 3.1.1.28: acylcarnitine hydrolase +EC 3.1.1.29: aminoacyl-tRNA hydrolase +EC 3.1.1.30: D-arabinonolactonase +EC 3.1.1.31: 6-phosphogluconolactonase +EC 3.1.1.32: phospholipase A1 +EC 3.1.1.33: 6-acetylglucose deacetylase +EC 3.1.1.34: lipoprotein lipase +EC 3.1.1.35: dihydrocoumarin hydrolase +EC 3.1.1.36: limonin-D-ring-lactonase +EC 3.1.1.37: steroid-lactonase +EC 3.1.1.38: triacetate-lactonase +EC 3.1.1.39: actinomycin lactonase +EC 3.1.1.40: orsellinate-depside hydrolase +EC 3.1.1.41: cephalosporin-C deacetylase +EC 3.1.1.42: chlorogenate hydrolase +EC 3.1.1.43: α-amino-acid esterase +EC 3.1.1.44: 4-methyloxaloacetate esterase +EC 3.1.1.45: carboxymethylenebutenolidase +EC 3.1.1.46: deoxylimonate A-ring-lactonase +EC 3.1.1.47: 1-alkyl-2-acetylglycerophosphocholine esterase +EC 3.1.1.48: fusarinine-C ornithinesterase +EC 3.1.1.49: sinapine esterase +EC 3.1.1.50: wax-ester hydrolase +EC 3.1.1.51: phorbol-diester hydrolase +EC 3.1.1.52: phosphatidylinositol deacylase +EC 3.1.1.53: sialate O-acetylesterase +EC 3.1.1.54: acetoxybutynylbithiophene deacetylase +EC 3.1.1.55: acetylsalicylate deacetylase +EC 3.1.1.56: methylumbelliferyl-acetate deacetylase +EC 3.1.1.57: 2-pyrone-4,6-dicarboxylate lactonase +EC 3.1.1.58: N-acetylgalactosaminoglycan deacetylase +EC 3.1.1.59: juvenile-hormone esterase +EC 3.1.1.60: bis(2-ethylhexyl)phthalate esterase +EC 3.1.1.61: protein-glutamate methylesterase +EC 3.1.1.62: Now listed as EC 3.5.1.47, N-acetyldiaminopimelate deacetylase +EC 3.1.1.63: 11-cis-retinyl-palmitate hydrolase +EC 3.1.1.64: retinoid isomerohydrolase +EC 3.1.1.65: L-rhamnono-1,4-lactonase +EC 3.1.1.66: 5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene deacetylase +EC 3.1.1.67: fatty-acyl-ethyl-ester synthase +EC 3.1.1.68: xylono-1,4-lactonase +EC 3.1.1.69: Now EC 3.5.1.89, N-acetylglucosaminylphosphatidylinositol deacetylase +EC 3.1.1.70: cetraxate benzylesterase +EC 3.1.1.71: acetylalkylglycerol acetylhydrolase +EC 3.1.1.72: acetylxylan esterase +EC 3.1.1.73: feruloyl esterase +EC 3.1.1.74: cutinase +EC 3.1.1.75: poly(3-hydroxybutyrate) depolymerase +EC 3.1.1.76: poly(3-hydroxyoctanoate) depolymerase +EC 3.1.1.77: acyloxyacyl hydrolase +EC 3.1.1.78: polyneuridine-aldehyde esterase +EC 3.1.1.79: hormone-sensitive lipase +EC 3.1.1.80: acetylajmaline esterase +EC 3.1.1.81: quorum-quenching N-acyl-homoserine lactonase +EC 3.1.1.82: pheophorbidase +EC 3.1.1.83: monoterpene ε-lactone hydrolase +EC 3.1.1.84: cocaine esterase +EC 3.1.1.85: pimelyl-(acyl-carrier protein) methyl ester esterase +EC 3.1.1.86: rhamnogalacturonan acetylesterase +EC 3.1.1.87: fumonisin B1 esterase +EC 3.1.1.88: pyrethroid hydrolase +EC 3.1.1.89: protein phosphatase methylesterase-1 +EC 3.1.1.90: all-trans-retinyl ester 13-cis isomerohydrolase +EC 3.1.1.91: 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase +EC 3.1.1.92: 4-sulfomuconolactone hydrolase +EC 3.1.1.93: mycophenolic acid acyl-glucuronide esterase +EC 3.1.1.94: versiconal hemiacetal acetate esterase +EC 3.1.1.95: aclacinomycin methylesterase +EC 3.1.1.96: D-aminoacyl-tRNA deacylase +EC 3.1.1.97: methylated diphthine methylhydrolase +EC 3.1.1.98: [Wnt protein] O-palmitoleoyl-L-serine hydrolase +EC 3.1.1.99: 6-deoxy-6-sulfogluconolactonase +EC 3.1.1.100: chlorophyllide a hydrolase +EC 3.1.1.101: poly(ethylene terephthalate) hydrolase +EC 3.1.1.102: mono(ethylene terephthalate) hydrolase +EC 3.1.1.103: teichoic acid D-alanine hydrolase +EC 3.1.1.104: 5-phospho-D-xylono-1,4-lactonase +EC 3.1.1.105: 3-O-acetylpapaveroxine carboxylesterase +EC 3.1.1.106: O-acetyl-ADP-ribose deacetylase +EC 3.1.1.107: apo-salmochelin esterase +EC 3.1.1.108: iron(III)-enterobactin esterase +EC 3.1.1.109: iron(III)-salmochelin esterase +EC 3.1.1.110: xylono-1,5-lactonase +EC 3.1.1.111: phosphatidylserine sn-1 acylhydrolase +EC 3.1.1.112: isoamyl acetate esterase +EC 3.1.1.113: ethyl acetate hydrolase +EC 3.1.1.114: methyl acetate hydrolase +EC 3.1.1.115: D-apionolactonase +EC 3.1.1.116: sn-1-specific diacylglycerol lipase +EC 3.1.1.117: (4-O-methyl)-D-glucuronate—lignin esterase +EC 3.1.1.118: phospholipid sn-1 acylhydrolase + +=== EC 3.1.2: Thioester Hydrolases === +EC 3.1.2.1: acetyl-CoA hydrolase +EC 3.1.2.2: palmitoyl-CoA hydrolase +EC 3.1.2.3: succinyl-CoA hydrolase +EC 3.1.2.4: 3-hydroxyisobutyryl-CoA hydrolase +EC 3.1.2.5: hydroxymethylglutaryl-CoA hydrolase +EC 3.1.2.6: hydroxyacylglutathione hydrolase +EC 3.1.2.7: glutathione thiolesterase +EC 3.1.2.8: Now included with EC 3.1.2.6 hydroxyacylglutathione hydrolase +EC 3.1.2.9: S-acetoacetylhydrolipoate hydrolase deleted +EC 3.1.2.10: formyl-CoA hydrolase +EC 3.1.2.11: acetoacetyl-CoA hydrolase +EC 3.1.2.12: S-formylglutathione hydrolase +EC 3.1.2.13: S-succinylglutathione hydrolase +EC 3.1.2.14: oleoyl-[acyl-carrier-protein] hydrolase +EC 3.1.2.15: covered by EC 3.4.19.12, ubiquitinyl hydrolase 1 +EC 3.1.2.16: citrate lyase deacetylase +EC 3.1.2.17: (S)-methylmalonyl-CoA hydrolase +EC 3.1.2.18: ADP-dependent short-chain-acyl-CoA hydrolase +EC 3.1.2.19: ADP-dependent medium-chain-acyl-CoA hydrolase +EC 3.1.2.20: acyl-CoA hydrolase +EC 3.1.2.21: dodecanoyl-(acyl-carrier-protein) hydrolase +EC 3.1.2.22: palmitoyl[protein] hydrolase +EC 3.1.2.23: 4-hydroxybenzoyl-CoA thioesterase +EC 3.1.2.24: transferred entry now EC 3.13.1.3, 2′-hydroxybiphenyl-2-sulfinate desulfinase. +EC 3.1.2.25: phenylacetyl-CoA hydrolase +EC 3.1.2.26: Now EC 2.8.3.25, bile acid CoA transferase +EC 3.1.2.27: choloyl-CoA hydrolase +EC 3.1.2.28: 1,4-dihydroxy-2-naphthoyl-CoA hydrolase +EC 3.1.2.29: fluoroacetyl-CoA thioesterase +EC 3.1.2.30: (3S)-malyl-CoA thioesterase +EC 3.1.2.31: dihydromonacolin L-[lovastatin nonaketide synthase] thioesterase +EC 3.1.2.32: 2-aminobenzoylacetyl-CoA thioesterase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-1.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-1.md new file mode 100644 index 000000000..7cfbe7eeb --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-1.md @@ -0,0 +1,227 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 2/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== EC 3.1.3: Phosphoric Monoester Hydrolases === +EC 3.1.3.1: alkaline phosphatase +EC 3.1.3.2: acid phosphatase +EC 3.1.3.3: phosphoserine phosphatase +EC 3.1.3.4: phosphatidate phosphatase +EC 3.1.3.5: 5′-nucleotidase +EC 3.1.3.6: 3′-nucleotidase +EC 3.1.3.7: 3′(2′),5′-bisphosphate nucleotidase +EC 3.1.3.8: 3-phytase +EC 3.1.3.9: glucose-6-phosphatase +EC 3.1.3.10: glucose-1-phosphatase +EC 3.1.3.11: fructose-bisphosphatase +EC 3.1.3.12: trehalose-phosphatase +EC 3.1.3.13: [[Recent studies have shown that this is a partial activity of ((EnzExplorer|5.4.2.11)), phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)|Recent studies have shown that this is a partial activity of EC 5.4.2.11, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)]] +EC 3.1.3.14: methylphosphothioglycerate phosphatase +EC 3.1.3.15: histidinol-phosphatase +EC 3.1.3.16: protein serine/threonine phosphatase +EC 3.1.3.17: (phosphorylase) phosphatase +EC 3.1.3.18: phosphoglycolate phosphatase +EC 3.1.3.19: glycerol-2-phosphatase +EC 3.1.3.20: phosphoglycerate phosphatase +EC 3.1.3.21: glycerol-1-phosphatase +EC 3.1.3.22: mannitol-1-phosphatase +EC 3.1.3.23: sugar-phosphatase +EC 3.1.3.24: sucrose-phosphatase +EC 3.1.3.25: inositol-phosphate phosphatase +EC 3.1.3.26: 4-phytase +EC 3.1.3.27: phosphatidylglycerophosphatase +EC 3.1.3.28: ADP-phosphoglycerate phosphatase +EC 3.1.3.29: N-acylneuraminate-9-phosphatase +EC 3.1.3.30: The activity may be that of an acid phosphatase +EC 3.1.3.31: The activity may be that of an acid phosphatase +EC 3.1.3.32: polynucleotide 3′-phosphatase +EC 3.1.3.33: polynucleotide 5′-phosphatase +EC 3.1.3.34: deoxynucleotide 3′-phosphatase +EC 3.1.3.35: thymidylate 5′-phosphatase +EC 3.1.3.36: phosphoinositide 5-phosphatase +EC 3.1.3.37: sedoheptulose-bisphosphatase +EC 3.1.3.38: 3-phosphoglycerate phosphatase +EC 3.1.3.39: streptomycin-6-phosphatase +EC 3.1.3.40: guanidinodeoxy-scyllo-inositol-4-phosphatase +EC 3.1.3.41: 4-nitrophenylphosphatase +EC 3.1.3.42: glycogen-synthase-D] phosphatase +EC 3.1.3.43: [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase +EC 3.1.3.44: [acetyl-CoA carboxylase]-phosphatase +EC 3.1.3.45: 3-deoxy-manno-octulosonate-8-phosphatase +EC 3.1.3.46: fructose-2,6-bisphosphate 2-phosphatase +EC 3.1.3.47: [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase +EC 3.1.3.48: protein-tyrosine-phosphatase +EC 3.1.3.49: [pyruvate kinase]-phosphatase +EC 3.1.3.50: sorbitol-6-phosphatase +EC 3.1.3.51: dolichyl-phosphatase +EC 3.1.3.52: [3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)]-phosphatase +EC 3.1.3.53: [myosin-light-chain] phosphatase +EC 3.1.3.54: fructose-2,6-bisphosphate 6-phosphatase +EC 3.1.3.55: caldesmon-phosphatase +EC 3.1.3.56: inositol-polyphosphate 5-phosphatase +EC 3.1.3.57: inositol-1,4-bisphosphate 1-phosphatase +EC 3.1.3.58: sugar-terminal-phosphatase +EC 3.1.3.59: alkylacetylglycerophosphatase +EC 3.1.3.60: phosphoenolpyruvate phosphatase +EC 3.1.3.61: deleted, as its existence has not been established +EC 3.1.3.62: multiple inositol-polyphosphate phosphatase +EC 3.1.3.63: 2-carboxy-D-arabinitol-1-phosphatase +EC 3.1.3.64: phosphatidylinositol-3-phosphatase +EC 3.1.3.65: Now included with EC 3.1.3.64, phosphatidylinositol-3-phosphatase +EC 3.1.3.66: phosphatidylinositol-3,4-bisphosphate 4-phosphatase +EC 3.1.3.67: phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase +EC 3.1.3.68: 2-deoxyglucose-6-phosphatase +EC 3.1.3.69: glucosylglycerol 3-phosphatase +EC 3.1.3.70: mannosyl-3-phosphoglycerate phosphatase +EC 3.1.3.71: 2-phosphosulfolactate phosphatase +EC 3.1.3.72: 5-phytase +EC 3.1.3.73: adenosylcobalamin/α-ribazole phosphatase +EC 3.1.3.74: pyridoxal phosphatase +EC 3.1.3.75: phosphoethanolamine/phosphocholine phosphatase +EC 3.1.3.76: lipid-phosphate phosphatase +EC 3.1.3.77: acireductone synthase +EC 3.1.3.78: phosphatidylinositol-4,5-bisphosphate 4-phosphatase +EC 3.1.3.79: mannosylfructose-phosphate phosphatase +EC 3.1.3.80: 2,3-bisphosphoglycerate 3-phosphatase +EC 3.1.3.81: Transferred entry, now EC 3.6.1.75, diacylglycerol diphosphate phosphatase +EC 3.1.3.82: D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphatase +EC 3.1.3.83: D-glycero-α-D-manno-heptose 1,7-bisphosphate 7-phosphatase +EC 3.1.3.84: ADP-ribose 1′′-phosphate phosphatase +EC 3.1.3.85: glucosyl-3-phosphoglycerate phosphatase +EC 3.1.3.86: phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase +EC 3.1.3.87: 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase +EC 3.1.3.88: 5′′-phosphoribostamycin phosphatase + +=== EC 3.1.4: Phosphoric Diester Hydrolases === +EC 3.1.4.1: phosphodiesterase I +EC 3.1.4.2: glycerophosphocholine phosphodiesterase +EC 3.1.4.3: lecithinase C +EC 3.1.4.4: phospholipase D +EC 3.1.4.5: Now EC 3.1.21.1, deoxyribonuclease I +EC 3.1.4.6: Now EC 3.1.22.1, deoxyribonuclease II +EC 3.1.4.7: Now EC 3.1.31.1, micrococcal nuclease +EC 3.1.4.8: Now EC 3.1.27.3, ribonuclease T1 +EC 3.1.4.9: Now EC 3.1.30.2, Serratia marcescens nuclease +EC 3.1.4.10: Now EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase +EC 3.1.4.11: phosphoinositide phospholipase C +EC 3.1.4.12: sphingomyelin phosphodiesterase +EC 3.1.4.13: serine-ethanolaminephosphate phosphodiesterase +EC 3.1.4.14: [acyl-carrier-protein] phosphodiesterase +EC 3.1.4.15 : transferred to EC 2.7.7.89, adenylyl-[glutamateammonia ligase] phosphorylase +EC 3.1.4.16: 2′,3′-cyclic-nucleotide 2′-phosphodiesterase +EC 3.1.4.17: 3′,5′-cyclic-nucleotide phosphodiesterase +EC 3.1.4.18: Now EC 3.1.16.1, spleen exonuclease +EC 3.1.4.19: Now EC 3.1.13.3, oligonucleotidase +EC 3.1.4.20: Now EC 3.1.13.1, exoribonuclease II +EC 3.1.4.21: Now EC 3.1.30.1, Aspergillus nuclease S1 +EC 3.1.4.22: Now EC 3.1.27.5, pancreatic ribonuclease +EC 3.1.4.23: Now EC 3.1.27.1, ribonuclease T2 +EC 3.1.4.24: deleted +EC 3.1.4.25: Now EC 3.1.11.1, exodeoxyribonuclease I +EC 3.1.4.26: deleted +EC 3.1.4.27: Now EC 3.1.11.2, exodeoxyribonuclease III +EC 3.1.4.28: Now EC 3.1.11.3, exodeoxyribonuclease (lambda-induced) +EC 3.1.4.29: deleted +EC 3.1.4.30: Now EC 3.1.21.2, deoxyribonuclease IV (phage-T4-induced) +EC 3.1.4.31: Now EC 3.1.11.4 +EC 3.1.4.32: deleted +EC 3.1.4.33: deleted +EC 3.1.4.34: deleted +EC 3.1.4.35: 3′,5′-cyclic-GMP phosphodiesterase +EC 3.1.4.36: Now with EC 3.1.4.43 +EC 3.1.4.37: 2′,3′-cyclic-nucleotide 3'-phosphodiesterase +EC 3.1.4.38: glycerophosphocholine cholinephosphodiesterase +EC 3.1.4.39: alkylglycerophosphoethanolamine phosphodiesterase +EC 3.1.4.40: CMP-N-acylneuraminate phosphodiesterase +EC 3.1.4.41: sphingomyelin phosphodiesterase D +EC 3.1.4.42: glycerol-1,2-cyclic-phosphate 2-phosphodiesterase +EC 3.1.4.43: glycerophosphoinositol inositolphosphodiesterase +EC 3.1.4.44: glycerophosphoinositol glycerophosphodiesterase +EC 3.1.4.45: N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase +EC 3.1.4.46: glycerophosphodiester phosphodiesterase +EC 3.1.4.47: Now EC 4.6.1.14, glycosylphosphatidylinositol diacylglycerol-lyase +EC 3.1.4.48: dolichylphosphate-glucose phosphodiesterase +EC 3.1.4.49: dolichylphosphate-mannose phosphodiesterase +EC 3.1.4.50: glycosylphosphatidylinositol phospholipase D +EC 3.1.4.51: glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase +EC 3.1.4.52: cyclic-guanylate-specific phosphodiesterase +EC 3.1.4.53: 3′,5′-cyclic-AMP phosphodiesterase +EC 3.1.4.54: N-acetylphosphatidylethanolamine-hydrolysing phospholipase D +EC 3.1.4.55: phosphoribosyl 1,2-cyclic phosphate phosphodiesterase +EC 3.1.4.56: 7,8-dihydroneopterin 2′,3′-cyclic phosphate phosphodiesterase +EC 3.1.4.57: phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase +EC 3.1.4.58: RNA 2′,3′-cyclic 3′-phosphodiesterase +EC 3.1.4.59: cyclic-di-AMP phosphodiesterase +EC 3.1.4.60: pApA phosphodiesterase +EC 3.1.4.61: cyclic 2,3-diphosphoglycerate hydrolase + +=== EC 3.1.5: Triphosphoric Monoester Hydrolases === +EC 3.1.5.1: dGTPase + +=== EC 3.1.6: Sulfuric Ester Hydrolases === +EC 3.1.6.1: arylsulfatase (type I) +EC 3.1.6.2: steryl-sulfatase +EC 3.1.6.3: glycosulfatase +EC 3.1.6.4: N-acetylgalactosamine-6-sulfatase +EC 3.1.6.5: deleted +EC 3.1.6.6: choline-sulfatase +EC 3.1.6.7: cellulose-polysulfatase +EC 3.1.6.8: cerebroside-sulfatase +EC 3.1.6.9: chondro-4-sulfatase +EC 3.1.6.10: chondro-6-sulfatase +EC 3.1.6.11: disulfoglucosamine-6-sulfatase +EC 3.1.6.12: N-acetylgalactosamine-6-sulfatase +EC 3.1.6.13: iduronate-2-sulfatase +EC 3.1.6.14: N-acetylglucosamine-6-sulfatase +EC 3.1.6.15: N-sulfoglucosamine-3-sulfatase +EC 3.1.6.16: monomethyl-sulfatase +EC 3.1.6.17: D-lactate-2-sulfatase +EC 3.1.6.18: Glucuronate-2-sulfatase +EC 3.1.6.19: (R)-specific secondary-alkylsulfatase (type III) +EC 3.1.6.20: S-sulfosulfanyl-L-cysteine sulfohydrolase +EC 3.1.6.21: linear primary-alkylsulfatase +EC 3.1.6.22: branched primary-alkylsulfatase + +=== EC 3.1.7: Diphosphoric Monoester Hydrolases === +EC 3.1.7.1: prenyl-diphosphatase +EC 3.1.7.2: guanosine-3′,5′-bis(diphosphate) 3′-diphosphatase +EC 3.1.7.3: monoterpenyl-diphosphatase +EC 3.1.7.4: Now recognized as two enzymes EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141, sclareol synthase +EC 3.1.7.5: geranylgeranyl diphosphate diphosphatase +EC 3.1.7.6: farnesyl diphosphatase +EC 3.1.7.7: Now EC 4.2.3.194, (–)-drimenol synthase +EC 3.1.7.8: Now known to be a partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase. +EC 3.1.7.9: Now known to be a partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase +EC 3.1.7.10: (13E)-labda-7,13-dien-15-ol synthase +EC 3.1.7.11: geranyl diphosphate diphosphatase +EC 3.1.7.12: (+)-kolavelool synthase + +=== EC 3.1.8: Phosphoric Triester Hydrolases === +EC 3.1.8.1: aryldialkylphosphatase +EC 3.1.8.2: diisopropyl-fluorophosphatase + +=== EC 3.1.11: Exodeoxyribonucleases Producing 5'-Phosphomonoesters === +EC 3.1.11.1: exodeoxyribonuclease I +EC 3.1.11.2: exodeoxyribonuclease III +EC 3.1.11.3: exodeoxyribonuclease (lambda-induced) +EC 3.1.11.4: exodeoxyribonuclease (phage SP3-induced) +EC 3.1.11.5: exodeoxyribonuclease V +EC 3.1.11.6: exodeoxyribonuclease VII +EC 3.1.11.7: Now EC 3.6.1.71, adenosine-5′-diphospho-5′-[DNA] diphosphatase +EC 3.1.11.8: Now EC 3.6.1.70, guanosine-5′-diphospho-5′-[DNA] diphosphatase + +=== EC 3.1.13: Exoribonucleases Producing 5'-Phosphomonoesters === +EC 3.1.13.1: exoribonuclease II +EC 3.1.13.2: exoribonuclease H +EC 3.1.13.3: oligonucleotidase +EC 3.1.13.4: poly(A)-specific ribonuclease +EC 3.1.13.5: ribonuclease D + +=== EC 3.1.14: Exoribonucleases Producing 3'-Phosphomonoesters === +EC 3.1.14.1: yeast ribonuclease \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-10.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-10.md new file mode 100644 index 000000000..1b9343b49 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-10.md @@ -0,0 +1,122 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 11/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== 3.6.4: Acting on acid anhydrides to facilitate cellular and subcellular movement === +EC 3.6.4.1: Now EC 5.6.1.8, myosin ATPase +EC 3.6.4.2: Now EC 5.6.1.2, dynein ATPase +EC 3.6.4.3: Now EC 5.6.1.1, microtubule-severing ATPase +EC 3.6.4.4: Now EC 5.6.1.3, plus-end-directed kinesin ATPase +EC 3.6.4.5: Now EC 5.6.1.4, minus-end-directed kinesin ATPase +EC 3.6.4.6: vesicle-fusing ATPase +EC 3.6.4.7: peroxisome-assembly ATPase +EC 3.6.4.8: Now EC 5.6.1.5, proteasome ATPase +EC 3.6.4.9: Now EC 5.6.1.7, chaperonin ATPase +EC 3.6.4.10: non-chaperonin molecular chaperone ATPase +EC 3.6.4.11: Deleted, the activity has been shown not to take place +EC 3.6.4.12: DNA helicase +EC 3.6.4.13: RNA helicase + +=== 3.6.5: Acting on GTP to facilitate cellular and subcellular movement === +EC 3.6.5.1: heterotrimeric G-protein GTPase +EC 3.6.5.2: small monomeric GTPase +EC 3.6.5.3: protein-synthesizing GTPase +EC 3.6.5.4: signal-recognition-particle GTPase +EC 3.6.5.5: dynamin GTPase +EC 3.6.5.6: tubulin GTPase + +== EC 3.7: Acting on carbon-carbon bonds == + +=== EC 3.7.1: In ketonic substances === +EC 3.7.1.1: oxaloacetase +EC 3.7.1.2: fumarylacetoacetase +EC 3.7.1.3: kynureninase +EC 3.7.1.4: phloretin hydrolase +EC 3.7.1.5: acylpyruvate hydrolase +EC 3.7.1.6: acetylpyruvate hydrolase +EC 3.7.1.7: β-diketone hydrolase +EC 3.7.1.8: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase +EC 3.7.1.9: 2-hydroxymuconate-semialdehyde hydrolase +EC 3.7.1.10: cyclohexane-1,3-dione hydrolase +EC 3.7.1.11: cyclohexane-1,2-dione hydrolase +EC 3.7.1.12: cobalt-precorrin 5A hydrolase +EC 3.7.1.13: 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase +EC 3.7.1.14: 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase +EC 3.7.1.15: Now EC 4.2.1.138, (+)-caryolan-1-ol synthase +EC 3.7.1.16: Now EC 3.3.2.12, oxepin-CoA hydrolase +EC 3.7.1.17: 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase +EC 3.7.1.18: 6-oxocamphor hydrolase +EC 3.7.1.19: 2,6-dihydroxypseudooxynicotine hydrolase +EC 3.7.1.20: 3-fumarylpyruvate hydrolase +EC 3.7.1.21: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase +EC 3.7.1.22: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (ring-opening) +EC 3.7.1.23: maleylpyruvate hydrolase +EC 3.7.1.24: 2,4-diacetylphloroglucinol hydrolase +EC 3.7.1.25: 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase +EC 3.7.1.26: 2,4-didehydro-3-deoxy-L-rhamnonate hydrolase +EC 3.7.1.27: neryl diphosphate diphosphatase +EC 3.7.1.28: 3-oxoisoapionate-4-phosphate transcarboxylase/hydrolase + +== EC 3.8: Acting on halide bonds == + +=== EC 3.8.1: Acting on halide bonds === +EC 3.8.1.1: Covered by EC 3.8.1.5, haloalkane dehalogenase. +EC 3.8.1.2: (S)-2-haloacid dehalogenase +EC 3.8.1.3: haloacetate dehalogenase +EC 3.8.1.4: Now EC 1.97.1.10, thyroxine 5′-deiodinase +EC 3.8.1.5: haloalkane dehalogenase +EC 3.8.1.6: 4-chlorobenzoate dehalogenase +EC 3.8.1.7: 4-chlorobenzoyl-CoA dehalogenase +EC 3.8.1.8: atrazine chlorohydrolase +EC 3.8.1.9: (R)-2-haloacid dehalogenase +EC 3.8.1.10: 2-haloacid dehalogenase (configuration-inverting) +EC 3.8.1.11: 2-haloacid dehalogenase (configuration-retaining) + +=== 3.8.2: In phosphorus-halide compounds (deleted sub-subclass) === +EC 3.8.2.1: Now EC 3.1.8.2, diisopropyl-fluorophosphatase + +== EC 3.9: act on phosphorus-nitrogen bonds == + +=== EC 3.9.1: Acting on phosphorus-nitrogen bonds (only sub-subclass identified to date) === +EC 3.9.1.1: phosphoamidase +EC 3.9.1.2: protein arginine phosphatase +EC 3.9.1.3: phosphohistidine phosphatase + +== EC 3.10: Acting on sulfur-nitrogen bonds == + +=== EC 3.10.1: Acting on sulfur-nitrogen bonds (only sub-subclass identified to date) === +EC 3.10.1.1: N-sulfoglucosamine sulfohydrolase +EC 3.10.1.2: cyclamate sulfohydrolase + +== EC 3.11: Acting on carbon-phosphorus bonds == + +=== EC 3.11.1: Acting on carbon-phosphorus bonds (only sub-subclass identified to date) === +EC 3.11.1.1: phosphonoacetaldehyde hydrolase +EC 3.11.1.2: phosphonoacetate hydrolase +EC 3.11.1.3: phosphonopyruvate hydrolase + +== EC 3.12: Acting on sulfur-sulfur bonds == + +=== EC 3.12.1: Acting on sulfur-sulfur bonds (only sub-subclass identified to date) === +EC 3.12.1.1: trithionate hydrolase + +== EC 3.13: Acting on carbon-sulfur bonds == + +=== EC 3.13.1: Acting on carbon-sulfur bonds (only sub-subclass identified to date) === +EC 3.13.1.1: UDP-sulfoquinovose synthase +EC 3.13.1.2: Deleted, the activity is most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase +EC 3.13.1.3: 2′-hydroxybiphenyl-2-sulfinate desulfinase +EC 3.13.1.4: 3-sulfinopropanoyl-CoA desulfinase +EC 3.13.1.5: carbon disulfide hydrolase +EC 3.13.1.6: [CysO sulfur-carrier protein]-S-L-cysteine hydrolase +EC 3.13.1.7: Carbonyl sulfide hydrolase +EC 3.13.1.8: S-adenosyl-L-methionine hydrolase (adenosine-forming) +EC 3.13.1.9: S-inosyl-L-homocysteine hydrolase + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-2.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-2.md new file mode 100644 index 000000000..4c759d805 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-2.md @@ -0,0 +1,77 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 3/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== EC 3.1.15: Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters === +EC 3.1.15.1: venom exonuclease + +=== EC 3.1.16: Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters === +EC 3.1.16.1: spleen exonuclease + +=== EC 3.1.21: Endodeoxyribonucleases Producing 5'-Phosphomonoesters === +EC 3.1.21.1: deoxyribonuclease I +EC 3.1.21.2: deoxyribonuclease IV +EC 3.1.21.3: type I site-specific deoxyribonuclease +EC 3.1.21.4: type II site-specific deoxyribonuclease +EC 3.1.21.5: type III site-specific deoxyribonuclease +EC 3.1.21.6: CC-preferring endodeoxyribonuclease +EC 3.1.21.7: deoxyribonuclease V +EC 3.1.21.8: T4 deoxyribonuclease II +EC 3.1.21.9: T4 deoxyribonuclease IV +EC 3.1.21.10: crossover junction endodeoxyribonuclease + +=== EC 3.1.22: Endodeoxyribonucleases Producing 3'-Phosphomonoesters === +EC 3.1.22.1: deoxyribonuclease II +EC 3.1.22.2: Aspergillus deoxyribonuclease K1 +EC 3.1.22.3: now EC 3.1.21.7 +EC 3.1.22.4: crossover junction endodeoxyribonuclease +EC 3.1.22.5: deoxyribonuclease X + +=== EC 3.1.23: and EC 3.1.24 now EC 3.1.21.3, EC 3.1.21.4 and EC 3.1.21.5 === +Deleted sub-subclasses. + +=== EC 3.1.25: Site-Specific Endodeoxyribonucleases Specific for Altered Bases === +EC 3.1.25.1: deoxyribonuclease (pyrimidine dimer) +EC 3.1.25.2: Now EC 4.2.99.18, DNA-(apurinic or apyrimidinic site) lyase + +=== EC 3.1.26: Endoribonucleases Producing 5'-Phosphomonoesters === +EC 3.1.26.1: Physarum polycephalum ribonuclease +EC 3.1.26.2: ribonuclease α +EC 3.1.26.3: ribonuclease III +EC 3.1.26.4: ribonuclease H +EC 3.1.26.5: ribonuclease P +EC 3.1.26.6: ribonuclease IV +EC 3.1.26.7: ribonuclease P4 +EC 3.1.26.8: ribonuclease M5 +EC 3.1.26.9: ribonuclease (poly-(U)-specific) +EC 3.1.26.10: ribonuclease IX +EC 3.1.26.11: tRNase Z +EC 3.1.26.12: ribonuclease E +EC 3.1.26.13: retroviral ribonuclease H + +=== EC 3.1.27: Endoribonucleases Producing 3'-Phosphomonoesters === +EC 3.1.27.1: Now EC 4.6.1.19, ribonuclease T2, since the primary reaction is that of a lyase +EC 3.1.27.2: Now EC 4.6.1.22, Bacillus subtilis ribonuclease, since the reaction catalysed is that of a lyase +EC 3.1.27.3: Now EC 4.6.1.24, ribonuclease T1, since the primary reaction is that of a lyase +EC 3.1.27.4: Now EC 4.6.1.20, ribonuclease U2, since the primary reaction is that of a lyase +EC 3.1.27.5: Now EC 4.6.1.18, pancreatic ribonuclease. +EC 3.1.27.6: Now EC 4.6.1.21, Enterobacter ribonuclease, since the primary reaction is that of a lyase +EC 3.1.27.7: ribonuclease F +EC 3.1.27.8: ribonuclease V +EC 3.1.27.9: Now EC 4.6.1.16, tRNA-intron lyase +EC 3.1.27.10: Now EC 4.6.1.23, ribotoxin, + +=== EC 3.1.30: Endoribonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters === +EC 3.1.30.1: Aspergillus nuclease S1 +EC 3.1.30.2: Serratia marcescens nuclease + +=== EC 3.1.31: Endoribonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters === +EC 3.1.31.1: micrococcal nuclease + +== EC 3.2: Glycosylases == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-3.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-3.md new file mode 100644 index 000000000..b355d443d --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-3.md @@ -0,0 +1,225 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 4/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== EC 3.2.1: Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds === +EC 3.2.1.1: α-amylase +EC 3.2.1.2: β-amylase +EC 3.2.1.3: glucan 1,4-α-glucosidase +EC 3.2.1.4: cellulase +EC 3.2.1.5: deleted +EC 3.2.1.6: endo-1,3(4)-β-glucanase +EC 3.2.1.7: inulinase +EC 3.2.1.8: endo-1,4-β-xylanase +EC 3.2.1.9: deleted +EC 3.2.1.10: oligo-1,6-glucosidase +EC 3.2.1.11: dextranase +EC 3.2.1.12: Now included with EC 3.2.1.54, cyclomaltodextrinase +EC 3.2.1.13: Now included with EC 3.2.1.54, cyclomaltodextrinase +EC 3.2.1.14: chitinase +EC 3.2.1.15: polygalacturonase +EC 3.2.1.16: deleted +EC 3.2.1.17: lysozyme +EC 3.2.1.18: exo-α-sialidase +EC 3.2.1.19: deleted +EC 3.2.1.20: α-glucosidase +EC 3.2.1.21: β-glucosidase +EC 3.2.1.22: α-galactosidase +EC 3.2.1.23: β-galactosidase +EC 3.2.1.24: α-mannosidase +EC 3.2.1.25: β-mannosidase +EC 3.2.1.26: β-fructofuranosidase (invertase) +EC 3.2.1.27: deleted +EC 3.2.1.28: α,α-trehalase +EC 3.2.1.29: Now included with EC 3.2.1.52, β-N-acetylhexosaminidase +EC 3.2.1.30: Now included with EC 3.2.1.52, β-N-acetylhexosaminidase +EC 3.2.1.31: β-glucuronidase +EC 3.2.1.32: endo-1,3-β-xylanase +EC 3.2.1.33: amylo-α-1,6-glucosidase +EC 3.2.1.34: Now included with EC 3.2.1.35, hyaluronoglucosaminidase +EC 3.2.1.35: hyaluronoglucosaminidase +EC 3.2.1.36: hyaluronoglucuronidase +EC 3.2.1.37: xylan 1,4-β-xylosidase +EC 3.2.1.38: β-D-fucosidase +EC 3.2.1.39: glucan endo-1,3-β-D-glucosidase +EC 3.2.1.40: α-L-rhamnosidase +EC 3.2.1.41: pullulanase +EC 3.2.1.42: GDP-glucosidase +EC 3.2.1.43: β-L-rhamnosidase +EC 3.2.1.44: Now EC 3.2.1.211, endo-(13)-fucoidanase and EC 3.2.1.212, endo-(14)-fucoidanase +EC 3.2.1.45: glucosylceramidase +EC 3.2.1.46: galactosylceramidase +EC 3.2.1.47: Now known to be catalyzed by EC 3.2.1.22, α-galactosidase +EC 3.2.1.48: sucrose α-glucosidase +EC 3.2.1.49: α-N-acetylgalactosaminidase +EC 3.2.1.50: α-N-acetylglucosaminidase +EC 3.2.1.51: α-L-fucosidase +EC 3.2.1.52: β-N-acetylhexosaminidase +EC 3.2.1.53: β-N-acetylgalactosaminidase +EC 3.2.1.54: cyclomaltodextrinase +EC 3.2.1.55: non-reducing end α-L-arabinofuranosidase +EC 3.2.1.56: glucuronosyl-disulfoglucosamine glucuronidase +EC 3.2.1.57: isopullulanase +EC 3.2.1.58: glucan 1,3-β-glucosidase +EC 3.2.1.59: glucan endo-1,3-α-glucosidase +EC 3.2.1.60: glucan 1,4-α-maltotetraohydrolase +EC 3.2.1.61: mycodextranase +EC 3.2.1.62: glycosylceramidase +EC 3.2.1.63: 1,2-α-L-fucosidase +EC 3.2.1.64: 2,6-β-fructan 6-levanbiohydrolase +EC 3.2.1.65: levanase +EC 3.2.1.66: Deleted entry: The activity is covered by EC 3.2.1.40, α-L-rhamnosidase +EC 3.2.1.67: galacturan 1,4-α-galacturonidase +EC 3.2.1.68: isoamylase +EC 3.2.1.69: Now included with EC 3.2.1.41, pullulanase +EC 3.2.1.70: glucan 1,6-α-glucosidase +EC 3.2.1.71: glucan endo-1,2-β-glucosidase +EC 3.2.1.72: xylan 1,3-β-xylosidase +EC 3.2.1.73: licheninase +EC 3.2.1.74: glucan 1,4-β-glucosidase +EC 3.2.1.75: glucan endo-1,6-β-glucosidase +EC 3.2.1.76: L-iduronidase +EC 3.2.1.77: mannan 1,2-(1,3)-α-mannosidase +EC 3.2.1.78: mannan endo-1,4-β-mannosidase +EC 3.2.1.79: Now included with EC 3.2.1.55, non-reducing end α-L-arabinofuranosidase +EC 3.2.1.80: fructan β-fructosidase +EC 3.2.1.81: β-agarase +EC 3.2.1.82: exo-poly-α-digalacturonosidas +EC 3.2.1.83: κ-carrageenase +EC 3.2.1.84: glucan 1,3-α-glucosidase +EC 3.2.1.85: 6-phospho-β-galactosidase +EC 3.2.1.86: 6-phospho-β-glucosidase +EC 3.2.1.87: capsular-polysaccharide endo-1,3-α-galactosidase +EC 3.2.1.88: non-reducing end β-L-arabinopyranosidase +EC 3.2.1.89: arabinogalactan endo-β-1,4-galactanase +EC 3.2.1.90: Deleted, not sufficiently characterised. +EC 3.2.1.91: cellulose 1,4-β-cellobiosidase (non-reducing end) +EC 3.2.1.92: peptidoglycan β-N-acetylmuramidase +EC 3.2.1.93: α,α-phosphotrehalase +EC 3.2.1.94: glucan 1,6-α-isomaltosidase +EC 3.2.1.95: dextran 1,6-α-isomaltotriosidase +EC 3.2.1.96: mannosyl-glycoprotein endo-β-N-acetylglucosaminidase +EC 3.2.1.97: endo-α-N-acetylgalactosaminidase +EC 3.2.1.98: glucan 1,4-α-maltohexaosidase +EC 3.2.1.99: arabinan endo-1,5-α-L-arabinanase +EC 3.2.1.100: mannan 1,4-mannobiosidase +EC 3.2.1.101: mannan endo-1,6-α-mannosidase +EC 3.2.1.102: blood-group-substance endo-1,4-β-galactosidase +EC 3.2.1.103: keratan-sulfate endo-1,4-β-galactosidase +EC 3.2.1.104: steryl-β-glucosidase +EC 3.2.1.105: 3α(S)-strictosidine β-glucosidase +EC 3.2.1.106: mannosyl-oligosaccharide glucosidase +EC 3.2.1.107: protein-glucosylgalactosylhydroxylysine glucosidase +EC 3.2.1.108: lactase +EC 3.2.1.109: endogalactosaminidase +EC 3.2.1.110: identical to EC 3.2.1.97, endo-α-N-acetylgalactosaminidase +EC 3.2.1.111: 1,3-α-L-fucosidase +EC 3.2.1.112: 2-deoxyglucosidase +EC 3.2.1.113: mannosyl-oligosaccharide 1,2-α-mannosidase +EC 3.2.1.114: mannosyl-oligosaccharide 1,3-1,6-α-mannosidas +EC 3.2.1.115: branched-dextran exo-1,2-α-glucosidase +EC 3.2.1.116: glucan 1,4-α-maltotriohydrolase +EC 3.2.1.117: amygdalin β-glucosidase +EC 3.2.1.118: prunasin β-glucosidase +EC 3.2.1.119: vicianin β-glucosidase +EC 3.2.1.120: oligoxyloglucan β-glycosidase +EC 3.2.1.121: polymannuronate hydrolase +EC 3.2.1.122: maltose-6′-phosphate glucosidase +EC 3.2.1.123: endoglycosylceramidase +EC 3.2.1.124: 3-deoxy-2-octulosonidase +EC 3.2.1.125: raucaffricine β-glucosidase +EC 3.2.1.126: coniferin β-glucosidase +EC 3.2.1.127: 1,6-α-L-fucosidase +EC 3.2.1.128: glycyrrhizin hydrolase +EC 3.2.1.129: endo-α-sialidase +EC 3.2.1.130: glycoprotein endo-α-1,2-mannosidase +EC 3.2.1.131: xylan α-1,2-glucuronosidase +EC 3.2.1.132: chitosanase +EC 3.2.1.133: glucan 1,4-α-maltohydrolase +EC 3.2.1.134: difructose-anhydride synthase +EC 3.2.1.135: neopullulanase +EC 3.2.1.136: glucuronoarabinoxylan endo-1,4-β-xylanase +EC 3.2.1.137: mannan exo-1,2-1,6-α-mannosidase +EC 3.2.1.138: Now EC 4.2.2.15, anhydrosialidase +EC 3.2.1.139: α-glucuronidase +EC 3.2.1.140: lacto-N-biosidase +EC 3.2.1.141: 4-α-D-{(1→4)-α-D-glucano}trehalose trehalohydrolase +EC 3.2.1.142: limit dextrinase +EC 3.2.1.143: poly(ADP-ribose) glycohydrolase +EC 3.2.1.144: 3-deoxyoctulosonase +EC 3.2.1.145: galactan 1,3-β-galactosidase +EC 3.2.1.146: β-galactofuranosidase +EC 3.2.1.147: thioglucosidase +EC 3.2.1.148: [[The activity is most probably attributable to ((EnzExplorer|4.4.1.21)), S-ribosylhomocysteine lyase|The activity is most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase]] +EC 3.2.1.149: β-primeverosidase +EC 3.2.1.150: oligoxyloglucan reducing-end-specific cellobiohydrolase +EC 3.2.1.151: xyloglucan-specific endo-β-1,4-glucanase +EC 3.2.1.152: mannosylglycoprotein endo-β-mannosidase +EC 3.2.1.153: fructan β-(2,1)-fructosidase +EC 3.2.1.154: fructan β-(2,6)-fructosidase +EC 3.2.1.155: xyloglucan-specific endo-processive β-1,4-glucanase +EC 3.2.1.156: oligosaccharide reducing-end xylanase +EC 3.2.1.157: ι-carrageenase +EC 3.2.1.158: α-agarase +EC 3.2.1.159: α-neoagaro-oligosaccharide hydrolase +EC 3.2.1.160: identical to EC 3.2.1.155, xyloglucan-specific exo-β-1,4-glucanase +EC 3.2.1.161: β-apiosyl-β-glucosidase +EC 3.2.1.162: λ-carrageenase +EC 3.2.1.163: 1,6-α-D-mannosidase +EC 3.2.1.164: galactan endo-1,6-β-galactosidase +EC 3.2.1.165: exo-1,4-β-D-glucosaminidase +EC 3.2.1.166: heparanase +EC 3.2.1.167: baicalin-β-D-glucuronidase +EC 3.2.1.168: hesperidin 6-O-α-L-rhamnosyl-β-D-glucosidase +EC 3.2.1.169: protein O-GlcNAcas +EC 3.2.1.170: mannosylglycerate hydrolase +EC 3.2.1.171: rhamnogalacturonan hydrolase +EC 3.2.1.172: unsaturated rhamnogalacturonyl hydrolase +EC 3.2.1.173: rhamnogalacturonan galacturonohydrolase +EC 3.2.1.174: rhamnogalacturonan rhamnohydrolase +EC 3.2.1.175: β-D-glucopyranosyl abscisate β-glucosidase +EC 3.2.1.176: cellulose 1,4-β-cellobiosidase (reducing end) +EC 3.2.1.177: α-D-xyloside xylohydrolase +EC 3.2.1.178: β-porphyranase +EC 3.2.1.179: gellan tetrasaccharide unsaturated glucuronyl hydrolase +EC 3.2.1.180: unsaturated chondroitin disaccharide hydrolase +EC 3.2.1.181: galactan endo-β-1,3-galactanase +EC 3.2.1.182: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside β-D-glucosidase +EC 3.2.1.183: UDP-N-acetylglucosamine 2-epimerase (hydrolysing) +EC 3.2.1.184: UDP-N,N′-diacetylbacillosamine 2-epimerase (hydrolysing) +EC 3.2.1.185: non-reducing end β-L-arabinofuranosidase +EC 3.2.1.186: protodioscin 26-O-β-D-glucosidase +EC 3.2.1.187: (Ara-f)3-Hyp β-L-arabinobiosidase +EC 3.2.1.188: avenacosidase * +EC 3.2.1.189: dioscin glycosidase (diosgenin-forming) +EC 3.2.1.190: dioscin glycosidase (3-O-β-D-Glc-diosgenin-forming) +EC 3.2.1.191: ginsenosidase type III +EC 3.2.1.192: ginsenoside Rb1 β-glucosidase +EC 3.2.1.193: ginsenosidase type I +EC 3.2.1.194: ginsenosidase type IV +EC 3.2.1.195: 20-O-multi-glycoside ginsenosidase +EC 3.2.1.196: limit dextrin α-1,6-maltotetraose-hydrolase +EC 3.2.1.197: β-1,2-mannosidase +EC 3.2.1.198: α-mannan endo-1,2-α-mannanase +EC 3.2.1.199: sulfoquinovosidase +EC 3.2.1.200: exo-chitinase (non-reducing end) +EC 3.2.1.201: exo-chitinase (reducing end) +EC 3.2.1.202: endo-chitodextinase +EC 3.2.1.203: carboxymethylcellulase +EC 3.2.1.204: 1,3-α-isomaltosidase +EC 3.2.1.205: isomaltose glucohydrolase +EC 3.2.1.206: oleuropein β-glucosidase +EC 3.2.1.207: mannosyl-oligosaccharide α-1,3-glucosidase +EC 3.2.1.208: glucosylglycerate hydrolase +EC 3.2.1.209: endoplasmic reticulum Man9GlcNAc2 1,2-α-mannosidase +EC 3.2.1.210: endoplasmic reticulum Man8GlcNAc2 1,2-α-mannosidase +EC 3.2.1.211: endo-(1→3)-fucoidanase +EC 3.2.1.212: endo-(1→4)-fucoidanase +EC 3.2.1.213: galactan exo-1,6-β-galactobiohydrolase (non-reducing end) +EC 3.2.1.214: exo β-1,2-glucooligosaccharide sophorohydrolase (non-reducing end) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-4.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-4.md new file mode 100644 index 000000000..78544d81a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-4.md @@ -0,0 +1,161 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 5/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== EC 3.2.2: Hydrolysing N-Glycosyl Compounds === +EC 3.2.2.1: purine nucleosidase +EC 3.2.2.2: inosine nucleosidase +EC 3.2.2.3: uridine nucleosidase +EC 3.2.2.4: AMP nucleosidase +EC 3.2.2.5: NAD+ glycohydrolase +EC 3.2.2.6: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase +EC 3.2.2.7: adenosine nucleosidase +EC 3.2.2.8: ribosylpyrimidine nucleosidase +EC 3.2.2.9: adenosylhomocysteine nucleosidase +EC 3.2.2.10: pyrimidine-5′-nucleotide nucleosidase +EC 3.2.2.11: β-aspartyl-N-acetylglucosaminidase +EC 3.2.2.12: inosinate nucleosidase +EC 3.2.2.13: 1-methyladenosine nucleosidase +EC 3.2.2.14: NMN nucleosidase +EC 3.2.2.15: DNA-deoxyinosine glycosylase +EC 3.2.2.16: methylthioadenosine nucleosidase +EC 3.2.2.17: deoxyribodipyrimidine endonucleosidase +EC 3.2.2.18: Now included with EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase +EC 3.2.2.19: ADP-ribosylarginine hydrolase +EC 3.2.2.20: DNA-3-methyladenine glycosylase I +EC 3.2.2.21: DNA-3-methyladenine glycosylase II, MAG1 +EC 3.2.2.22: rRNA 'N-glycosylase +EC 3.2.2.23: DNA-formamidopyrimidine glycosylase +EC 3.2.2.24: ADP-ribosyl-[dinitrogen reductase] hydrolase +EC 3.2.2.25: N-methyl nucleosidase +EC 3.2.2.26: futalosine hydrolase +EC 3.2.2.27: uracil-DNA glycosylase +EC 3.2.2.28: double-stranded uracil-DNA glycosylase +EC 3.2.2.29: thymine-DNA glycosylase +EC 3.2.2.30: aminodeoxyfutalosine nucleosidase +EC 3.2.2.31: adenine glycosylase + +=== EC 3.2.3: Hydrolysing S-Glycosyl Compounds === +Deleted sub-subclass + +== EC 3.3: Acting on Ether Bonds == + +=== EC 3.3.1: Thioether and trialkylsulfonium hydrolases === +EC 3.3.1.1: adenosylhomocysteinase +EC 3.3.1.2: S-adenosyl-L-methionine hydrolase (L-homoserine-forming) +EC 3.3.1.3: [[The activity is most probably attributable to ((EnzExplorer|4.4.1.21)), S-ribosylhomocysteine lyase|The activity is most probably attributable to EC 4.4.1.21, S-ribosylhomocysteine lyase]] + +=== EC 3.3.2: Ether Hydrolases === +EC 3.3.2.1: isochorismatase +EC 3.3.2.2: alkenylglycerophosphocholine hydrolase +EC 3.3.2.3: Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10) +EC 3.3.2.4: trans-epoxysuccinate hydrolase +EC 3.3.2.5: Now included in EC 3.3.2.2, lysoplasmalogenase +EC 3.3.2.6: leukotriene-A4 hydrolase +EC 3.3.2.7: hepoxilin-epoxide hydrolase +EC 3.3.2.8: limonene-1,2-epoxide hydrolase +EC 3.3.2.9: microsomal epoxide hydrolase +EC 3.3.2.10: soluble epoxide hydrolase +EC 3.3.2.11: cholesterol-5,6-oxide hydrolase +EC 3.3.2.12: oxepin-CoA hydrolase +EC 3.3.2.13: chorismatase +EC 3.3.2.14: 2,4-dinitroanisole O-demethylase +EC 3.3.2.15: trans-2,3-dihydro-3-hydroxyanthranilic acid synthase + +== EC 3.4: Acting on peptide bonds – Peptidase == + +=== EC 3.4.1 α-amino acyl peptide hydrolases (discontinued) === +EC 3.4.1.1: Now EC 3.4.11.1, leucyl aminopeptidase +EC 3.4.1.2: Now EC 3.4.11.2, membrane alanyl aminopeptidase +EC 3.4.1.3: Now EC 3.4.11.4, tripeptide aminopeptidase +EC 3.4.1.4: Now EC 3.4.11.5, prolyl aminopeptidase + +=== EC 3.4.2 Peptidyl amino acid hydrolases (discontinued) === +EC 3.4.2.1: Now EC 3.4.17.1, carboxypeptidase A +EC 3.4.2.2: Now EC 3.4.17.2, carboxypeptidase B +EC 3.4.2.3: Now EC 3.4.17.4, Gly-Xaa carboxypeptidase + +=== EC 3.4.3: Dipeptide hydrolases (deleted sub-subclass) === +EC 3.4.3.1: Now EC 3.4.13.18, cytosol nonspecific dipeptidase +EC 3.4.3.2: Now EC 3.4.13.18, cytosol nonspecific dipeptidase +EC 3.4.3.3: Now EC 3.4.13.3, Xaa-His dipeptidase +EC 3.4.3.4: Now EC 3.4.13.5, Xaa-methyl-His dipeptidase +EC 3.4.3.5: Now EC 3.4.11.2, membrane alanyl aminopeptidase +EC 3.4.3.6: Now EC 3.4.13.18, cytosol nonspecific dipeptidase +EC 3.4.3.7: Now EC 3.4.13.9, Xaa-Pro dipeptidase + +=== EC 3.4.4 Peptidyl Peptide Hydrolases (discontinued) === +EC 3.4.4.1: Now EC 3.4.23.1, pepsin A +EC 3.4.4.2: Now EC 3.4.23.2, pepsin B +EC 3.4.4.3: Now EC 3.4.23.4, chymosin +EC 3.4.4.4: Now EC 3.4.21.4, trypsin +EC 3.4.4.5: Now EC 3.4.21.1, chymotrypsin +EC 3.4.4.6: Now EC 3.4.21.1, chymotrypsin +EC 3.4.4.7: Now covered by EC 3.4.21.36, pancreatic elastase and EC 3.4.21.37, leukocyte elastase +EC 3.4.4.8: Now EC 3.4.21.9, enteropeptidase +EC 3.4.4.9: Now EC 3.4.14.1, dipeptidyl-peptidase I +EC 3.4.4.10: Now EC 3.4.22.2, papain +EC 3.4.4.11: Now EC 3.4.22.6, chymopapain +EC 3.4.4.12: Now EC 3.4.22.3, ficain +EC 3.4.4.13: Now EC 3.4.21.5, thrombin +EC 3.4.4.14: Now EC 3.4.21.7, plasmin +EC 3.4.4.15: Now EC 3.4.23.15, renin +EC 3.4.4.16: Now covered by the microbial serine proteinases EC 3.4.21.62 (subtilisin), EC 3.4.21.63 (oryzin), EC 3.4.21.64 (endopeptidase K), EC 3.4.21.65 (thermomycolin), EC 3.4.21.66 (thermitase) and EC 3.4.21.67 (endopeptidase So) +EC 3.4.4.17: Now covered by the microbial aspartic proteinases EC 3.4.23.20 (penicillopepsin), EC 3.4.23.21 (rhizopuspepsin), EC 3.4.23.22 (endothiapepsin), EC 3.4.23.23 (mucorpepsin), EC 3.4.23.24 (candidapepsin), EC 3.4.23.25 (saccharopepsin), EC 3.4.23.26 (rhodotorulapepsin), EC 3.4.21.103 (physarolisin), EC 3.4.23.28 (acrocylindropepsin), EC 3.4.23.29 (polyporopepsin) and EC 3.4.23.30 (pycnoporopepsin) +EC 3.4.4.18: Now EC 3.4.22.10, streptopain +EC 3.4.4.19: Now EC 3.4.24.3, microbial collagenase +EC 3.4.4.20: Now EC 3.4.22.8, clostripain +EC 3.4.4.21: Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein) +EC 3.4.4.22: Now EC 3.4.23.3, gastricsin +EC 3.4.4.23: Now EC 3.4.23.5, cathepsin D +EC 3.4.4.24: Now covered by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain) +EC 3.4.4.25: deleted + +=== EC 3.4.11 Aminopeptidases === +EC 3.4.11.1: leucyl aminopeptidase +EC 3.4.11.2: membrane alanyl aminopeptidase +EC 3.4.11.3: cystinyl aminopeptidase +EC 3.4.11.4: tripeptide aminopeptidase +EC 3.4.11.5: prolyl aminopeptidase +EC 3.4.11.6: aminopeptidase B +EC 3.4.11.7: glutamyl aminopeptidase +EC 3.4.11.8: Now EC 3.4.19.3, pyroglutamyl-peptidase I +EC 3.4.11.9: Xaa-Pro aminopeptidase +EC 3.4.11.10: bacterial leucyl aminopeptidase +EC 3.4.11.11: Deleted +EC 3.4.11.12: Deleted +EC 3.4.11.13: Clostridial aminopeptidase +EC 3.4.11.14: cytosol alanyl aminopeptidase +EC 3.4.11.15: aminopeptidase Y +EC 3.4.11.16: Xaa-Trp aminopeptidase +EC 3.4.11.17: tryptophanyl aminopeptidase +EC 3.4.11.18: methionyl aminopeptidase +EC 3.4.11.19: D-stereospecific aminopeptidase +EC 3.4.11.20: aminopeptidase Ey +EC 3.4.11.21: aspartyl aminopeptidase +EC 3.4.11.22: aminopeptidase I +EC 3.4.11.23: PepB aminopeptidase +EC 3.4.11.24: aminopeptidase S +EC 3.4.11.25: β-peptidyl aminopeptidase +EC 3.4.11.26: intermediate cleaving peptidase 55 + +=== EC 3.4.12 Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted sub-subclass) === +EC 3.4.12.1: Now EC 3.4.16.5 (carboxypeptidase C) and EC 3.4.16.6 (carboxypeptidase D) +EC 3.4.12.2: Now EC 3.4.17.1, carboxypeptidase A +EC 3.4.12.3: Now EC 3.4.17.2, carboxypeptidase B +EC 3.4.12.4: Now EC 3.4.16.2, lysosomal Pro-Xaa carboxypeptidase +EC 3.4.12.5: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase +EC 3.4.12.6: Now EC 3.4.17.8, muramoyl-pentapeptidase carboxypeptidase +EC 3.4.12.7: Now EC 3.4.17.3, lysine carboxypeptidase +EC 3.4.12.8: Now EC 3.4.17.4, Gly-Xaa carboxypeptidase +EC 3.4.12.9: aspartate carboxypeptidase +EC 3.4.12.10: Now EC 3.4.19.9, γ-glutamyl hydrolase +EC 3.4.12.11: Now EC 3.4.17.6, alanine carboxypeptidase +EC 3.4.12.12: Now EC 3.4.16.5 (carboxypeptidase C) and EC 3.4.16.6 (carboxypeptidase D) +EC 3.4.12.13: γ-glutamylglutamate carboxypeptidase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-5.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-5.md new file mode 100644 index 000000000..50a231f3c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-5.md @@ -0,0 +1,113 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 6/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== EC 3.4.13 Dipeptidases === +EC 3.4.13.1: Now EC 3.4.13.18, cytosol nonspecific dipeptidase +EC 3.4.13.2: Now EC 3.4.13.18, cytosol nonspecific dipeptidase +EC 3.4.13.3: The activity is covered by EC .4.13.18, cytosol nonspecific dipeptidase and EC 3.4.13.20, β-Ala-His dipeptidase +EC 3.4.13.4: Xaa-Arg dipeptidase +EC 3.4.13.5: Xaa-methyl-His dipeptidase +EC 3.4.13.6: Now EC 3.4.11.2, membrane alanyl aminopeptidase +EC 3.4.13.7: Glu-Glu dipeptidase +EC 3.4.13.8: Now EC 3.4.13.18, cytosol nonspecific dipeptidase +EC 3.4.13.9: Xaa-Pro dipeptidase +EC 3.4.13.10: Now EC 3.4.19.5, β-aspartyl-peptidase +EC 3.4.13.11: Now EC 3.4.13.19, membrane dipeptidase +EC 3.4.13.12: Met-Xaa dipeptidase +EC 3.4.13.13: Now EC 3.4.13.3, Xaa-His dipeptidase +EC 3.4.13.14: Deleted +EC 3.4.13.15: Now EC 3.4.13.18, cytosol nonspecific dipeptidase +EC 3.4.13.16: Deleted +EC 3.4.13.17: non-stereospecific dipeptidase +EC 3.4.13.18: cytosol nonspecific dipeptidase +EC 3.4.13.19: membrane dipeptidase +EC 3.4.13.20: β-Ala-His dipeptidase +EC 3.4.13.21: dipeptidase E +EC 3.4.13.22: D-Ala-D-Ala dipeptidase +EC 3.4.13.23: cysteinylglycine-S-conjugate dipeptidase + +=== EC 3.4.14 Dipeptidyl peptidases and tripeptidyl peptidases === +EC 3.4.14.1: dipeptidyl-peptidase I +EC 3.4.14.2: dipeptidyl-peptidase II +EC 3.4.14.3: Now EC 3.4.19.1, acylaminoacyl-peptidase +EC 3.4.14.4: dipeptidyl-peptidase III +EC 3.4.14.5: dipeptidyl-peptidase IV +EC 3.4.14.6: dipeptidyl-dipeptidase +EC 3.4.14.7: Deleted +EC 3.4.14.8: Now EC 3.4.14.10, tripeptidyl-peptidase II +EC 3.4.14.9: tripeptidyl-peptidase I +EC 3.4.14.10: tripeptidyl-peptidase II +EC 3.4.14.11: Xaa-Pro dipeptidyl-peptidase +EC 3.4.14.12: Xaa-Xaa-Pro tripeptidyl-peptidase +EC 3.4.14.13: γ-D-glutamyl-Llysine dipeptidyl-peptidase +EC 3.4.14.14: [mycofactocin precursor peptide] peptidase + +=== EC 3.4.15 Peptidyl dipeptidases === +EC 3.4.15.1: peptidyl-dipeptidase A +EC 3.4.15.2: Now EC 3.4.19.2, peptidyl-glycinamidase +EC 3.4.15.3: Now EC 3.4.15.5, peptidyl-dipeptidase Dcp +EC 3.4.15.4: Peptidyl-dipeptidase B +EC 3.4.15.5: Peptidyl-dipeptidase Dcp +EC 3.4.15.6: cyanophycinase + +=== EC 3.4.16 Serine type carboxypeptidases === +EC 3.4.16.1: Transferred entry: serine carboxypeptidase. Now EC 3.4.16.6, carboxypeptidase D +EC 3.4.16.2: lysosomal Pro-Xaa carboxypeptidase +EC 3.4.16.3: Now included with EC 3.4.16.5, carboxypeptidase C +EC 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase +EC 3.4.16.5: carboxypeptidase C +EC 3.4.16.6: carboxypeptidase D + +=== EC 3.4.17 Metallocarboxypeptidases === +EC 3.4.17.1: carboxypeptidase A +EC 3.4.17.2: carboxypeptidase B +EC 3.4.17.3: lysine carboxypeptidase +EC 3.4.17.4: Gly-Xaa carboxypeptidase +EC 3.4.17.5: Deleted +EC 3.4.17.6: alanine carboxypeptidase +EC 3.4.17.7: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase +EC 3.4.17.8: muramoylpentapeptide carboxypeptidase +EC 3.4.17.9: Now included with EC 3.4.17.4, Gly-Xaa carboxypeptidase +EC 3.4.17.10: carboxypeptidase E +EC 3.4.17.11: glutamate carboxypeptidase +EC 3.4.17.12: carboxypeptidase M +EC 3.4.17.13: Muramoyltetrapeptide carboxypeptidase +EC 3.4.17.14: zinc D-Ala-D-Ala carboxypeptidase +EC 3.4.17.15: carboxypeptidase A2 +EC 3.4.17.16: membrane Pro-Xaa carboxypeptidase +EC 3.4.17.17: tubulinyl-Tyr carboxypeptidase +EC 3.4.17.18: carboxypeptidase T +EC 3.4.17.19: Carboxypeptidase Taq +EC 3.4.17.20: carboxypeptidase U +EC 3.4.17.21: Glutamate carboxypeptidase II +EC 3.4.17.22: metallocarboxypeptidase D +EC 3.4.17.23: angiotensin-converting enzyme 2 +EC 3.4.17.24: tubulin-glutamate carboxypeptidase + +=== EC 3.4.18 Cysteine type carboxypeptidases === +EC 3.4.18.1: cathepsin X + +=== EC 3.4.19 Omega peptidases === +EC 3.4.19.1: acylaminoacyl-peptidase +EC 3.4.19.2: peptidyl-glycinamidase +EC 3.4.19.3: pyroglutamyl-peptidase I +EC 3.4.19.4: Deleted +EC 3.4.19.5: β-aspartyl-peptidase +EC 3.4.19.6: pyroglutamyl-peptidase II +EC 3.4.19.7: N-formylmethionyl-peptidase +EC 3.4.19.8: now EC 3.4.17.21, glutamate carboxypeptidase II +EC 3.4.19.9: folate γ-glutamyl hydrolase +EC 3.4.19.10: Now EC 3.5.1.28, N-acetylmuramoyl-L-alanine amidase +EC 3.4.19.11: γ-Dglutamyl-meso-diaminopimelate peptidase +EC 3.4.19.12: ubiquitinyl hydrolase 1 +EC 3.4.19.13: glutathione γ-glutamate hydrolase +EC 3.4.19.14: leukotriene-C4 hydrolase +EC 3.4.19.15: desampylase +EC 3.4.19.16: glucosinolate γ-glutamyl hydrolase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-6.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-6.md new file mode 100644 index 000000000..8554656d7 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-6.md @@ -0,0 +1,205 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 7/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== EC 3.4.21: Serine proteases === +EC 3.4.21.1: chymotrypsin +EC 3.4.21.2: chymotrypsin C +EC 3.4.21.3: metridin +EC 3.4.21.4: trypsin +EC 3.4.21.5: thrombin +EC 3.4.21.6: coagulation factor Xa +EC 3.4.21.7: plasmin +EC 3.4.21.8: Now EC 3.4.21.34 (plasma kallikrein) and EC 3.4.21.35 (tissue kallikrein) +EC 3.4.21.9: enteropeptidase +EC 3.4.21.10: acrosin +EC 3.4.21.11: Now EC 3.4.21.37, leukocyte elastase +EC 3.4.21.12: α-lytic endopeptidase +EC 3.4.21.13: Now EC 3.4.16.6, carboxypeptidase D +EC 3.4.21.14: now EC 3.4.21.67, endopeptidase So +EC 3.4.21.15: Now EC 3.4.21.63, oryzin +EC 3.4.21.16: Deleted +EC 3.4.21.17: Deleted +EC 3.4.21.18: Deleted +EC 3.4.21.19: glutamyl endopeptidase +EC 3.4.21.20: cathepsin G +EC 3.4.21.21: coagulation factor VIIa +EC 3.4.21.22: coagulation factor IXa +EC 3.4.21.23: Deleted +EC 3.4.21.24: Deleted +EC 3.4.21.25: cucumisin +EC 3.4.21.26: prolyl oligopeptidase +EC 3.4.21.27: coagulation factor XIa +EC 3.4.21.28: Now EC 3.4.21.74, venombin A +EC 3.4.21.29: Now EC 3.4.21.74, venombin A +EC 3.4.21.30: Now EC 3.4.21.74, venombin A +EC 3.4.21.31: Now EC 3.4.21.73, u-plasminogen activator +EC 3.4.21.32: brachyurin +EC 3.4.21.33: Deleted +EC 3.4.21.34: plasma kallikrein +EC 3.4.21.35: tissue kallikrein +EC 3.4.21.36: pancreatic elastase +EC 3.4.21.37: leukocyte elastase +EC 3.4.21.38: coagulation factor XIIa +EC 3.4.21.39: chymase +EC 3.4.21.40: Deleted +EC 3.4.21.41: Complement subcomponent C1r +EC 3.4.21.42: complement subcomponent C1s +EC 3.4.21.43: classical-complement-pathway C3/C5 convertase +EC 3.4.21.44: Now EC 3.4.21.43, classical-complement-pathway C3/C5 convertase +EC 3.4.21.45: complement factor I +EC 3.4.21.46: complement factor D +EC 3.4.21.47: alternative-complement-pathway C3/C5 convertase +EC 3.4.21.48: cerevisin +EC 3.4.21.49: hypodermin C +EC 3.4.21.50: lysyl endopeptidase +EC 3.4.21.51: Deleted +EC 3.4.21.52: Deleted +EC 3.4.21.53: edopeptidase La +EC 3.4.21.54: γ-renin +EC 3.4.21.55: venombin AB +EC 3.4.21.56: Now considered to be EC 3.4.21.25, cucumisin +EC 3.4.21.57: leucyl endopeptidase +EC 3.4.21.58: Deleted +EC 3.4.21.59: tryptase +EC 3.4.21.60: scutelarin +EC 3.4.21.61: kexin +EC 3.4.21.62: subtilisin +EC 3.4.21.63: oryzin +EC 3.4.21.64: endopeptidase K +EC 3.4.21.65: thermomycolin +EC 3.4.21.66: thermitase +EC 3.4.21.67: endopeptidase So +EC 3.4.21.68: t-plasminogen activator +EC 3.4.21.69: protein C (activated) +EC 3.4.21.70: pancreatic endopeptidase E +EC 3.4.21.71: pancreatic elastase II +EC 3.4.21.72: IgA-specific serine endopeptidase +EC 3.4.21.73: u-plasminogen activator +EC 3.4.21.74: venombin A +EC 3.4.21.75: furin +EC 3.4.21.76: myeloblastin +EC 3.4.21.77: semenogelase +EC 3.4.21.78: granzyme A +EC 3.4.21.79: granzyme B +EC 3.4.21.80: streptogrisin A +EC 3.4.21.81: streptogrisin B +EC 3.4.21.82: glutamyl endopeptidase II +EC 3.4.21.83: oligopeptidase B +EC 3.4.21.84: limulus clotting factor C +EC 3.4.21.85: limulus clotting factor B +EC 3.4.21.86: limulus clotting enzyme +EC 3.4.21.87: Now EC 3.4.23.49, omptin +EC 3.4.21.88: repressor LexA +EC 3.4.21.89: signal peptidase I +EC 3.4.21.90: togavirin +EC 3.4.21.91: flavivirin +EC 3.4.21.92: endopeptidase Clp +EC 3.4.21.93: proprotein convertase 1 +EC 3.4.21.94: proprotein convertase 2 +EC 3.4.21.95: snake venom factor V activator +EC 3.4.21.96: lactocepin +EC 3.4.21.97: assemblin +EC 3.4.21.98: hepacivirin +EC 3.4.21.99: spermosin +EC 3.4.21.100: sedolisin +EC 3.4.21.101: xanthomonalisin +EC 3.4.21.102: C-terminal processing peptidase +EC 3.4.21.103: physarolisin +EC 3.4.21.104: mannan-binding lectin-associated serine protease-2 +EC 3.4.21.105: rhomboid protease +EC 3.4.21.106: hepsin +EC 3.4.21.107: peptidase Do +EC 3.4.21.108: HtrA2 peptidase +EC 3.4.21.109: matriptase +EC 3.4.21.110: C5a peptidase +EC 3.4.21.111: aqualysin 1 +EC 3.4.21.112: site-1 protease +EC 3.4.21.113: pestivirus NS3 polyprotein peptidase +EC 3.4.21.114: equine arterivirus serine peptidase +EC 3.4.21.115: infectious pancreatic necrosis birnavirus Vp4 peptidase +EC 3.4.21.116: SpoIVB peptidase +EC 3.4.21.117: stratum corneum chymotryptic enzyme +EC 3.4.21.118: kallikrein 8 +EC 3.4.21.119: kallikrein 13 +EC 3.4.21.120: oviductin +EC 3.4.21.121: Lys-Lys/Arg-Xaa endopeptidase + +=== EC 3.4.22 Cysteine proteases === +EC 3.4.22.1: cathepsin B +EC 3.4.22.2: papain +EC 3.4.22.3: ficain +EC 3.4.22.4: Now EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain) +EC 3.4.22.5: Now EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain) +EC 3.4.22.6: chymopapain +EC 3.4.22.7: asclepain +EC 3.4.22.8: clostripain +EC 3.4.22.9: Now EC 3.4.21.48, cerevisin +EC 3.4.22.10: streptopain +EC 3.4.22.11: Now EC 3.4.24.56, insulysin +EC 3.4.22.12: Now EC 3.4.19.9, γ-glutamyl hydrolase +EC 3.4.22.13: Deleted +EC 3.4.22.14: actinidain +EC 3.4.22.15: cathepsin L +EC 3.4.22.16: cathepsin H +EC 3.4.22.17: Now EC 3.4.22.53, calpain-2 +EC 3.4.22.18: Now EC 3.4.21.26, prolyl oligopeptidase +EC 3.4.22.19: Now EC 3.4.24.15, thimet oligopeptidase +EC 3.4.22.20: Deleted +EC 3.4.22.21: Now EC 3.4.25.1, proteasome endopeptidase complex +EC 3.4.22.22: Now EC 3.4.24.37, saccharolysin +EC 3.4.22.23: Now EC 3.4.21.61, kexin +EC 3.4.22.24: Cathepsin T +EC 3.4.22.25: Glycyl endopeptidase +EC 3.4.22.26: Cancer procoagulant +EC 3.4.22.27: cathepsin S +EC 3.4.22.28: picornain 3C +EC 3.4.22.29: picornain 2A +EC 3.4.22.30: Caricain +EC 3.4.22.31: Ananain +EC 3.4.22.32: Stem bromelain +EC 3.4.22.33: Fruit bromelain +EC 3.4.22.34: Legumain +EC 3.4.22.35: Histolysain +EC 3.4.22.36: caspase-1 +EC 3.4.22.37: Gingipain R +EC 3.4.22.38: Cathepsin K +EC 3.4.22.39: adenain +EC 3.4.22.40: bleomycin hydrolase +EC 3.4.22.41: cathepsin F +EC 3.4.22.42: cathepsin O +EC 3.4.22.43: cathepsin V +EC 3.4.22.44: nuclear-inclusion-a endopeptidase +EC 3.4.22.45: helper-component proteinase +EC 3.4.22.46: L-peptidase +EC 3.4.22.47: gingipain K +EC 3.4.22.48: staphopain +EC 3.4.22.49: separase +EC 3.4.22.50: V-cath endopeptidase +EC 3.4.22.51: cruzipain +EC 3.4.22.52: calpain-1 +EC 3.4.22.53: calpain-2 +EC 3.4.22.54: calpain-3 +EC 3.4.22.55: caspase-2 +EC 3.4.22.56: caspase-3 +EC 3.4.22.57: caspase-4 +EC 3.4.22.58: caspase-5 +EC 3.4.22.59: caspase-6 +EC 3.4.22.60: caspase-7 +EC 3.4.22.61: caspase-8 +EC 3.4.22.62: caspase-9 +EC 3.4.22.63: caspase-10 +EC 3.4.22.64: caspase-11 +EC 3.4.22.65: peptidase 1 (mite) +EC 3.4.22.66: calicivirin +EC 3.4.22.67: zingipain +EC 3.4.22.68: Ulp1 peptidase +EC 3.4.22.69: SARS coronavirus main proteinase +EC 3.4.22.70: sortase A +EC 3.4.22.71: sortase B \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-7.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-7.md new file mode 100644 index 000000000..1a7c1e119 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-7.md @@ -0,0 +1,198 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 8/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== EC 3.4.23 Aspartic endopeptidases === +EC 3.4.23.1: pepsin A +EC 3.4.23.2: pepsin B +EC 3.4.23.3: gastricsin +EC 3.4.23.4: chymosin +EC 3.4.23.5: cathepsin D +EC 3.4.23.6: Now EC 3.4.23.30, pycnoporopepsin +EC 3.4.23.7: Now EC 3.4.23.20, penicillopepsin +EC 3.4.23.8: Now EC 3.4.23.25, saccharopepsin +EC 3.4.23.9: Now EC 3.4.23.21, rhizopuspepsin +EC 3.4.23.10: Now EC 3.4.23.22, endothiapepsin +EC 3.4.23.11: Deleted entry +EC 3.4.23.12: nepenthesin +EC 3.4.23.13: Deleted +EC 3.4.23.14: Deleted +EC 3.4.23.15: renin +EC 3.4.23.16: HIV-1 retropepsin +EC 3.4.23.17: pro-opiomelanocortin converting enzyme +EC 3.4.23.18: aspergillopepsin I +EC 3.4.23.19: aspergillopepsin II +EC 3.4.23.20: penicillopepsin +EC 3.4.23.21: rhizopuspepsin +EC 3.4.23.22: endothiapepsin +EC 3.4.23.23: mucorpepsin +EC 3.4.23.24: candidapepsin +EC 3.4.23.25: saccharopepsin +EC 3.4.23.26: rhodotorulapepsin +EC 3.4.23.27: Now EC 3.4.21.103, physarolisin +EC 3.4.23.28: acrocylindropepsin +EC 3.4.23.29: polyporopepsin +EC 3.4.23.30: pycnoporopepsin +EC 3.4.23.31: scytalidopepsin A +EC 3.4.23.32: scytalidopepsin B +EC 3.4.23.33: Now EC 3.4.21.101, xanthomonalisin +EC 3.4.23.34: cathepsin E +EC 3.4.23.35: barrierpepsin +EC 3.4.23.36: signal peptidase II +EC 3.4.23.37: Now EC 3.4.21.100, pseudomonalisin +EC 3.4.23.38: plasmepsin I +EC 3.4.23.39: plasmepsin II +EC 3.4.23.40: phytepsin +EC 3.4.23.41: yapsin 1 +EC 3.4.23.42: thermopsin +EC 3.4.23.43: prepilin peptidase +EC 3.4.23.44: nodavirus endopeptidase +EC 3.4.23.45: memapsin 1 +EC 3.4.23.46: memapsin 2 +EC 3.4.23.47: HIV-2 retropepsin +EC 3.4.23.48: plasminogen activator Pla +EC 3.4.23.49: omptin +EC 3.4.23.50: human endogenous retrovirus K endopeptidase +EC 3.4.23.51: HycI peptidase +EC 3.4.23.52: preflagellin peptidase + +=== EC 3.4.24: Metallopeptidases === +EC 3.4.24.1: atrolysin A +EC 3.4.24.2: Deleted entry: Sepia proteinase +EC 3.4.24.3: microbial collagenase +EC 3.4.24.4: now EC 3.4.24.40 serralysin +EC 3.4.24.5: Deleted entry: lens neutral proteinase. Now included with EC 3.4.22.53 (calpain-2) and EC 3.4.25.1 (proteasome endopeptidase complex) +EC 3.4.24.6: leucolysin +EC 3.4.24.7: interstitial collagenase +EC 3.4.24.8: Transferred entry: Achromobacter iophagus collagenase. Now EC 3.4.24.3, microbial collagenase +EC 3.4.24.9: Deleted entry: Trichophyton schoenleinii collagenase +EC 3.4.24.10: Deleted entry: Trichophyton mentagrophytes keratinase +EC 3.4.24.11: neprilysin +EC 3.4.24.12: envelysin +EC 3.4.24.13: IgA-specific metalloendopeptidase +EC 3.4.24.14: procollagen N-endopeptidase +EC 3.4.24.15: thimet oligopeptidase +EC 3.4.24.16: neurolysin +EC 3.4.24.17: stromelysin 1 +EC 3.4.24.18: meprin A +EC 3.4.24.19: procollagen C-endopeptidase +EC 3.4.24.20: peptidyl-Lys metalloendopeptidase +EC 3.4.24.21: astacin +EC 3.4.24.22: stromelysin 2 +EC 3.4.24.23: matrilysin +EC 3.4.24.24: gelatinase a +EC 3.4.24.25: vibriolysin +EC 3.4.24.26: pseudolysin +EC 3.4.24.27: thermolysin +EC 3.4.24.28: bacillolysin +EC 3.4.24.29: aureolysin +EC 3.4.24.30: coccolysin +EC 3.4.24.31: mycolysin +EC 3.4.24.32: β-lytic metalloendopeptidase +EC 3.4.24.33: peptidyl-Asp metalloendopeptidase +EC 3.4.24.34: neutrophil collagenase +EC 3.4.24.35: gelatinase B +EC 3.4.24.36: leishmanolysin +EC 3.4.24.37: saccharolysin +EC 3.4.24.38: gametolysin +EC 3.4.24.39: deuterolysin +EC 3.4.24.40: serralysin +EC 3.4.24.41: atrolysin B +EC 3.4.24.42: atrolysin C +EC 3.4.24.43: atroxase +EC 3.4.24.44: atrolysin E +EC 3.4.24.45: atrolysin F +EC 3.4.24.46: adamalysin +EC 3.4.24.47: horrilysin +EC 3.4.24.48: ruberlysin +EC 3.4.24.49: bothropasin +EC 3.4.24.50: bothrolysin +EC 3.4.24.51: ophiolysin +EC 3.4.24.52: trimerelysin I +EC 3.4.24.53: trimerelysin II +EC 3.4.24.54: mucrolysin +EC 3.4.24.55: pitrilysin +EC 3.4.24.56: insulysin +EC 3.4.24.57: O-sialoglycoprotein endopeptidase +EC 3.4.24.58: russellysin +EC 3.4.24.59: mitochondrial intermediate peptidase +EC 3.4.24.60: dactylysin +EC 3.4.24.61: nardilysin +EC 3.4.24.62: magnolysin +EC 3.4.24.63: meprin B +EC 3.4.24.64: mitochondrial processing peptidase +EC 3.4.24.65: macrophage elastase +EC 3.4.24.66: choriolysin L +EC 3.4.24.67: choriolysin H +EC 3.4.24.68: tentoxilysin +EC 3.4.24.69: bontoxilysin +EC 3.4.24.70: oligopeptidase A +EC 3.4.24.71: endothelin-converting enzyme 1 +EC 3.4.24.72: fibrolase +EC 3.4.24.73: jararhagin +EC 3.4.24.74: fragilysin +EC 3.4.24.75: lysostaphin +EC 3.4.24.76: flavastacin +EC 3.4.24.77: snapalysin +EC 3.4.24.78: gpr endopeptidase +EC 3.4.24.79: pappalysin-1 +EC 3.4.24.80: membrane-type matrix metalloproteinase-1 +EC 3.4.24.81: ADAM10 endopeptidase +EC 3.4.24.82: ADAMTS-4 endopeptidase +EC 3.4.24.83: anthrax lethal factor endopeptidase +EC 3.4.24.84: Ste24 endopeptidase +EC 3.4.24.85: S2P endopeptidase +EC 3.4.24.86: ADAM 17 endopeptidase +EC 3.4.24.87: ADAMTS13 endopeptidase + +=== EC 3.4.25 Threonine endopeptidases === +EC 3.4.25.1: proteasome endopeptidase complex +EC 3.4.25.2: HslU—HslV peptidase +EC 3.4.99.7: Deleted entry: euphorbain +EC 3.4.99.8: Deleted entry: Gliocladium proteinase +EC 3.4.99.9: Deleted entry: hurain. Now considered to be EC 3.4.21.25, cucumisin +EC 3.4.99.10: Transferred entry: insulinase. Now EC 3.4.24.56, insulysin +EC 3.4.99.11: Deleted entry: Streptomyces alkalophilic keratinase +EC 3.4.99.12: Deleted entry: Trichophyton mentagrophytes keratinase +EC 3.4.99.13: Transferred entry: β-lytic proteinase (Mycobacterium sorangium). Now EC 3.4.24.32 EC 3.4.24.32, β-lytic metalloendopeptidase +EC 3.4.99.14: Deleted entry: mexicanain +EC 3.4.99.15: Deleted entry: Paecilomyces proteinase +EC 3.4.99.16: Deleted entry: Penicillium notatum extracellular proteinase +EC 3.4.99.17: Deleted entry: peptidoglycan endopeptidase +EC 3.4.99.18: Deleted entry: pinguinain +EC 3.4.99.19: Transferred entry: renin. Now EC 3.4.23.15, renin +EC 3.4.99.20: Deleted entry: scopulariopsis proteinase +EC 3.4.99.21: Deleted entry: solanain. Now considered EC 3.4.21.25, cucumisin +EC 3.4.99.22: Transferred entry: staphylokinase. EC 3.4.24.29, aureolysin +EC 3.4.99.23: Deleted entry: tabernamontanain. Now considered EC 3.4.21.25, cucumisin +EC 3.4.99.24: Deleted entry: Tenebrio α-proteinase +EC 3.4.99.25: Transferred entry: trametes acid proteinase. EC 3.4.23.21, rhizopuspepsin +EC 3.4.99.26: Transferred entry: urokinase. Now EC 3.4.21.68, t-plasminogen activator +EC 3.4.99.27: Deleted entry: Echis carinatus prothrombin-activating proteinase +EC 3.4.99.28: Transferred entry: Oxyuranus scutellatus prothrombin-activating proteinase. EC 3.4.21.60 EC 3.4.21.60, scutelarin +EC 3.4.99.29: Deleted entry: Myxobacter AL-1 proteinase I +EC 3.4.99.30: Transferred entry: Myxobacter AL-1 proteinase II. EC 3.4.24.20, peptidyl-Lys metalloendopeptidase +EC 3.4.99.31: Transferred entry: tissue endopeptidase degrading collagenase synthetic substrate. EC 3.4.24.15, thimet oligopeptidase +EC 3.4.99.32: Transferred entry: Armillaria mellea neutral proteinase. Now EC 3.4.24.20, peptidyl-Lys metalloendopeptidase +EC 3.4.99.33: Deleted entry: cathepsin R +EC 3.4.99.34: Deleted entry: mytilidase +EC 3.4.99.35: Transferred entry: premurein-leader peptidase. Now EC 3.4.23.36, signal peptidase II +EC 3.4.99.36: Transferred entry: leader peptidase. Now EC 3.4.21.89, signal peptidase I +EC 3.4.99.37: Deleted entry: RecA peptidase +EC 3.4.99.38: Transferred entry: pro-opiomelanotropin-converting proteinase. Now EC 3.4.23.17, pro-opiomelanocortin converting enzyme +EC 3.4.99.39: Deleted entry: pseudomurein endopeptidase +EC 3.4.99.40: Deleted entry: pro-gonadoliberin proteinase +EC 3.4.99.41: Transferred entry: mitochondrial processing peptidase. Now EC 3.4.24.64, mitochondrial processing peptidase +EC 3.4.99.42: Deleted entry: leucyllysine endopeptidase +EC 3.4.99.43: Transferred entry: thermopsin. Npw EC 3.4.23.42, thermopsin +EC 3.4.99.44: Transferred entry: pitrilysin. Now EC 3.4.24.55, pitrilysin +EC 3.4.99.45: Transferred entry: insulinase. Now EC 3.4.24.56, insulysin +EC 3.4.99.46: Transferred entry: multicatalytic endopeptidase complex. Now EC 3.4.25.1, proteasome endopeptidase complex + +== EC 3.5: Acting on carbon-nitrogen bonds, other than peptide bonds == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-8.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-8.md new file mode 100644 index 000000000..dee87802a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-8.md @@ -0,0 +1,245 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 9/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== 3.5.1: In linear amides === +EC 3.5.1.1: asparaginase +EC 3.5.1.2: glutaminase +EC 3.5.1.3: ω-amidase +EC 3.5.1.4: amidase +EC 3.5.1.5: urease +EC 3.5.1.6: β-ureidopropionase +EC 3.5.1.7: ureidosuccinase +EC 3.5.1.8: formylaspartate deformylase +EC 3.5.1.9: arylformamidase +EC 3.5.1.10: formyltetrahydrofolate deformylase +EC 3.5.1.11: penicillin amidase +EC 3.5.1.12: biotinidase +EC 3.5.1.13: aryl-acylamidase +EC 3.5.1.14: N-acyl-aliphatic-L-amino acid amidohydrolase +EC 3.5.1.15: aspartoacylase +EC 3.5.1.16: acetylornithine deacetylase +EC 3.5.1.17: acyl-lysine deacylase +EC 3.5.1.18: succinyl-diaminopimelate desuccinylase +EC 3.5.1.19: nicotinamidase +EC 3.5.1.20: citrullinase +EC 3.5.1.21: N-acetyl-β-alanine deacetylas +EC 3.5.1.22: pantothenase +EC 3.5.1.23: ceramidase +EC 3.5.1.24: choloylglycine hydrolase +EC 3.5.1.25: N-acetylglucosamine-6-phosphate deacetylase +EC 3.5.1.26: N4-(β-N-acetylglucosaminyl)-L-asparaginase +EC 3.5.1.27: The activity is covered by EC 3.5.1.88, peptide deformylase +EC 3.5.1.28: N-acetylmuramoyl-L-alanine amidase +EC 3.5.1.29: 2-(acetamidomethylene)succinate hydrolase +EC 3.5.1.30: 5-aminopentanamidase +EC 3.5.1.31: formylmethionine deformylase +EC 3.5.1.32: hippurate hydrolase +EC 3.5.1.33: N-acetylglucosamine deacetylase +EC 3.5.1.34: [[Identical with ((EnzExplorer|3.4.13.5)), Xaa-methyl-His dipeptidase|Identical with EC 3.4.13.5, Xaa-methyl-His dipeptidase]] +EC 3.5.1.35: D-glutaminase +EC 3.5.1.36: N-methyl-2-oxoglutaramate hydrolase +EC 3.5.1.37: [[Delete, identical with ((EnzExplorer|3.5.1.26)) N(4)-(β-N-acetylglucosaminyl)-L-asparaginase|Delete, identical with EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase]] +EC 3.5.1.38: glutamin-(asparagin-)ase +EC 3.5.1.39: alkylamidase +EC 3.5.1.40: acylagmatine amidase +EC 3.5.1.41: chitin deacetylase +EC 3.5.1.42: nicotinamide-nucleotide amidase +EC 3.5.1.43: peptidyl-glutaminase +EC 3.5.1.44: protein-glutamine glutaminase +EC 3.5.1.45: Now listed only as EC 6.3.4.6 urea carboxylase +EC 3.5.1.46: 6-aminohexanoate-dimer hydrolase +EC 3.5.1.47: N-acetyldiaminopimelate deacetylase +EC 3.5.1.48: acetylspermidine deacetylase +EC 3.5.1.49: formamidase +EC 3.5.1.50: pentanamidase +EC 3.5.1.51: 4-acetamidobutyryl-CoA deacetylase +EC 3.5.1.52: peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase +EC 3.5.1.53: N-carbamoylputrescine amidase +EC 3.5.1.54: allophanate hydrolase +EC 3.5.1.55: long-chain-fatty-acyl-glutamate deacylase +EC 3.5.1.56: N,N-dimethylformamidase +EC 3.5.1.57: tryptophanamidase +EC 3.5.1.58: N-benzyloxycarbonylglycine hydrolase +EC 3.5.1.59: N-carbamoylsarcosine amidase +EC 3.5.1.60: N-(long-chain-acyl)ethanolamine deacylase +EC 3.5.1.61: mimosinase +EC 3.5.1.62: acetylputrescine deacetylase +EC 3.5.1.63: 4-acetamidobutyrate deacetylase +EC 3.5.1.64: Nα-benzyloxycarbonylleucine hydrolase +EC 3.5.1.65: theanine hydrolase +EC 3.5.1.66: 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase +EC 3.5.1.67: 4-methyleneglutaminase +EC 3.5.1.68: N-formylglutamate deformylase +EC 3.5.1.69: glycosphingolipid deacylase +EC 3.5.1.70: aculeacin-A deacylase +EC 3.5.1.71: N-feruloylglycine deacylase +EC 3.5.1.72: D-benzoylarginine-4-nitroanilide amidase +EC 3.5.1.73: carnitinamidase +EC 3.5.1.74: chenodeoxycholoyltaurine hydrolase +EC 3.5.1.75: urethanase +EC 3.5.1.76: arylalkyl acylamidase +EC 3.5.1.77: N-carbamoyl-D-amino-acid hydrolase +EC 3.5.1.78: glutathionylspermidine amidase +EC 3.5.1.79: phthalyl amidase +EC 3.5.1.80: Identical to EC 3.5.1.25, N-acetylglucosamine-6-phosphate deacetylase +EC 3.5.1.81: N-acyl-D-amino-acid deacylase +EC 3.5.1.82: N-acyl-D-glutamate deacylase +EC 3.5.1.83: N-acyl-D-aspartate deacylase +EC 3.5.1.84: biuret amidohydrolase +EC 3.5.1.85: (S)-N-acetyl-1-phenylethylamine hydrolase +EC 3.5.1.86: mandelamide amidase +EC 3.5.1.87: N-carbamoyl-L-amino-acid hydrolase +EC 3.5.1.88: peptide deformylase +EC 3.5.1.89: N-acetylglucosaminylphosphatidylinositol deacetylase +EC 3.5.1.90: adenosylcobinamide hydrolase +EC 3.5.1.91: N-substituted formamide deformylase +EC 3.5.1.92: pantetheine hydrolase +EC 3.5.1.93: glutaryl-7-aminocephalosporanic-acid acylase +EC 3.5.1.94: γ-glutamyl-γ-aminobutyrate hydrolase +EC 3.5.1.95: N-malonylurea hydrolase +EC 3.5.1.96: succinylglutamate desuccinylase +EC 3.5.1.97: acyl-homoserine-lactone acylase +EC 3.5.1.98: histone deacetylase +EC 3.5.1.99: fatty acid amide hydrolase +EC 3.5.1.100: (R)-amidase +EC 3.5.1.101: L-proline amide hydrolase +EC 3.5.1.102: 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5′-monophosphate deformylase +EC 3.5.1.103: N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-α-D-glucopyranoside deacetylase +EC 3.5.1.104: peptidoglycan-N-acetylglucosamine deacetylase +EC 3.5.1.105: chitin disaccharide deacetylase +EC 3.5.1.106: N-formylmaleamate deformylase +EC 3.5.1.107: maleamate amidohydrolase +EC 3.5.1.108: UDP-3-O-acyl-N-acetylglucosamine deacetylase +EC 3.5.1.109: sphingomyelin deacylase +EC 3.5.1.110: ureidoacrylate amidohydrolase +EC 3.5.1.111: 2-oxoglutaramate amidase +EC 3.5.1.112: 2′-N-acetylparomamine deacetylase +EC 3.5.1.113: 2′′′-acetyl-6′′′-hydroxyneomycin C deacetylase +EC 3.5.1.114: N-acyl-aromatic-L-amino acid amidohydrolase +EC 3.5.1.115: mycothiol S-conjugate amidase +EC 3.5.1.116: ureidoglycolate amidohydrolase +EC 3.5.1.117: 6-aminohexanoate-oligomer endohydrolase +EC 3.5.1.118: γ-glutamyl hercynylcysteine S-oxide hydrolase +EC 3.5.1.119: Pup amidohydrolase +EC 3.5.1.120: Now EC 3.5.99.11, 2-aminomuconate deaminase (2-hydroxymuconate-forming) +EC 3.5.1.121: protein N-terminal asparagine amidohydrolase +EC 3.5.1.122: protein N-terminal glutamine amidohydrolase +EC 3.5.1.123: γ-glutamylanilide hydrolase +EC 3.5.1.124: protein deglycase +EC 3.5.1.125: N 2-acetyl-L-2,4-diaminobutanoate deacetylase +EC 3.5.1.126: oxamate amidohydrolase +EC 3.5.1.127: jasmonoyl-L-amino acid hydrolase +EC 3.5.1.128: deaminated glutathione amidase +EC 3.5.1.129: N 5-(cytidine 5′-diphosphoramidyl)-L-glutamine hydrolase +EC 3.5.1.130: [amino group carrier protein]-lysine hydrolase +EC 3.5.1.131: 1-carboxybiuret hydrolase +EC 3.5.1.132: [amino group carrier protein]-ornithine hydrolase +EC 3.5.1.133: N α-acyl-L-glutamine aminoacylase +EC 3.5.1.134: (indol-3-yl)acetyl-L-aspartate hydrolase +EC 3.5.1.135: N 4-acetylcytidine amidohydrolase +EC 3.5.1.136: N,N′-diacetylchitobiose non-reducing end deacetylase + +=== 3.5.2: In cyclic amides === +EC 3.5.2.1: barbiturase +EC 3.5.2.2: dihydropyrimidinase +EC 3.5.2.3: dihydroorotase +EC 3.5.2.4: carboxymethylhydantoinase +EC 3.5.2.5: allantoinase +EC 3.5.2.6: β-lactamase +EC 3.5.2.7: imidazolonepropionase +EC 3.5.2.8: Now included with EC 3.5.2.6, β-lactamase +EC 3.5.2.9: 5-oxoprolinase (ATP-hydrolysing) +EC 3.5.2.10: creatininase +EC 3.5.2.11: L-lysine-lactamase +EC 3.5.2.12: 6-aminohexanoate-cyclic-dimer hydrolase +EC 3.5.2.13: 2,5-dioxopiperazine hydrolase +EC 3.5.2.14: N-methylhydantoinase (ATP-hydrolysing) +EC 3.5.2.15: cyanuric acid amidohydrolase +EC 3.5.2.16: maleimide hydrolase +EC 3.5.2.17: hydroxyisourate hydrolase +EC 3.5.2.18: enamidase +EC 3.5.2.19: streptothricin hydrolase +EC 3.5.2.20: isatin hydrolase + +=== 3.5.3: In linear amidines === +EC 3.5.3.1: arginase +EC 3.5.3.2: guanidinoacetase +EC 3.5.3.3: creatinase +EC 3.5.3.4: allantoicase +EC 3.5.3.5: formimidoylaspartate deiminase +EC 3.5.3.6: arginine deiminase +EC 3.5.3.7: guanidinobutyrase +EC 3.5.3.8: formimidoylglutamase +EC 3.5.3.9: allantoate deiminase +EC 3.5.3.10: D-arginase +EC 3.5.3.11: agmatinase +EC 3.5.3.12: agmatine deiminase +EC 3.5.3.13: formimidoylglutamate deiminase +EC 3.5.3.14: amidinoaspartase +EC 3.5.3.15: protein-arginine deiminase +EC 3.5.3.16: methylguanidinase +EC 3.5.3.17: guanidinopropionase +EC 3.5.3.18: dimethylargininase +EC 3.5.3.19: Now EC 3.5.1.116, ureidoglycolate amidohydrolase +EC 3.5.3.20: diguanidinobutanase +EC 3.5.3.21: Methylenediurea deaminase +EC 3.5.3.22: proclavaminate amidinohydrolase +EC 3.5.3.23: N-succinylarginine dihydrolase +EC 3.5.3.24: N 1-aminopropylagmatine ureohydrolase +EC 3.5.3.25: N ω-hydroxy-L-arginine amidinohydrolase +EC 3.5.3.26: (S)-ureidoglycine aminohydrolase + +=== 3.5.4: In cyclic amidines === +EC 3.5.4.1: cytosine deaminase +EC 3.5.4.2: adenine deaminase +EC 3.5.4.3: guanine deaminase +EC 3.5.4.4: adenosine deaminase +EC 3.5.4.5: cytidine deaminase +EC 3.5.4.6: AMP deaminase +EC 3.5.4.7: ADP deaminase +EC 3.5.4.8: aminoimidazolase +EC 3.5.4.9: methenyltetrahydrofolate cyclohydrolase +EC 3.5.4.10: IMP cyclohydrolase +EC 3.5.4.11: pterin deaminase +EC 3.5.4.12: dCMP deaminase +EC 3.5.4.13: dCTP deaminase +EC 3.5.4.14: Now included in EC 3.5.4.5, (deoxy)cytidine deaminase +EC 3.5.4.15: guanosine deaminase +EC 3.5.4.16: GTP cyclohydrolase I +EC 3.5.4.17: adenosine-phosphate deaminase +EC 3.5.4.18: ATP deaminase +EC 3.5.4.19: phosphoribosyl-AMP cyclohydrolase +EC 3.5.4.20: pyrithiamine deaminase +EC 3.5.4.21: creatinine deaminase +EC 3.5.4.22: 1-pyrroline-4-hydroxy-2-carboxylate deaminase +EC 3.5.4.23: blasticidin-S deaminase +EC 3.5.4.24: sepiapterin deaminase +EC 3.5.4.25: GTP cyclohydrolase II +EC 3.5.4.26: diaminohydroxyphosphoribosylaminopyrimidine deaminase +EC 3.5.4.27: methenyltetrahydromethanopterin cyclohydrolase +EC 3.5.4.28: S-adenosylhomocysteine deaminase +EC 3.5.4.29: GTP cyclohydrolase IIa +EC 3.5.4.30: dCTP deaminase (dUMP-forming) +EC 3.5.4.31: S-methyl-5′-thioadenosine deaminase +EC 3.5.4.32: 8-oxoguanine deaminase +EC 3.5.4.33: tRNA(adenine34) deaminase +EC 3.5.4.34: tRNAAla(adenine37) deaminase +EC 3.5.4.35: tRNA(cytosine8) deaminase +EC 3.5.4.36: mRNA(cytosine6666) deaminase +EC 3.5.4.37: double-stranded RNA adenine deaminase +EC 3.5.4.38: single-stranded DNA cytosine deaminase +EC 3.5.4.39: GTP cyclohydrolase IV +EC 3.5.4.40: aminodeoxyfutalosine deaminase +EC 3.5.4.41: 5'-deoxyadenosine deaminase +EC 3.5.4.42: N-isopropylammelide isopropylaminohydrolase +EC 3.5.4.43: hydroxydechloroatrazine ethylaminohydrolase +EC 3.5.4.44: ectoine hydrolase +EC 3.5.4.45: melamine deaminase +EC 3.5.4.46: cAMP deaminase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-9.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-9.md new file mode 100644 index 000000000..28ab9624e --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)-9.md @@ -0,0 +1,171 @@ +--- +title: "List of EC numbers (EC 3)" +chunk: 10/11 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_3)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:08.231305+00:00" +instance: "kb-cron" +--- + +=== 3.5.5: In nitriles === +EC 3.5.5.1: nitrilase +EC 3.5.5.2: ricinine nitrilase +EC 3.5.5.3: Now EC 4.2.1.104, cyanate hydratase +EC 3.5.5.4: cyanoalanine nitrilase +EC 3.5.5.5: arylacetonitrilase +EC 3.5.5.6: bromoxynil nitrilase +EC 3.5.5.7: aliphatic nitrilase +EC 3.5.5.8: thiocyanate hydrolase + +=== 3.5.99: In other compounds === +EC 3.5.99.1: riboflavinase +EC 3.5.99.2: aminopyrimidine aminohydrolase +EC 3.5.99.3: Now EC 3.5.4.43, hydroxydechloroatrazine ethylaminohydrolase +EC 3.5.99.4: Now EC 3.5.4.42, N-isopropylammelide isopropylaminohydrolase +EC 3.5.99.5: 2-aminomuconate deaminase +EC 3.5.99.6: glucosamine-6-phosphate deaminase +EC 3.5.99.7: 1-aminocyclopropane-1-carboxylate deaminase +EC 3.5.99.8: 5-nitroanthranilic acid aminohydrolase +EC 3.5.99.9: 2-nitroimidazole nitrohydrolase +EC 3.5.99.10: 2-iminobutanoate/2-iminopropanoate deaminase +EC 3.5.99.11: 2-aminomuconate deaminase (2-hydroxymuconate-forming) +EC 3.5.99.14: (S)-norcoclaurine synthase + +== EC 3.6: Acting on acid anhydrides == + +=== 3.6.1: In phosphorus-containing anhydrides === +EC 3.6.1.1: inorganic diphosphatase +EC 3.6.1.2: trimetaphosphatase +EC 3.6.1.3: adenosinetriphosphatase +EC 3.6.1.4: Now included with EC 3.6.1.3, adenosinetriphosphatase +EC 3.6.1.5: apyrase +EC 3.6.1.6: nucleoside diphosphate phosphatase +EC 3.6.1.7: acylphosphatase +EC 3.6.1.8: ATP diphosphatase +EC 3.6.1.9: nucleotide diphosphatase +EC 3.6.1.10: endopolyphosphatase +EC 3.6.1.11: exopolyphosphatase +EC 3.6.1.12: dCTP diphosphatase +EC 3.6.1.13: ADP-ribose diphosphatase +EC 3.6.1.14: adenosine-tetraphosphatase +EC 3.6.1.15: nucleoside-triphosphatase +EC 3.6.1.16: CDP-glycerol diphosphatase +EC 3.6.1.17: bis(5′-nucleosyl)-tetraphosphatase (asymmetrical)) +EC 3.6.1.18: FAD diphosphatase +EC 3.6.1.19: Now EC 3.6.1.9, nucleotide diphosphatase +EC 3.6.1.20: 5′-acylphosphoadenosine hydrolase +EC 3.6.1.21: ADP-sugar diphosphatase +EC 3.6.1.22: NAD+ diphosphatase +EC 3.6.1.23: dUTP diphosphatase +EC 3.6.1.24: nucleoside phosphoacylhydrolase +EC 3.6.1.25: triphosphatase +EC 3.6.1.26: CDP-diacylglycerol diphosphatase +EC 3.6.1.27: undecaprenyl-diphosphatase +EC 3.6.1.28: thiamine-triphosphatase +EC 3.6.1.29: bis(5′-adenosyl)-triphosphatase +EC 3.6.1.30: Now covered by EC 3.6.1.59 [m7GpppX diphosphatase] and EC 3.6.1.62 [m7GpppN-mRNA hydrolase]. +EC 3.6.1.31: phosphoribosyl-ATP diphosphatase +EC 3.6.1.32: Now EC 3.6.4.1, myosin ATPase +EC 3.6.1.33: Now EC 3.6.4.2, dynein ATPase +EC 3.6.1.34: Transferred entry: H+-transporting ATP synthase. Now EC 3.6.3.14, H+-transporting two-sector ATPase +EC 3.6.1.35: Now EC 3.6.3.6, H+-exporting ATPase +EC 3.6.1.36: Now EC 3.6.3.10, H+/K+-exchanging ATPase +EC 3.6.1.37: Now EC 3.6.3.9, Na+/K+-exchanging ATPase +EC 3.6.1.38: Now EC 3.6.3.8, Ca2+-transporting ATPase +EC 3.6.1.39: thymidine-triphosphatase +EC 3.6.1.40: guanosine-5′-triphosphate,3′-diphosphate phosphatase +EC 3.6.1.41: bis(5′-nucleosyl)-tetraphosphatase (symmetrical) +EC 3.6.1.42: guanosine-diphosphatase +EC 3.6.1.43: dolichyldiphosphatase +EC 3.6.1.44: oligosaccharide-diphosphodolichol diphosphatase +EC 3.6.1.45: UDP-sugar diphosphatase +EC 3.6.1.46: Now EC 3.6.5.1, heterotrimeric G-protein GTPase +EC 3.6.1.47: Now EC 3.6.5.3, protein-synthesizing GTPase +EC 3.6.1.49: Now EC 3.6.5.4, signal-recognition-particle GTPase +EC 3.6.1.50: Now EC 3.6.5.5, dynamin GTPase +EC 3.6.1.51: Now EC 3.6.5.6, tubulin GTPase +EC 3.6.1.52: diphosphoinositol-polyphosphate diphosphatase +EC 3.6.1.53: Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase +EC 3.6.1.54: UDP-2,3-diacylglucosamine diphosphatase +EC 3.6.1.55: 8-oxo-dGTP diphosphatase +EC 3.6.1.56: 2-hydroxy-dATP diphosphatase +EC 3.6.1.57: UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose hydrolase +EC 3.6.1.58: 8-oxo-dGDP phosphatase +EC 3.6.1.59: 5′-(N7-methyl 5′-triphosphoguanosine)-[mRNA] diphosphatase +EC 3.6.1.60: diadenosine hexaphosphate hydrolase (AMP-forming) +EC 3.6.1.61: diadenosine hexaphosphate hydrolase (ATP-forming) +EC 3.6.1.62: 5′-(N7-methylguanosine 5′-triphospho)-[mRNA] hydrolase +EC 3.6.1.63: α-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase +EC 3.6.1.64: inosine diphosphate phosphatase +EC 3.6.1.65: (d)CTP diphosphatase +EC 3.6.1.66: XTP/dITP diphosphatase +EC 3.6.1.67: dihydroneopterin triphosphate diphosphatase +EC 3.6.1.68: geranyl diphosphate phosphohydrolase +EC 3.6.1.69: 8-oxo-(d)GTP phosphatase +EC 3.6.1.70: guanosine-5′-diphospho-5′-[DNA] diphosphatase +EC 3.6.1.71: adenosine-5′-diphospho-5′-[DNA] diphosphatase +EC 3.6.1.72: DNA-3′-diphospho-5′-guanosine diphosphatase +EC 3.6.1.73: inosine/xanthosine triphosphatase +EC 3.6.1.74: mRNA 5′-phosphatase + +=== 3.6.2: In sulfonyl-containing anhydrides === +EC 3.6.2.1: adenylylsulfatase +EC 3.6.2.2: phosphoadenylylsulfatase + +=== 3.6.3: Acting on acid anhydrides to catalyse transmembrane movement of substances === +EC 3.6.3.1: phospholipid-translocating ATPase +EC 3.6.3.2: Now EC 7.2.2.14, P-type Mg2+ transporter +EC 3.6.3.3: Now EC 7.2.2.21, Cd2+-exporting ATPase +EC 3.6.3.4: Now EC 7.2.2.9, Cu2+-exporting ATPase +EC 3.6.3.5: Now EC 7.2.2.12, Zn2+-exporting ATPase +EC 3.6.3.6: Now EC 7.1.2.1, P-type H+-exporting transporter +EC 3.6.3.7: Now EC 7.2.2.3, P-type Na+ transporter +EC 3.6.3.8: Now EC 7.2.2.10, Ca2+-transporting ATPase +EC 3.6.3.9: Now EC 7.2.2.13, Na+/K+-exchanging ATPase +EC 3.6.3.10: Now EC 7.2.2.19, H+/K+-exchanging ATPase +EC 3.6.3.11: "Cl–-transporting ATPase". The activity was only ever studied in crude extracts, and is an artifact +EC 3.6.3.12: Now EC 7.2.2.6, K+-transporting ATPase +EC 3.6.3.13:Identical to EC 3.6.3.1, phospholipid-translocating ATPase +EC 3.6.3.14: Now EC 7.1.2.2, H+-transporting two-sector ATPase +EC 3.6.3.15: Now EC 7.2.2.1, Na+-transporting two-sector ATPase +EC 3.6.3.16: Now EC 7.3.2.7, arsenite-transporting ATPase +EC 3.6.3.17: Now covered by various ABC-type monosaccharide transporters in sub-subclass EC 7.5.2 +EC 3.6.3.18: Now EC 7.5.2.2, ABC-type oligosaccharide transporter +EC 3.6.3.19: Now EC 7.5.2.1, ABC-type maltose transporter +EC 3.6.3.20: Now EC 7.6.2.10, glycerol-3-phosphate-transporting ATPase +EC 3.6.3.21: Now EC 7.4.2.1, ABC-type polar-amino-acid transporter +EC 3.6.3.22: Now EC 7.4.2.2, ABC-type nonpolar-amino-acid transporter +EC 3.6.3.23: Now EC 7.4.2.6, oligopeptide-transporting ATPase +EC 3.6.3.24: Now EC 7.2.2.11, nickel-transporting ATPase +EC 3.6.3.25: Now EC 7.3.2.3, sulfate-transporting ATPase +EC 3.6.3.26: Now EC 7.3.2.4, nitrate-transporting ATPase +EC 3.6.3.27: Now EC 7.3.2.1, ABC-type phosphate transporter +EC 3.6.3.28: Now EC 7.3.2.2, ABC-type phosphonate transporter +EC 3.6.3.29: Now EC 7.3.2.5, molybdate-transporting ATPase +EC 3.6.3.30: Now EC 7.2.2.7, Fe3+-transporting ATPase +EC 3.6.3.31: Now EC 7.6.2.11, polyamine-transporting ATPase +EC 3.6.3.32: Now EC 7.6.2.9, quaternary-amine-transporting ATPase +EC 3.6.3.33: Now EC 7.6.2.8, vitamin B12-transporting ATPase +EC 3.6.3.34: now recognized to be at least three separate enzymes EC 7.2.2.16, iron(III) hydroxamate ABC transporter, EC 7.2.2.17, ferric enterobactin ABC transporter, and EC 7.2.2.18, ferric citrate ABC transporter +EC 3.6.3.35: Now EC 7.2.2.5, manganese-transporting ATPase +EC 3.6.3.36: Now EC 7.6.2.7, taurine-transporting ATPase +EC 3.6.3.37: Now EC 7.6.2.6, guanine-transporting ATPase +EC 3.6.3.38: Now EC 7.6.2.12, ABC-type capsular-polysaccharide transporter +EC 3.6.3.39: Now EC 7.5.2.5, lipopolysaccharide-transporting ATPase +EC 3.6.3.40: Now EC 7.5.2.4, teichoic-acid-transporting ATPase +EC 3.6.3.41: Now EC 7.6.2.5, heme-transporting ATPase +EC 3.6.3.42: Now EC 7.5.2.3, β-glucan-transporting ATPase +EC 3.6.3.43: Now EC 7.4.2.5, peptide-transporting ATPase +EC 3.6.3.44: Now EC 7.6.2.2, ABC-type xenobiotic transporter +EC 3.6.3.45: Now included with EC 3.6.3.44, xenobiotic-transporting ATPase +EC 3.6.3.46: Now EC 7.2.2.2, ABC-type Cd2+ transporter +EC 3.6.3.47: Now EC 7.6.2.4, fatty-acyl-CoA-transporting ATPase +EC 3.6.3.48: Now EC 7.4.2.7 as α-factor-pheromone transporting ATPase +EC 3.6.3.49: Now EC 5.6.1.6, channel-conductance-controlling ATPase +EC 3.6.3.50: Now EC 7.4.2.8, protein-secreting ATPase +EC 3.6.3.51: Now EC 7.4.2.3, mitochondrial protein-transporting ATPase +EC 3.6.3.52: Now EC 7.4.2.4, chloroplast protein-transporting ATPase +EC 3.6.3.53: Now EC 7.2.2.15, Ag+-exporting ATPase +EC 3.6.3.54: Now EC 7.2.2.8, Cu+-exporting ATPase +EC 3.6.3.55: Now EC 7.3.2.6, tungstate-importing ATPase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-0.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-0.md new file mode 100644 index 000000000..b57187914 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-0.md @@ -0,0 +1,202 @@ +--- +title: "List of EC numbers (EC 4)" +chunk: 1/5 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:09.661506+00:00" +instance: "kb-cron" +--- + +This list contains a list of EC numbers for the fourth group, EC 4, lyases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. + +== EC 4.1: Carbon-Carbon Lyases == + +=== EC 4.1.1: Carboxy-lyases === +EC 4.1.1.1: pyruvate decarboxylase +EC 4.1.1.2: oxalate decarboxylase +EC 4.1.1.3: Now recognized to be two enzymes EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)] and EC 4.1.1.112 (oxaloacetate decarboxylase). +EC 4.1.1.4: acetoacetate decarboxylase +EC 4.1.1.5: acetolactate decarboxylase +EC 4.1.1.6: cis-aconitate decarboxylase +EC 4.1.1.7: benzoylformate decarboxylase +EC 4.1.1.8: oxalyl-CoA decarboxylase +EC 4.1.1.9: malonyl-CoA decarboxylase +EC 4.1.1.10: Now included with EC 4.1.1.12, aspartate 4-decarboxylase +EC 4.1.1.11: aspartate 1-decarboxylase +EC 4.1.1.12: aspartate 4-decarboxylase +EC 4.1.1.13: deleted +EC 4.1.1.14: valine decarboxylase +EC 4.1.1.15: glutamate decarboxylase +EC 4.1.1.16: hydroxyglutamate decarboxylase +EC 4.1.1.17: ornithine decarboxylase +EC 4.1.1.18: lysine decarboxylase +EC 4.1.1.19: arginine decarboxylase +EC 4.1.1.20: diaminopimelate decarboxylase +EC 4.1.1.21: phosphoribosylaminoimidazole carboxylase +EC 4.1.1.22: histidine decarboxylase +EC 4.1.1.23: orotidine-5′-phosphate decarboxylase +EC 4.1.1.24: aminobenzoate decarboxylase +EC 4.1.1.25: tyrosine decarboxylase +EC 4.1.1.26: Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase +EC 4.1.1.27: Now included with EC 4.1.1.28 aromatic-L-amino-acid decarboxylase +EC 4.1.1.28: aromatic-L-amino-acid decarboxylase +EC 4.1.1.29: sulfoalanine decarboxylase +EC 4.1.1.30: pantothenoylcysteine decarboxylase +EC 4.1.1.31: phosphoenolpyruvate carboxylase +EC 4.1.1.32: phosphoenolpyruvate carboxykinase (GTP) +EC 4.1.1.33: diphosphomevalonate decarboxylase +EC 4.1.1.34: dehydro-L-gulonate decarboxylase +EC 4.1.1.35: UDP-glucuronate decarboxylase +EC 4.1.1.36: phosphopantothenoylcysteine decarboxylase +EC 4.1.1.37: uroporphyrinogen decarboxylase +EC 4.1.1.38: phosphoenolpyruvate carboxykinase (diphosphate) +EC 4.1.1.39: ribulose-bisphosphate carboxylase +EC 4.1.1.40: hydroxypyruvate decarboxylase +EC 4.1.1.41: Now EC 7.2.4.3, (S)-methylmalonyl-CoA decarboxylase +EC 4.1.1.42: carnitine decarboxylase +EC 4.1.1.43: phenylpyruvate decarboxylase +EC 4.1.1.44: 4-carboxymuconolactone decarboxylase +EC 4.1.1.45: aminocarboxymuconate-semialdehyde decarboxylase +EC 4.1.1.46: o-pyrocatechuate decarboxylase +EC 4.1.1.47: tartronate-semialdehyde synthase +EC 4.1.1.48: indole-3-glycerol-phosphate synthase +EC 4.1.1.49: phosphoenolpyruvate carboxykinase (ATP) +EC 4.1.1.50: adenosylmethionine decarboxylase +EC 4.1.1.51: 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase +EC 4.1.1.52: 6-methylsalicylate decarboxylase +EC 4.1.1.53: phenylalanine decarboxylase +EC 4.1.1.54: dihydroxyfumarate decarboxylase +EC 4.1.1.55: 4,5-dihydroxyphthalate decarboxylase +EC 4.1.1.56: 3-oxolaurate decarboxylase +EC 4.1.1.57: methionine decarboxylase +EC 4.1.1.58: orsellinate decarboxylase +EC 4.1.1.59: gallate decarboxylase +EC 4.1.1.60: stipitatonate decarboxylase +EC 4.1.1.61: 4-hydroxybenzoate decarboxylase +EC 4.1.1.62: gentisate decarboxylase +EC 4.1.1.63: protocatechuate decarboxylase +EC 4.1.1.64: 2,2-dialkylglycine decarboxylase (pyruvate) +EC 4.1.1.65: phosphatidylserine decarboxylase +EC 4.1.1.66: uracil-5-carboxylate decarboxylase +EC 4.1.1.67: UDP-galacturonate decarboxylase +EC 4.1.1.68: 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase +EC 4.1.1.69: 3,4-dihydroxyphthalate decarboxylase +EC 4.1.1.70: Now EC 7.2.4.5, glutaconyl-CoA decarboxylase +EC 4.1.1.71: 2-oxoglutarate decarboxylase +EC 4.1.1.72: branched-chain-2-oxoacid decarboxylase +EC 4.1.1.73: tartrate decarboxylase +EC 4.1.1.74: indolepyruvate decarboxylase +EC 4.1.1.75: 5-guanidino-2-oxopentanoate decarboxylase +EC 4.1.1.76: arylmalonate decarboxylase +EC 4.1.1.77: 4-oxalocrotonate decarboxylase +EC 4.1.1.78: acetylenedicarboxylate decarboxylase +EC 4.1.1.79: sulfopyruvate decarboxylase +EC 4.1.1.80: 4-hydroxyphenylpyruvate decarboxylase +EC 4.1.1.81: threonine-phosphate decarboxylase +EC 4.1.1.82: phosphonopyruvate decarboxylase +EC 4.1.1.83: 4-hydroxyphenylacetate decarboxylase +EC 4.1.1.84: D-dopachrome decarboxylase +EC 4.1.1.85: 3-dehydro-L-gulonate-6-phosphate decarboxylase +EC 4.1.1.86: diaminobutyrate decarboxylase +EC 4.1.1.87: malonyl-S-ACP decarboxylase +EC 4.1.1.88: biotin-independent malonate decarboxylase +EC 4.1.1.89: Now EC 7.2.4.4 EC 7.2.4.4, biotin-dependent malonate decarboxylase +EC 4.1.1.90: peptidyl-glutamate 4-carboxylase +EC 4.1.1.91: salicylate decarboxylase +EC 4.1.1.92: indole-3-carboxylate decarboxylase +EC 4.1.1.93: pyrrole-2-carboxylate decarboxylase +EC 4.1.1.94: ethylmalonyl-CoA decarboxylase +EC 4.1.1.95: L-glutamyl-[BtrI acyl-carrier protein] decarboxylase +EC 4.1.1.96: carboxynorspermidine decarboxylase +EC 4.1.1.97: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase +EC 4.1.1.98: 4-hydroxy-3-polyprenylbenzoate decarboxylase +EC 4.1.1.99: phosphomevalonate decarboxylase +EC 4.1.1.100: prephenate decarboxylase +EC 4.1.1.101: malolactic enzyme +EC 4.1.1.102: phenacrylate decarboxylase +EC 4.1.1.103: γ-resorcylate decarboxylase +EC 4.1.1.104: 3-dehydro-4-phosphotetronate decarboxylase +EC 4.1.1.105: L-tryptophan decarboxylase +EC 4.1.1.106: fatty acid photodecarboxylase +EC 4.1.1.107: 3,4-dihydroxyphenylacetaldehyde synthase +EC 4.1.1.108: 4-hydroxyphenylacetaldehyde synthase +EC 4.1.1.109: phenylacetaldehyde synthase +EC 4.1.1.110: bisphosphomevalonate decarboxylase +EC 4.1.1.111: siroheme decarboxylase +EC 4.1.1.112: oxaloacetate decarboxylase +EC 4.1.1.113: trans-aconitate decarboxylase +EC 4.1.1.114: cis-3-alkyl-4-alkyloxetan-2-one decarboxylase +EC 4.1.1.115: indoleacetate decarboxylase +EC 4.1.1.116: D-ornithine/D-lysine decarboxylase +EC 4.1.1.117: [[2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate decarboxylase|2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate decarboxylase]] +EC 4.1.1.118: isophthalyl-CoA decarboxylase +EC 4.1.1.119: phenylacetate decarboxylase +EC 4.1.1.120: 3-oxoisoapionate decarboxylase +EC 4.1.1.121: 3-oxoisoapionate-4-phosphate decarboxylase + +=== EC 4.1.2: Aldehyde-lyases === +EC 4.1.2.1: Now included with EC 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase +EC 4.1.2.2: ketotetrose-phosphate aldolase +EC 4.1.2.3: deleted, was pentosealdolase. +EC 4.1.2.4: deoxyribose-phosphate aldolase +EC 4.1.2.5: L-threonine aldolase +EC 4.1.2.6: Deleted, reaction is due to EC 2.1.2.1, glycine hydroxymethyltransferase +EC 4.1.2.7: Now included with EC 4.1.2.13 fructose-bisphosphate aldolase +EC 4.1.2.8: indole-3-glycerol-phosphate lyase +EC 4.1.2.9: phosphoketolase +EC 4.1.2.10: (R)-mandelonitrile lyase +EC 4.1.2.11: hydroxymandelonitrile lyase +EC 4.1.2.12: 2-dehydropantoate aldolase +EC 4.1.2.13: fructose-bisphosphate aldolase +EC 4.1.2.14: 2-dehydro-3-deoxy-phosphogluconate aldolase +EC 4.1.2.15: Now EC 2.5.1.54, 3-deoxy-7-phosphoheptulonate synthase +EC 4.1.2.16: Now EC 2.5.1.55, 3-deoxy-8-phosphooctulonate synthase +EC 4.1.2.17: L-fuculose-phosphate aldolase +EC 4.1.2.18: 2-dehydro-3-deoxy-L-pentonate aldolase +EC 4.1.2.19: rhamnulose-1-phosphate aldolase +EC 4.1.2.20: 2-dehydro-3-deoxyglucarate aldolase +EC 4.1.2.21: 2-dehydro-3-deoxy-6-phosphogalactonate aldolase +EC 4.1.2.22: fructose-6-phosphate phosphoketolase +EC 4.1.2.23: 3-deoxy-D-manno-octulosonate aldolase +EC 4.1.2.24: dimethylaniline-N-oxide aldolase +EC 4.1.2.25: dihydroneopterin aldolase +EC 4.1.2.26: phenylserine aldolase +EC 4.1.2.27: sphinganine-1-phosphate aldolase +EC 4.1.2.28: 2-dehydro-3-deoxy-D-pentonate aldolase +EC 4.1.2.29: 5-dehydro-2-deoxyphosphogluconate aldolase +EC 4.1.2.30: Now EC 1.14.14.32}, 17α-hydroxyprogesterone deacetylase +EC 4.1.2.31: Now included with EC 4.1.3.16 4-hydroxy-2-oxoglutarate aldolase +EC 4.1.2.32: trimethylamine-oxide aldolase +EC 4.1.2.33: fucosterol-epoxide lyase +EC 4.1.2.34: 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase +EC 4.1.2.35: propioin synthase +EC 4.1.2.36: lactate aldolase +EC 4.1.2.37: Now covered by EC 4.1.2.46 [aliphatic (R)-hydroxynitrile lyase] and EC 4.1.2.47 [(S)-hydroxynitrile ketone-lyase (cyanide forming)] +EC 4.1.2.38: benzoin aldolase +EC 4.1.2.39: Deleted, identical to EC 4.1.2.37, hydroxynitrilase +EC 4.1.2.40: tagatose-bisphosphate aldolase +EC 4.1.2.41: Now included with EC 4.1.2.61, feruloyl-CoA hydratase/lyase +EC 4.1.2.42: D-threonine aldolase +EC 4.1.2.43: 3-hexulose-6-phosphate synthase +EC 4.1.2.44: benzoyl-CoA-dihydrodiol lyase +EC 4.1.2.45: trans-o-hydroxybenzylidenepyruvate hydratase-aldolase +EC 4.1.2.46: aliphatic (R)-hydroxynitrile lyase +EC 4.1.2.47: (S)-hydroxynitrile lyase +EC 4.1.2.48: low-specificity L-threonine aldolase +EC 4.1.2.49: L-allo-threonine aldolase +EC 4.1.2.50: 6-carboxytetrahydropterin synthase +* EC 4.1.2.50: 6-carboxytetrahydropterin synthase +* EC 4.1.2.51: 2-dehydro-3-deoxy-D-gluconate aldolase +* EC 4.1.2.52: 4-hydroxy-2-oxoheptanedioate aldolase +* EC 4.1.2.53: 2-keto-3-deoxy-L-rhamnonate aldolase +* EC 4.1.2.54: L-threo-3-deoxy-hexylosonate aldolase +* EC 4.1.2.55: 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase +* EC 4.1.2.56: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate synthase +* EC 4.1.2.57: sulfofructosephosphate aldolase +* EC 4.1.2.58: 2-dehydro-3,6-dideoxy-6-sulfogluconate aldolase +* EC 4.1.2.59: dihydroneopterin phosphate aldolase +* EC 4.1.2.60: dihydroneopterin triphosphate aldolase +* EC 4.1.2.61: feruloyl-CoA hydratase/lyase +* EC 4.1.2.62: 5-deoxyribulose 1-phosphate aldolase +* EC 4.1.2.63: 2-hydroxyacyl-CoA lyase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-1.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-1.md new file mode 100644 index 000000000..af183020a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-1.md @@ -0,0 +1,87 @@ +--- +title: "List of EC numbers (EC 4)" +chunk: 2/5 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:09.661506+00:00" +instance: "kb-cron" +--- + +=== EC 4.1.3: Oxo-Acid-Lyases === +EC 4.1.3.1: isocitrate lyase +EC 4.1.3.2: Now EC 2.3.3.9, malate synthase +EC 4.1.3.3: N-acetylneuraminate lyase +EC 4.1.3.4: hydroxymethylglutaryl-CoA lyase +EC 4.1.3.5: Now EC 2.3.3.10, hydroxymethylglutaryl-CoA synthase +EC 4.1.3.6: citrate (pro-3S)-lyase +EC 4.1.3.7: Now EC 2.3.3.1, citrate (Si)-synthase +EC 4.1.3.8: Now EC 2.3.3.8, ATP citrate synthase +EC 4.1.3.9: Now EC 2.3.3.11, 2-hydroxyglutarate synthase +EC 4.1.3.10: Now EC 2.3.3.7, 3-ethylmalate synthase +EC 4.1.3.11: Now EC 2.3.3.12, 3-propylmalate synthase +EC 4.1.3.12: Now EC 2.3.3.13, 2-isopropylmalate synthase +EC 4.1.3.13: oxalomalate lyase +EC 4.1.3.14: L-erythro-3-hydroxyaspartate aldolase +EC 4.1.3.15: Now EC 2.2.1.5, 2-hydroxy-3-oxoadipate synthase +EC 4.1.3.16: 4-hydroxy-2-oxoglutarate aldolase +EC 4.1.3.17: 4-hydroxy-4-methyl-2-oxoglutarate aldolase +EC 4.1.3.18: Now EC 2.2.1.6, acetolactate synthase +EC 4.1.3.19: Now EC 2.5.1.56 +EC 4.1.3.20: Now EC 2.5.1.57 +EC 4.1.3.21: Now EC 2.3.3.14 +EC 4.1.3.22: citramalate lyase +EC 4.1.3.23: Now EC 2.3.3.2, decylcitrate synthase +EC 4.1.3.24: malyl-CoA lyase +EC 4.1.3.25: (S)-citramalyl-CoA lyase +EC 4.1.3.26: 3-hydroxy-3-isohexenylglutaryl-CoA lyase +EC 4.1.3.27: anthranilate synthase +EC 4.1.3.28: Now EC 2.3.3.3, citrate (Re)-synthase +EC 4.1.3.29: Now EC 2.3.3.4, decylhomocitrate synthase +EC 4.1.3.30: methylisocitrate lyase +EC 4.1.3.31: Now EC 2.3.3.5, 2-methylcitrate synthase +EC 4.1.3.32: 2,3-dimethylmalate lyase +EC 4.1.3.33: Now EC 2.3.3.6 +EC 4.1.3.34: citryl-CoA lyase +EC 4.1.3.35: (1-hydroxycyclohexan-1-yl)acetyl-CoA lyase +EC 4.1.3.36: naphthoate synthase +EC 4.1.3.37: Now EC 2.2.1.7, 1-deoxy-D-xylulose 5-phosphate synthase +EC 4.1.3.38: aminodeoxychorismate lyase +EC 4.1.3.39: 4-hydroxy-2-oxovalerate aldolase +EC 4.1.3.40: chorismate lyase +EC 4.1.3.41: 3-hydroxy-D-aspartate aldolase +EC 4.1.3.42: (4S)-4-hydroxy-2-oxoglutarate aldolase +EC 4.1.3.43: 4-hydroxy-2-oxohexanoate aldolase +EC 4.1.3.44: tRNA 4-demethylwyosine synthase (AdoMet-dependent) +EC 4.1.3.45: 3-hydroxybenzoate synthase +EC 4.1.3.46: (R)-citramalyl-CoA lyase + +=== EC 4.1.99: Other Carbon-Carbon Lyases === +EC 4.1.99.1: tryptophanase +EC 4.1.99.2: tyrosine phenol-lyase +EC 4.1.99.3: deoxyribodipyrimidine photo-lyase +EC 4.1.99.4: Now EC 3.5.99.7, 1-aminocyclopropane-1-carboxylate deaminase +EC 4.1.99.5: octadecanal decarbonylase +EC 4.1.99.6: Now EC 4.2.3.6, trichodiene synthase +EC 4.1.99.7: Now EC 4.2.3.9, aristolochene synthase +EC 4.1.99.8: Now EC 4.2.3.14, pinene synthase +EC 4.1.99.9: Now EC 4.2.3.15, myrcene synthase +EC 4.1.99.10: Now EC 4.2.3.16, (4S)-limonene synthase +EC 4.1.99.11: benzylsuccinate synthase +EC 4.1.99.12: 3,4-dihydroxy-2-butanone-4-phosphate synthase +EC 4.1.99.13: (6-4)DNA photolyase +EC 4.1.99.14: spore photoproduct lyase +EC 4.1.99.15: The activity is covered by EC 4.1.99.14, spore photoproduct lyase +EC 4.1.99.16: geosmin synthase +EC 4.1.99.17: phosphomethylpyrimidine synthase +EC 4.1.99.18: Now known to be catalysed by the combined effect of EC 4.1.99.22, GTP 3,8-cyclase, and EC 4.6.1.17, cyclic pyranopterin monophosphate synthase +EC 4.1.99.19: 2-iminoacetate synthase +EC 4.1.99.20: 3-amino-4-hydroxybenzoate synthase +EC 4.1.99.21: Now EC 4.2.3.153 (5-formylfuran-3-yl)methyl phosphate synthase. +EC 4.1.99.22: GTP 3′,8-cyclase +EC 4.1.99.23: 5-hydroxybenzimidazole synthase +EC 4.1.99.24: L-tyrosine isonitrile synthase +EC 4.1.99.25: L-tryptophan isonitrile synthase +EC 4.1.99.26: [[3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one|3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one]] + +== EC 4.2: Carbon-Oxygen Lyases == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-2.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-2.md new file mode 100644 index 000000000..3b6858694 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-2.md @@ -0,0 +1,188 @@ +--- +title: "List of EC numbers (EC 4)" +chunk: 3/5 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:09.661506+00:00" +instance: "kb-cron" +--- + +=== EC 4.2.1: Hydro-lyases === +EC 4.2.1.1: carbonic anhydrase +EC 4.2.1.2: fumarate hydratase +EC 4.2.1.3: aconitate hydratase +EC 4.2.1.4: Now known to be a partial reaction catalysed by EC 4.2.1.3, aconitate hydratase +EC 4.2.1.5: arabinonate dehydratase +EC 4.2.1.6: galactonate dehydratase +EC 4.2.1.7: altronate dehydratase +EC 4.2.1.8: mannonate dehydratase +EC 4.2.1.9: dihydroxy-acid dehydratase +EC 4.2.1.10: 3-dehydroquinate dehydratase +EC 4.2.1.11: phosphopyruvate hydratase (enolase) +EC 4.2.1.12: phosphogluconate dehydratase +EC 4.2.1.13: Now EC 4.3.1.17, L-serine ammonia-lyase +EC 4.2.1.14: Now EC 4.3.1.18, D-serine ammonia-lyase +EC 4.2.1.15: Identical with EC 4.4.1.1 cystathionine γ-lyase +EC 4.2.1.16: Now EC 4.3.1.19, threonine ammonia-lyase +EC 4.2.1.17: enoyl-CoA hydratase +EC 4.2.1.18: methylglutaconyl-CoA hydratase +EC 4.2.1.19: imidazoleglycerol-phosphate dehydratase +EC 4.2.1.20: tryptophan synthase +EC 4.2.1.21: Now EC 4.2.1.22 cystathionine β-synthase +EC 4.2.1.22: cystathionine β-synthase +EC 4.2.1.23: deleted, the reaction was due to a side-reaction of EC 4.2.1.22 cystathionine β-synthase +EC 4.2.1.24: porphobilinogen synthase +EC 4.2.1.25: L-arabinonate dehydratase +EC 4.2.1.26: identical to EC 4.3.1.9, glucosaminate ammonia-lyase +EC 4.2.1.27: acetylenecarboxylate hydratase +EC 4.2.1.28: propanediol dehydratase +EC 4.2.1.29: Now EC 4.99.1.6, indoleacetaldoxime dehydratase +EC 4.2.1.30: glycerol dehydratase +EC 4.2.1.31: maleate hydratase +EC 4.2.1.32: L(+)-tartrate dehydratase +EC 4.2.1.33: 3-isopropylmalate dehydratase +EC 4.2.1.34: (S)-2-methylmalate dehydratase +EC 4.2.1.35: (R)-2-methylmalate dehydratase +EC 4.2.1.36: homoaconitate hydratase +EC 4.2.1.37: Now EC 3.3.2.4, trans-epoxysuccinate hydrolase +EC 4.2.1.38: Now EC 4.3.1.20, erythro-3-hydroxyaspartate ammonia-lyase +EC 4.2.1.39: gluconate dehydratase +EC 4.2.1.40: glucarate dehydratase +EC 4.2.1.41: 5-dehydro-4-deoxyglucarate dehydratase +EC 4.2.1.42: galactarate dehydratase +EC 4.2.1.43: 2-dehydro-3-deoxy-L-arabinonate dehydratase +EC 4.2.1.44: myo-inosose-2 dehydratase +EC 4.2.1.45: CDP-glucose 4,6-dehydratase +EC 4.2.1.46: dTDP-glucose 4,6-dehydratase +EC 4.2.1.47: GDP-mannose 4,6-dehydratase +EC 4.2.1.48: D-glutamate cyclase +EC 4.2.1.49: urocanate hydratase +EC 4.2.1.50: pyrazolylalanine synthase +EC 4.2.1.51: prephenate dehydratase +EC 4.2.1.52: Now EC 4.3.3.7, 4-hydroxy-2,3,4,5-tetrahydrodipicolinate synthase. +EC 4.2.1.53: oleate hydratase +EC 4.2.1.54: lactoyl-CoA dehydratase +EC 4.2.1.55: 3-hydroxybutyryl-CoA dehydratase +EC 4.2.1.56: itaconyl-CoA hydratase +EC 4.2.1.57: isohexenylglutaconyl-CoA hydratase +EC 4.2.1.58: The reaction described is covered by EC 4.2.1.59 +EC 4.2.1.59: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase +EC 4.2.1.60: 3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase +EC 4.2.1.61: The reaction described is covered by EC 4.2.1.59. +EC 4.2.1.62: 5α-hydroxysteroid dehydratase +EC 4.2.1.63: Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10) +EC 4.2.1.64: Now known to comprise two enzymes, microsomal epoxide hydrolase (EC 3.3.2.9) and soluble epoxide hydrolase (EC 3.3.2.10) +EC 4.2.1.65: 3-cyanoalanine hydratase +EC 4.2.1.66: cyanide hydratase +EC 4.2.1.67: D-fuconate dehydratase +EC 4.2.1.68: L-fuconate dehydratase +EC 4.2.1.69: cyanamide hydratase +EC 4.2.1.70: pseudouridylate synthase +EC 4.2.1.71: identical to EC 4.2.1.27, acetylenecarboxylate hydratase +EC 4.2.1.72: Now EC 4.1.1.78, acetylenedicarboxylate decarboxylase +EC 4.2.1.73: protoaphin-aglucone dehydratase (cyclizing) +EC 4.2.1.74: long-chain-enoyl-CoA hydratase +EC 4.2.1.75: uroporphyrinogen-III synthase +EC 4.2.1.76: UDP-glucose 4,6-dehydratase +EC 4.2.1.77: trans-L-3-hydroxyproline dehydratase +EC 4.2.1.78: Now EC 3.5.99.14, (S)-norcoclaurine synthase +EC 4.2.1.79: 2-methylcitrate dehydratase +EC 4.2.1.80: 2-oxopent-4-enoate hydratase +EC 4.2.1.81: D(-)-tartrate dehydratase +EC 4.2.1.82: xylonate dehydratase +EC 4.2.1.83: 4-oxalmesaconate hydratase +EC 4.2.1.84: nitrile hydratase +EC 4.2.1.85: dimethylmaleate hydratase +EC 4.2.1.86: identical to EC 4.2.1.98, 16α-hydroxyprogesterone dehydratase +EC 4.2.1.87: octopamine dehydratase +EC 4.2.1.88: synephrine dehydratase +EC 4.2.1.89: The activity has now been shown to be due to EC 2.8.3.21, L-carnitine CoA-transferase and EC 4.2.1.149, crotonobetainyl-CoA hydratase +EC 4.2.1.90: L-rhamnonate dehydratase +EC 4.2.1.91: arogenate dehydratase +EC 4.2.1.92: hydroperoxide dehydratase +EC 4.2.1.93: ATP-dependent NAD(P)H-hydrate dehydratase +EC 4.2.1.94: scytalone dehydratase +EC 4.2.1.95: kievitone hydratase +EC 4.2.1.96: 4a-hydroxytetrahydrobiopterin dehydratase +EC 4.2.1.97: phaseollidin hydratase +EC 4.2.1.98: 16α-hydroxyprogesterone dehydratase +EC 4.2.1.99: 2-methylisocitrate dehydratase +EC 4.2.1.100: cyclohexa-1,5-dienecarbonyl-CoA hydratase +EC 4.2.1.101: Now included with EC 4.1.2.61, feruloyl-CoA hydratase/lyase +EC 4.2.1.102: Now EC 4.2.1.100, cyclohexa-1,5-dienecarbonyl-CoA hydratase +EC 4.2.1.103: cyclohexyl-isocyanide hydratase +EC 4.2.1.104: cyanase +EC 4.2.1.105: 2-hydroxyisoflavanone dehydratase +EC 4.2.1.106: bile-acid 7α-dehydratase +EC 4.2.1.107: 3α,7α,12α-trihydroxy-5β-cholest-24-enoyl-CoA hydratase +EC 4.2.1.108: ectoine synthase +EC 4.2.1.109: methylthioribulose 1-phosphate dehydratase +EC 4.2.1.110: aldos-2-ulose dehydratase +EC 4.2.1.111: 1,5-anhydro-D-fructose dehydratase +EC 4.2.1.112: acetylene hydratase +EC 4.2.1.113: o-succinylbenzoate synthase +EC 4.2.1.114: methanogen homoaconitase +EC 4.2.1.115: UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting) +EC 4.2.1.116: 3-hydroxypropionyl-CoA dehydratase +EC 4.2.1.117: 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) +EC 4.2.1.118: 3-dehydroshikimate dehydratase +EC 4.2.1.119: enoyl-CoA hydratase 2 +EC 4.2.1.120: 4-hydroxybutanoyl-CoA dehydratase +EC 4.2.1.121: colneleate synthase +EC 4.2.1.122: tryptophan synthase (indole-salvaging) +EC 4.2.1.123: tetrahymanol synthase +EC 4.2.1.124: arabidiol synthase +EC 4.2.1.125: dammarenediol II synthase +EC 4.2.1.126: N-acetylmuramic acid 6-phosphate etherase +EC 4.2.1.127: linalool dehydratase +EC 4.2.1.128: lupan-3β,20-diol synthase +EC 4.2.1.129: squalene—hopanol cyclase +EC 4.2.1.130: D-lactate dehydratase +EC 4.2.1.131: carotenoid 1,2-hydratase +EC 4.2.1.132: 2-hydroxyhexa-2,4-dienoate hydratase +EC 4.2.1.133: copal-8-ol diphosphate hydratase +EC 4.2.1.134: very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase +EC 4.2.1.135: UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining) +EC 4.2.1.136: ADP-dependent NAD(P)H-hydrate dehydratase +EC 4.2.1.137: sporulenol synthase +EC 4.2.1.138: (+)-Caryolan-1-ol synthase +EC 4.2.1.139: pterocarpan synthase +EC 4.2.1.140: gluconate/galactonate dehydratase +EC 4.2.1.141: 2-dehydro-3-deoxyD-arabinonate dehydratase +EC 4.2.1.142: 5′-oxoaverantin cyclase +EC 4.2.1.143: versicolorin B synthase +EC 4.2.1.144: 3-amino-5-hydroxybenzoate synthase +EC 4.2.1.145: capreomycidine synthase +EC 4.2.1.146: L-galactonate dehydratase +EC 4.2.1.147: 5,6,7,8-tetrahydromethanopterin hydro-lyase +EC 4.2.1.148: 2-methylfumaryl-CoA hydratase +EC 4.2.1.149: crotonobetainyl-CoA hydratase +EC 4.2.1.150: short-chain-enoyl-CoA hydratase +EC 4.2.1.151: chorismate dehydratase +EC 4.2.1.152: hydroperoxy icosatetraenoate dehydratase +EC 4.2.1.153: 3-methylfumaryl-CoA hydratase +EC 4.2.1.154: tetracenomycin F2 cyclase +EC 4.2.1.155: (methylthio)acryloyl-CoA hydratase +EC 4.2.1.156: L-talarate dehydratase +EC 4.2.1.157: (R)-2-hydroxyisocaproyl-CoA dehydratase +EC 4.2.1.158: galactarate dehydratase (D-threo-forming) +EC 4.2.1.159: dTDP-4-dehydro-6-deoxy-α-glucopyranose 2,3-dehydratase +EC 4.2.1.160: 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one isomerase/dehydratase +EC 4.2.1.161: bisanhydrobacterioruberin hydratase +EC 4.2.1.162: 6-deoxy-6-sulfo-D-gluconate dehydratase +EC 4.2.1.163: 2-oxo-hept-4-ene-1,7-dioate hydratase +EC 4.2.1.164: dTDP-4-dehydro-2,6-dideoxy-D-glucose 3-dehydratase +EC 4.2.1.165: chlorophyllide a 31-hydratase +EC 4.2.1.166: phosphinomethylmalate isomerase +EC 4.2.1.167: (R)-2-hydroxyglutaryl-CoA dehydratase +EC 4.2.1.168: GDP-4-dehydro-6-deoxy-α-D-mannose 3-dehydratase +EC 4.2.1.169: 3-vinyl bacteriochlorophyllide d 31-hydratase +EC 4.2.1.170: 2-(ω-methylthio)alkylmalate dehydratase +EC 4.2.1.171: cis-L-3-hydroxyproline dehydratase +EC 4.2.1.172: trans-4-hydroxy-L-proline dehydratase +EC 4.2.1.173: ent-8α-hydroxylabd-13-en-15-yl diphosphate synthase +EC 4.2.1.174: peregrinol diphosphate synthase +EC 4.2.1.175: (R)-3-(aryl)lactoyl-CoA dehydratase +EC 4.2.1.176: L-lyxonate dehydratase +EC 4.2.1.177: (2S)-3-sulfopropanediol dehydratase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-3.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-3.md new file mode 100644 index 000000000..c806b9377 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-3.md @@ -0,0 +1,245 @@ +--- +title: "List of EC numbers (EC 4)" +chunk: 4/5 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:09.661506+00:00" +instance: "kb-cron" +--- + +=== EC 4.2.2: Acting on Polysaccharides === +EC 4.2.2.1: hyaluronate lyase +EC 4.2.2.2: pectate lyase +EC 4.2.2.3: mannuronate-specific alginate lyase +EC 4.2.2.4: Now known to comprise two enzymes: EC 4.2.2.20, chondroitin-sulfate-ABC endolyase and EC 4.2.2.21, chondroitin-sulfate-ABC exolyase +EC 4.2.2.5: chondroitin AC lyase +EC 4.2.2.6: oligogalacturonide lyase +EC 4.2.2.7: heparin lyase +EC 4.2.2.8: heparin-sulfate lyase +EC 4.2.2.9: pectate disaccharide-lyase +EC 4.2.2.10: pectin lyase +EC 4.2.2.11: guluronate-specific alginate lyase +EC 4.2.2.12: xanthan lyase +EC 4.2.2.13: exo-(1→4)-α-D-glucan lyase +EC 4.2.2.14: glucuronan lyase +EC 4.2.2.15: anhydrosialidase +EC 4.2.2.16: levan fructotransferase (DFA-IV-forming) +EC 4.2.2.17: inulin fructotransferase (DFA-I-forming) +EC 4.2.2.18: inulin fructotransferase (DFA-III-forming) +EC 4.2.2.19: chondroitin B lyase +EC 4.2.2.20: chondroitin-sulfate-ABC endolyase +EC 4.2.2.21: chondroitin-sulfate-ABC exolyase +EC 4.2.2.22: pectate trisaccharide-lyase +EC 4.2.2.23: rhamnogalacturonan endolyase +EC 4.2.2.24: rhamnogalacturonan exolyase +EC 4.2.2.25: gellan lyase +EC 4.2.2.26: oligo-alginate lyase +EC 4.2.2.27: pectin monosaccharide-lyase + +=== EC 4.2.3: Acting on phosphates === +EC 4.2.3.1: threonine synthase +EC 4.2.3.2: ethanolamine-phosphate phospho-lyase +EC 4.2.3.3: methylglyoxal synthase +EC 4.2.3.4: 3-dehydroquinate synthase +EC 4.2.3.5: chorismate synthase +EC 4.2.3.6: trichodiene synthase +EC 4.2.3.7: pentalenene synthase +EC 4.2.3.8: casbene synthase +EC 4.2.3.9: aristolochene synthase +EC 4.2.3.10: (–)-endo-fenchol synthase +EC 4.2.3.11: sabinene-hydrate synthase +EC 4.2.3.12: 6-pyruvoyltetrahydropterin synthase +EC 4.2.3.13: (+)-δ-cadinene synthase +EC 4.2.3.14: Now covered by EC 4.2.3.119, (–)-α-pinene synthase, and EC 4.2.3.120, (–)-β-pinene synthase +EC 4.2.3.15: myrcene synthase +EC 4.2.3.16: (4S)-limonene synthase +EC 4.2.3.17: taxadiene synthase +EC 4.2.3.18: abietadiene synthase +EC 4.2.3.19: ent-kaurene synthase +EC 4.2.3.20: (R)-limonene synthase +EC 4.2.3.21: vetispiradiene synthase +EC 4.2.3.22: germacradienol synthase +EC 4.2.3.23: germacrene-A synthase +EC 4.2.3.24: amorpha-4,11-diene synthase +EC 4.2.3.25: S-linalool synthase +EC 4.2.3.26: R-linalool synthase +EC 4.2.3.27: isoprene synthase +EC 4.2.3.28: ent-cassa-12,15-diene synthase +EC 4.2.3.29: ent-sandaracopimaradiene synthase +EC 4.2.3.30: ent-pimara-8(14),15-diene synthase +EC 4.2.3.31: ent-pimara-9(11),15-diene synthase +EC 4.2.3.32: levopimaradiene synthase +EC 4.2.3.33: stemar-13-ene synthase +EC 4.2.3.34: stemod-13(17)-ene synthase +EC 4.2.3.35: syn-pimara-7,15-diene synthase +EC 4.2.3.36: terpentetriene synthase +EC 4.2.3.37: epi-isozizaene synthase +EC 4.2.3.38: α-bisabolene synthase +EC 4.2.3.39: epi-cedrol synthase +EC 4.2.3.40: (Z)-γ-bisabolene synthase +EC 4.2.3.41: elisabethatriene synthase +EC 4.2.3.42: aphidicolan-16β-ol synthase +EC 4.2.3.43: fusicocca-2,10(14)-diene synthase +EC 4.2.3.44: isopimara-7,15-diene synthase +EC 4.2.3.45: phyllocladan-16α-ol synthase +EC 4.2.3.46: α-farnesene synthase +EC 4.2.3.47: β-farnesene synthase +EC 4.2.3.48: (3S,6E)-nerolidol synthase +EC 4.2.3.49: (3R,6E)-nerolidol synthase +EC 4.2.3.50: (+)-α-santalene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] +EC 4.2.3.51: β-phellandrene synthase (neryl-diphosphate-cyclizing) +EC 4.2.3.52: (4S)-β-phellandrene synthase (geranyl-diphosphate-cyclizing) +EC 4.2.3.53: (+)-endo-β-bergamotene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] +EC 4.2.3.54: (–)-endo-α-bergamotene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] +EC 4.2.3.55: (S)-β-bisabolene synthase +EC 4.2.3.56: γ-humulene synthase +EC 4.2.3.57: (–)-β-caryophyllene synthase +EC 4.2.3.58: longifolene synthase +EC 4.2.3.59: (E)-γ-bisabolene synthase +EC 4.2.3.60: germacrene C synthase +EC 4.2.3.61: 5-epiaristolochene synthase +EC 4.2.3.62: (–)-γ-cadinene synthase [(2Z,6E)-farnesyl diphosphate cyclizing] +EC 4.2.3.63: (+)-cubenene synthase +EC 4.2.3.64: (+)-epicubenol synthase +EC 4.2.3.65: zingiberene synthase +EC 4.2.3.66: β-selinene cyclase +EC 4.2.3.67: cis-muuroladiene synthase +EC 4.2.3.68: β-eudesmol synthase +EC 4.2.3.69: (+)-α-barbatene synthase +EC 4.2.3.70: patchoulol synthase +EC 4.2.3.71: (E,E)-germacrene B synthase +EC 4.2.3.72: α-gurjunene synthase +EC 4.2.3.73: valencene synthase +EC 4.2.3.74: presilphiperfolanol synthase +EC 4.2.3.75: (–)-germacrene D synthase +EC 4.2.3.76: (+)-δ-selinene synthase +EC 4.2.3.77: (+)-germacrene D synthase +EC 4.2.3.78: β-chamigrene synthase +EC 4.2.3.79: thujopsene synthase +EC 4.2.3.80: α-longipinene synthase +EC 4.2.3.81: exo-α-bergamotene synthase +EC 4.2.3.82: α-santalene synthase +EC 4.2.3.83: β-santalene synthase +EC 4.2.3.84: 10-epi-γ-eudesmol synthase +EC 4.2.3.85: α-eudesmol synthase +EC 4.2.3.86: 7-epi-α-selinene synthase +EC 4.2.3.87: α-guaiene synthase +EC 4.2.3.88: viridiflorene synthase +EC 4.2.3.89: (+)-β-caryophyllene synthase +EC 4.2.3.90: 5-epi-α-selinene synthase +EC 4.2.3.91: cubebol synthase +EC 4.2.3.92: (+)-γ-cadinene synthase +EC 4.2.3.93: δ-guaiene synthase +EC 4.2.3.94: γ-curcumene synthase +EC 4.2.3.95: (–)-α-cuprenene synthase +EC 4.2.3.96: avermitilol synthase +EC 4.2.3.97: (–)-δ-cadinene synthase +EC 4.2.3.98: (+)-T-muurolol synthase +EC 4.2.3.99: labdatriene synthase +EC 4.2.3.100: bicyclogermacrene synthase +EC 4.2.3.101: 7-epi-sesquithujene synthase +EC 4.2.3.102: sesquithujene synthase +EC 4.2.3.103: ent-isokaurene synthase +EC 4.2.3.104: α-humulene synthase +EC 4.2.3.105: tricyclene synthase +EC 4.2.3.106: (E)-β-ocimene synthase +EC 4.2.3.107: (+)-car-3-ene synthase +EC 4.2.3.108: 1,8-cineole synthase +EC 4.2.3.109: (–)-sabinene synthase +EC 4.2.3.110: (+)-sabinene synthase +EC 4.2.3.111: (–)-α-terpineol synthase +EC 4.2.3.112: (+)-α-terpineol synthase +EC 4.2.3.113: terpinolene synthase +EC 4.2.3.114: γ-terpinene synthase +EC 4.2.3.115: α-terpinene synthase +EC 4.2.3.116: (+)-camphene synthase +EC 4.2.3.117: (–)-camphene synthase +EC 4.2.3.118: 2-methylisoborneol synthase +EC 4.2.3.119: (-)-α-pinene synthase +EC 4.2.3.120: (-)-β-pinene synthase +EC 4.2.3.121: (+)-α-pinene synthase +EC 4.2.3.122: (+)-β-pinene synthase +EC 4.2.3.123: β-sesquiphellandrene synthase +EC 4.2.3.124: 2-deoxy-scyllo-inosose synthase +EC 4.2.3.125: α-muurolene synthase +EC 4.2.3.126: γ-muurolene synthase +EC 4.2.3.127: β-copaene synthase +EC 4.2.3.128: β-cubebene synthase +EC 4.2.3.129: (+)-sativene synthase +EC 4.2.3.130: tetraprenyl-β-curcumene synthase +EC 4.2.3.131: miltiradiene synthase +EC 4.2.3.132: neoabietadiene synthase +EC 4.2.3.133: α-copaene synthase +EC 4.2.3.134: 5-phosphooxy-L-lysine phospho-lyase +EC 4.2.3.135: Δ6-protoilludene synthase +EC 4.2.3.136: α-isocomene synthase +EC 4.2.3.137: (E)-2-epi-β-caryophyllene synthase +EC 4.2.3.138: (+)-epi-α-bisabolol synthase +EC 4.2.3.139: valerena-4,7(11)-diene synthase +EC 4.2.3.140: cis-abienol synthase +EC 4.2.3.141: sclareol synthase +EC 4.2.3.142: 7-epizingiberene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing] +EC 4.2.3.143: kunzeaol synthase +EC 4.2.3.144: geranyllinalool synthase +EC 4.2.3.145: ophiobolin F synthase +EC 4.2.3.146: cyclooctat-9-en-7-ol synthase +EC 4.2.3.147: pimaradiene synthase +EC 4.2.3.148: cembrene C synthase +EC 4.2.3.149: nephthenol synthase +EC 4.2.3.150: cembrene A synthase +EC 4.2.3.151: pentamethylcyclopentadecatrienol synthase +EC 4.2.3.152: 2-epi-5-epi-valiolone synthase +EC 4.2.3.153: (5-formylfuran-3-yl)methyl phosphate synthase +EC 4.2.3.154: demethyl-4-deoxygadusol synthase +EC 4.2.3.155: 2-epi-valiolone synthase +EC 4.2.3.156: hydroxysqualene synthase +EC 4.2.3.157: (+)-isoafricanol synthase +EC 4.2.3.158: (–)-spiroviolene synthase +EC 4.2.3.159: tsukubadiene synthase +EC 4.2.3.160: (2S,3R,6S,9S)-(–)-protoillud-7-ene synthase +EC 4.2.3.161: (3S)-(+)-asterisca-2(9),6-diene synthase +EC 4.2.3.162: (–)-α-amorphene synthase +EC 4.2.3.163: (+)-corvol ether B synthase +EC 4.2.3.164: (+)-eremophilene synthase +EC 4.2.3.165: (1R,4R,5S)-(–)-guaia-6,10(14)-diene synthase +EC 4.2.3.166: (+)-(1E,4E,6S,7R)-germacra-1(10),4-dien-6-ol synthase +EC 4.2.3.167: dolabella-3,7-dien-18-ol synthase +EC 4.2.3.168: dolathalia-3,7,11-triene synthase +EC 4.2.3.169: 7-epi-α-eudesmol synthase +EC 4.2.3.170: 4-epi-cubebol synthase +EC 4.2.3.171: (+)-corvol ether A synthase +EC 4.2.3.172: 10-epi-juneol synthase +EC 4.2.3.173: τ-cadinol synthase +EC 4.2.3.174: (2E,6E)-hedycaryol synthase +EC 4.2.3.175: 10-epi-cubebol synthase +EC 4.2.3.176: sesterfisherol synthase +EC 4.2.3.177: β-thujene synthase +EC 4.2.3.178: stellata-2,6,19-triene synthase +EC 4.2.3.179: guaia-4,6-diene synthase +EC 4.2.3.180: pseudolaratriene synthase +EC 4.2.3.181: selina-4(15),7(11)-diene synthase +EC 4.2.3.182: pristinol synthase +EC 4.2.3.183: nezukol synthase +EC 4.2.3.184: 5-hydroxy-α-gurjunene synthase +EC 4.2.3.185: ent-atiserene synthase +EC 4.2.3.186: ent-13-epi-manoyl oxide synthase +EC 4.2.3.187: (2Z,6E)-hedycaryol synthase +EC 4.2.3.188: β-geranylfarnesene synthase +EC 4.2.3.189: 9,13-epoxylabd-14-ene synthase +EC 4.2.3.190: manoyl oxide synthase +EC 4.2.3.191: cycloaraneosene synthase +EC 4.2.3.192: labda-7,13(16),14-triene synthase +EC 4.2.3.193: (12E)-labda-8(17),12,14-triene synthase +EC 4.2.3.194: (–)-drimenol synthase +EC 4.2.3.195: rhizathalene A synthase +EC 4.2.3.196: dolabradiene synthase +EC 4.2.3.197: eudesmane-5,11-diol synthase +EC 4.2.3.198: α-selinene synthase +EC 4.2.3.199: (–)-5-epieremophilene synthase +EC 4.2.3.200: β-pinacene synthase +EC 4.2.3.201: hydropyrene synthase +EC 4.2.3.202: hydropyrenol synthase +EC 4.2.3.203: isoelisabethatriene synthase +EC 4.2.3.204: valerianol synthase +EC 4.2.3.205: sodorifen synthase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-4.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-4.md new file mode 100644 index 000000000..8043acf1d --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)-4.md @@ -0,0 +1,203 @@ +--- +title: "List of EC numbers (EC 4)" +chunk: 5/5 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_4)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:09.661506+00:00" +instance: "kb-cron" +--- + +=== EC 4.2.99: Other Carbon-Oxygen Lyases === +EC 4.2.99.1: Now EC 4.2.2.1, hyaluronate lyase +EC 4.2.99.2: Now EC 4.2.3.1, threonine synthase +EC 4.2.99.3: Now EC 4.2.2.2, pectate lyase +EC 4.2.99.4: Now EC 4.2.2.3, poly(β-D-mannuronate) lyase +EC 4.2.99.5: deleted +EC 4.2.99.6: Now included with EC 4.2.2.4 (chondroitin ABC lyase) and EC 4.2.2.5 (chondroitin AC lyase) +EC 4.2.99.7: Now EC 4.2.3.2, ethanolamine-phosphate phospho-lyase +EC 4.2.99.8: Now EC 2.5.1.47, cysteine synthase +EC 4.2.99.9: Now EC 2.5.1.48, cystathionine γ-synthase +EC 4.2.99.10: Now EC 2.5.1.49 EC 2.5.1.49, O-acetylhomoserine aminocarboxypropyltransferase +EC 4.2.99.11: Now EC 4.2.3.3, methylglyoxal synthase +EC 4.2.99.12: carboxymethyloxysuccinate lyase +EC 4.2.99.13: Now EC 2.5.1.50, zeatin 9-aminocarboxyethyltransferase +EC 4.2.99.14: Now EC 2.5.1.51, β-pyrazolylalanine synthase +EC 4.2.99.15: Now EC 2.5.1.52, L-mimosine synthase +EC 4.2.99.16: Now EC 2.5.1.53, uracilylalanine synthase +EC 4.2.99.17: Listed as EC 2.5.1.51, β-pyrazolylalanine synthase +EC 4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase +EC 4.2.99.19: Now EC 4.4.1.23, 2-hydroxypropyl-CoM lyase +EC 4.2.99.20: 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase +EC 4.2.99.21: isochorismate lyase +EC 4.2.99.22: tuliposide A-converting enzyme +EC 4.2.99.23: tuliposide B-converting enzyme +EC 4.2.99.24: thebaine synthase + +== EC 4.3: Carbon-Nitrogen Lyases == + +=== EC 4.3.1: Ammonia-Lyases === +EC 4.3.1.1: aspartate ammonia-lyase +EC 4.3.1.2: methylaspartate ammonia-lyase +EC 4.3.1.3: histidine ammonia-lyase +EC 4.3.1.4: formiminotetrahydrofolate cyclodeaminase +EC 4.3.1.5: Now divided into EC 4.3.1.23 (tyrosine ammonia-lyase), EC 4.3.1.24 (phenylalanine ammonia-lyase) and EC 4.3.1.25 (phenylalanine/tyrosine ammonia-lyase) +EC 4.3.1.6: β-alanyl-CoA ammonia-lyase +EC 4.3.1.7: ethanolamine ammonia-lyase +EC 4.3.1.8: Now EC 2.5.1.61, hydroxymethylbilane synthase +EC 4.3.1.9: glucosaminate ammonia-lyase +EC 4.3.1.10: serine-sulfate ammonia-lyase +EC 4.3.1.11: Deleted: inadequately characterized +EC 4.3.1.12: ornithine cyclodeaminase +EC 4.3.1.13: carbamoyl-serine ammonia-lyase +EC 4.3.1.14: 3-aminobutyryl-CoA ammonia-lyase +EC 4.3.1.15: diaminopropionate ammonia-lyase +EC 4.3.1.16: threo-3-hydroxy-L-aspartate ammonia-lyase +EC 4.3.1.17: L-serine ammonia-lyase +EC 4.3.1.18: D-serine ammonia-lyase +EC 4.3.1.19: threonine ammonia-lyase +EC 4.3.1.20: erythro-3-hydroxy-L-aspartate ammonia-lyase +EC 4.3.1.21: identical to EC 4.3.1.9, glucosaminate ammonia-lyase +EC 4.3.1.22: 3,4-dihydroxyphenylalanine reductive deaminase +EC 4.3.1.23: tyrosine ammonia-lyase +EC 4.3.1.24: phenylalanine ammonia-lyase +EC 4.3.1.25: phenylalanine/tyrosine ammonia-lyase +EC 4.3.1.26: Now EC 1.21.3.9, dichlorochromopyrrolate synthase +EC 4.3.1.27: threo-3-hydroxy-D-aspartate ammonia-lyase +EC 4.3.1.28: L-lysine cyclodeaminase +EC 4.3.1.29: D-glucosaminate-6-phosphate ammonia-lyase +EC 4.3.1.30: dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase +EC 4.3.1.31: L-tryptophan ammonia lyase +EC 4.3.1.32: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase + +=== EC 4.3.2: Amidine-Lyases === +EC 4.3.2.1: argininosuccinate lyase +EC 4.3.2.2: adenylosuccinate lyase +EC 4.3.2.3: ureidoglycolate lyase +EC 4.3.2.4: purine imidazole-ring cyclase +EC 4.3.2.5: peptidylamidoglycolate lyase +EC 4.3.2.6: γ-L-glutamyl-butirosin B γ-glutamyl cyclotransferase +EC 4.3.2.7: glutathione-specific γ-glutamylcyclotransferase +EC 4.3.2.8: γ-glutamylamine cyclotransferase +EC 4.3.2.9: γ-glutamylcyclotransferase +EC 4.3.2.10: imidazole glycerol-phosphate synthase + +=== EC 4.3.3: Amine-Lyases === +EC 4.3.3.1: 3-ketovalidoxylamine C-N-lyase +EC 4.3.3.2: strictosidine synthase +EC 4.3.3.3: deacetylisoipecoside synthase +EC 4.3.3.4: deacetylipecoside synthase +EC 4.3.3.5: 4′-demethylrebeccamycin synthase +EC 4.3.3.6: pyridoxal 5′-phosphate synthase (glutamine hydrolysing) +EC 4.3.3.7: 4-hydroxy-tetrahydrodipicolinate synthase + +=== EC 4.3.99: Other Carbon-Nitrogen Lyases === +EC 4.3.99.1: Now EC 4.2.1.104, cyanate hydratase +EC 4.3.99.2: Now EC 7.2.4.1, carboxybiotin decarboxylase +EC 4.3.99.3: 7-carboxy-7-deazaguanine synthase +EC 4.3.99.4: choline trimethylamine-lyase + +== EC 4.4: Carbon-Sulfur Lyases == + +=== EC 4.4.1: Carbon-sulfur lyases (only sub-subclass identified to date) === +EC 4.4.1.1: cystathionine γ-lyase +EC 4.4.1.2: homocysteine desulfhydrase +EC 4.4.1.3: dimethylpropiothetin dethiomethylase +EC 4.4.1.4: alliin lyase +EC 4.4.1.5: lactoylglutathione lyase +EC 4.4.1.6: Now included in EC 4.4.1.13, cysteine-S-conjugate β-lyase +EC 4.4.1.7: Now included with EC 2.5.1.18 glutathione transferase +EC 4.4.1.8: Now included in EC 4.4.1.13, cysteine-S-conjugate β-lyase +EC 4.4.1.9: L-3-cyanoalanine synthase +EC 4.4.1.10: cysteine lyase +EC 4.4.1.11: methionine γ-lyase +EC 4.4.1.12: deleted: activity due to EC 2.3.3.15, sulfoacetaldehyde acetyltransferase +EC 4.4.1.13: cysteine-S-conjugate β-lyase +EC 4.4.1.14: 1-aminocyclopropane-1-carboxylate synthase +EC 4.4.1.15: D-cysteine desulfhydrase +EC 4.4.1.16: selenocysteine lyase +EC 4.4.1.17: holocytochrome-c synthase +EC 4.4.1.18: Now EC 1.8.3.5, prenylcysteine oxidase +EC 4.4.1.19: phosphosulfolactate synthase +EC 4.4.1.20: leukotriene-C4 synthase +EC 4.4.1.21: S-ribosylhomocysteine lyase +EC 4.4.1.22: S-(hydroxymethyl)glutathione synthase +EC 4.4.1.23: 2-hydroxypropyl-CoM lyase +EC 4.4.1.24: (2R)-sulfolactate sulfo-lyase +EC 4.4.1.25: L-cysteate sulfo-lyase +EC 4.4.1.26: olivetolic acid cyclase +EC 4.4.1.27: Now EC 3.13.1.5, carbon disulfide hydrolase + +== EC 4.5: Carbon-Halide Lyases == + +=== EC 4.5.1: Carbon-halide lyases (only sub-subclass identified to date) === +EC 4.5.1.1: DDT-dehydrochlorinase +EC 4.5.1.2: 3-chloro-D-alanine dehydrochlorinase +EC 4.5.1.3: dichloromethane dehalogenase +EC 4.5.1.4: L-2-amino-4-chloropent-4-enoate dehydrochlorinase +EC 4.5.1.5: S-carboxymethylcysteine synthase + +== EC 4.6: Phosphorus-Oxygen Lyases == + +=== EC 4.6.1: Phosphorus-oxygen lyases (only sub-subclass identified to date) === +EC 4.6.1.1: adenylate cyclase +EC 4.6.1.2: guanylate cyclase +EC 4.6.1.3: Now EC 4.2.3.4, 3-dehydroquinate synthase +EC 4.6.1.4: Now EC 4.2.3.5, chorismate synthase +EC 4.6.1.5: Now EC 4.2.3.7, pentalenene synthase +EC 4.6.1.6: cytidylate cyclase +EC 4.6.1.7: Now EC 4.2.3.8, casbene synthase +EC 4.6.1.8: Now EC 4.2.3.10, (-)-endo-fenchol synthase +EC 4.6.1.9: Now Now EC 4.2.3.11, sabinene-hydrate synthase +EC 4.6.1.10: Now EC 4.2.3.12, 6-pyruvoyltetrahydropterin synthase +EC 4.6.1.11: Now EC 4.2.3.13, (+)-δ-cadinene synthase +EC 4.6.1.12: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase +EC 4.6.1.13: phosphatidylinositol diacylglycerol-lyase +EC 4.6.1.14: glycosylphosphatidylinositol diacylglycerol-lyase +EC 4.6.1.15: FAD-AMP lyase (cyclizing) +EC 4.6.1.16: tRNA-intron lyase +EC 4.6.1.17: cyclic pyranopterin monophosphate synthase +EC 4.6.1.18: pancreatic ribonuclease +EC 4.6.1.19: ribonuclease T2 +EC 4.6.1.20: ribonuclease U2 +EC 4.6.1.21: Enterobacter ribonuclease +EC 4.6.1.22: Bacillus subtilis ribonuclease +EC 4.6.1.23: ribotoxin * +EC 4.6.1.24: ribonuclease T1 +EC 4.6.1.25: bacteriophage T4 restriction endoribonuclease RegB + +== EC 4.7: Carbon-phosphorus lyases == + +=== EC 4.7.1: Carbon-phosphorus lyases (only sub-subclass identified to date) === +EC 4.7.1.1 α-D ribose 1-methylphosphonate 5-phosphate C-P-lyase * + +== EC 4.8: Nitrogen-oxygen lyases == + +=== EC 4.8.1: Hydro-lyases === +EC 4.8.1.1: L-piperazate synthase +EC 4.8.1.2: aliphatic aldoxime dehydratase +EC 4.8.1.3: indoleacetaldoxime dehydratase +EC 4.8.1.4: phenylacetaldoxime dehydratase + +== EC 4.98: ATP-independent chelatases == + +=== EC 4.98.1: Forming coordination complexes === +EC 4.98.1.1: protoporphyrin ferrochelatase + +== EC 4.99: Other Lyases == + +=== EC 4.99.1: Sole sub-subclass for lyases that do not belong in the other subclasses === +EC 4.99.1.1: Now EC 4.98.1.1 +EC 4.99.1.2: alkylmercury lyase +EC 4.99.1.3: sirohydrochlorin cobaltochelatase +EC 4.99.1.4: sirohydrochlorin ferrochelatase +EC 4.99.1.5: Now EC 4.8.1.2, aliphatic aldoxime dehydratase +EC 4.99.1.6: Now EC 4.8.1.3, indoleacetaldoxime dehydratase +EC 4.99.1.7: Now EC 4.8.1.4, phenylacetaldoxime dehydratase +EC 4.99.1.8: heme ligase +EC 4.99.1.9:: coproporphyrin ferrochelatase +EC 4.99.1.10: magnesium dechelatase +EC 4.99.1.11: sirohydrochlorin nickelchelatase +EC 4.99.1.12: pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel chelatase + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-0.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-0.md new file mode 100644 index 000000000..52dd3feec --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-0.md @@ -0,0 +1,215 @@ +--- +title: "List of EC numbers (EC 5)" +chunk: 1/2 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:10.997779+00:00" +instance: "kb-cron" +--- + +This list contains a list of EC numbers for the fifth group, EC 5, isomerases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. + +== EC 5.1: Epimerases and racemases == + +=== EC 5.1.1: Acting on Amino acids and Derivatives === +EC 5.1.1.1: alanine racemase +EC 5.1.1.2: methionine racemase +EC 5.1.1.3: glutamate racemase +EC 5.1.1.4: proline racemase +EC 5.1.1.5: lysine racemase +EC 5.1.1.6: threonine racemase +EC 5.1.1.7: diaminopimelate epimerase +EC 5.1.1.8: 4-hydroxyproline epimerase +EC 5.1.1.9: arginine racemase +EC 5.1.1.10: amino-acid racemase +EC 5.1.1.11: phenylalanine racemase (ATP-hydrolysing) +EC 5.1.1.12: ornithine racemase +EC 5.1.1.13: aspartate racemase +EC 5.1.1.14: nocardicin-A epimerase +EC 5.1.1.15: 2-aminohexano-6-lactam racemase +EC 5.1.1.16: protein-serine epimerase +EC 5.1.1.17: isopenicillin-N epimerase +EC 5.1.1.18: serine racemase +EC 5.1.1.20: L-Ala-D/L-Glu epimerase +EC 5.1.1.21: isoleucine 2-epimerase +EC 5.1.1.22: 4-hydroxyproline betaine 2-epimerase +EC 5.1.1.23: UDP-N-acetyl-α-D-muramoyl-L-alanyl-L-glutamate epimerase +EC 5.1.1.24: histidine racemase + +=== EC 5.1.2: Acting on Hydroxy acids and Derivatives === +EC 5.1.2.1: lactate racemase +EC 5.1.2.2: mandelate racemase +EC 5.1.2.3: 3-hydroxybutyryl-CoA epimerase +EC 5.1.2.4: acetoin racemase +EC 5.1.2.5: tartrate epimerase +EC 5.1.2.6: isocitrate epimerase +EC 5.1.2.7: tagaturonate epimerase + +=== EC 5.1.3: Acting on Carbohydrates and Derivatives === +EC 5.1.3.1: ribulose-phosphate 3-epimerase +EC 5.1.3.2: UDP-glucose 4-epimerase +EC 5.1.3.3: aldose 1-epimerase +EC 5.1.3.4: L-ribulose-5-phosphate 4-epimerase +EC 5.1.3.5: UDP-arabinose 4-epimerase +EC 5.1.3.6: UDP-glucuronate 4-epimerase +EC 5.1.3.7: UDP-N-acetylglucosamine 4-epimerase +EC 5.1.3.8: N-acylglucosamine 2-epimerase +EC 5.1.3.9: N-acylglucosamine-6-phosphate 2-epimerase +EC 5.1.3.10: CDP-paratose 2-epimerase +EC 5.1.3.11: cellobiose epimerase +EC 5.1.3.12: The enzyme has never been purified and the activity was later shown not to exist +EC 5.1.3.13: dTDP-4-dehydrorhamnose 3,5-epimerase +EC 5.1.3.14: UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) +EC 5.1.3.15: glucose-6-phosphate 1-epimerase +EC 5.1.3.16: UDP-glucosamine 4-epimerase +EC 5.1.3.17: heparosan-N-sulfate-glucuronate 5-epimerase +EC 5.1.3.18: GDP-mannose 3,5-epimerase +EC 5.1.3.19: chondroitin-glucuronate 5-epimerase +EC 5.1.3.20: ADP-glyceromanno-heptose 6-epimeras +EC 5.1.3.21: maltose epimerase +EC 5.1.3.22: L-ribulose-5-phosphate 3-epimerase +EC 5.1.3.23: UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase +EC 5.1.3.24: N-acetylneuraminate epimerase +EC 5.1.3.25: dTDP-L-rhamnose 4-epimerase +EC 5.1.3.26: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 4-epimerase +EC 5.1.3.27: dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase +EC 5.1.3.28: UDP-N-acetyl-L-fucosamine synthase +EC 5.1.3.29: L-fucose mutarotase +EC 5.1.3.30: D-psicose 3-epimerase +EC 5.1.3.31: D-tagatose 3-epimerase +EC 5.1.3.32: L-rhamnose mutarotase +EC 5.1.3.33: 2-epi-5-epi-valiolone epimerase +EC 5.1.3.34: monoglucosyldiacylglycerol epimerase +EC 5.1.3.35: 2-epi-5-epi-valiolone 7-phosphate 2-epimerase +EC 5.1.3.36: heparosan-glucuronate 5-epimerase +EC 5.1.3.37: mannuronan 5-epimerase +EC 5.1.3.38: D-erythrulose 1-phosphate 3-epimerase +EC 5.1.3.39: L-erythrulose 4-phosphate epimerase. The activity has been shown not to take place. +EC 5.1.3.40: D-tagatose 6-phosphate 4-epimerase +EC 5.1.3.41: fructoselysine 3-epimerase +EC 5.1.3.42: D-glucosamine-6-phosphate 4-epimerase +EC 5.1.3.43: sulfoquinovose mutarotase +EC 5.1.3.44: mannose 2-epimerase + +=== EC 5.1.99: Acting on Other Compounds === +EC 5.1.99.1: methylmalonyl-CoA epimerase +EC 5.1.99.2: 16-hydroxysteroid epimerase +EC 5.1.99.3: allantoin racemase +EC 5.1.99.4: α-methylacyl-CoA racemase +EC 5.1.99.5: hydantoin racemase +EC 5.1.99.6: NAD(P)H-hydrate epimerase +EC 5.1.99.7: dihydroneopterin triphosphate 2′-epimerase +EC 5.1.99.8: 7,8-dihydroneopterin epimerase + +== EC 5.2: cis-trans-Isomerases == + +=== EC 5.2.1: cis-trans Isomerases (only sub-subclass identified to date) === +EC 5.2.1.1: maleate isomerase +EC 5.2.1.2: maleylacetoacetate isomerase +EC 5.2.1.3: Now known to be catalysed by a pathway involving EC 1.1.1.300, NADP-retinol dehydrogenase; EC 2.3.1.135, phosphatidylcholine—retinol O-acyltransferase; EC 3.1.1.64, retinoid isomerohydrolase; and EC 1.1.1.315, 11-cis-retinol dehydrogenase. +EC 5.2.1.4: maleylpyruvate isomerase +EC 5.2.1.5: linoleate isomerase +EC 5.2.1.6: furylfuramide isomerase +EC 5.2.1.7: transferred to EC 3.1.1.64, retinoid isomerohydrolase +EC 5.2.1.8: peptidylprolyl isomerase +EC 5.2.1.9: farnesol 2-isomerase +EC 5.2.1.10: 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase +EC 5.2.1.11: DELETED "4-hydroxyphenylacetaldehyde-oxime isomerase" – The existence of this enzyme has been called into question by one of the authors of the reference cited +EC 5.2.1.12: ζ-carotene isomerase +EC 5.2.1.13: prolycopene isomerase +EC 5.2.1.14: β-carotene isomerase + +== EC 5.3: Intramolecular Oxidoreductases == + +=== EC 5.3.1: Interconverting Aldoses and Ketoses === +EC 5.3.1.1: triose-phosphate isomerase +EC 5.3.1.2: deleted +EC 5.3.1.3: D-arabinose isomerase +EC 5.3.1.4: L-arabinose isomerase +EC 5.3.1.5: xylose isomerase +EC 5.3.1.6: ribose-5-phosphate isomerase +EC 5.3.1.7: mannose isomerase +EC 5.3.1.8: mannose-6-phosphate isomerase +EC 5.3.1.9: glucose-6-phosphate isomerase +EC 5.3.1.10: Now EC 3.5.99.6, glucosamine-6-phosphate deaminase +EC 5.3.1.11: deleted +EC 5.3.1.12: glucuronate isomerase +EC 5.3.1.13: arabinose-5-phosphate isomerase +EC 5.3.1.14: L-rhamnose isomerase +EC 5.3.1.15: D-lyxose ketol-isomerase +EC 5.3.1.16: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase +EC 5.3.1.17: 5-dehydro-4-deoxy-D-glucuronate isomerase +EC 5.3.1.18: deleted: reaction is due to EC 5.3.1.9 glucose-6-phosphate isomerase, in the presence of arsenate, or EC 5.3.1.5 xylose isomerase +EC 5.3.1.19: Now EC 2.6.1.16, glutamine—fructose-6-phosphate transaminase (isomerizing) +EC 5.3.1.20: ribose isomerase +EC 5.3.1.21: corticosteroid side-chain-isomerase +EC 5.3.1.22: hydroxypyruvate isomerase +EC 5.3.1.23: S-methyl-5-thioribose-1-phosphate isomerase +EC 5.3.1.24: phosphoribosylanthranilate isomerase +EC 5.3.1.25: L-fucose isomerase +EC 5.3.1.26: galactose-6-phosphate isomerase +EC 5.3.1.27: 6-phospho-3-hexuloisomerase +EC 5.3.1.28: D-sedoheptulose 7-phosphate isomerase +EC 5.3.1.29: ribose 1,5-bisphosphate isomerase +EC 5.3.1.30: 5-deoxy-glucuronate isomerase +EC 5.3.1.31: sulfoquinovose isomerase +EC 5.3.1.32: (4S)-4-hydroxy-5-phosphooxypentane-2,3-dione isomerase +EC 5.3.1.33: L-erythrulose 1-phosphate isomerase +EC 5.3.1.34: D-erythrulose 4-phosphate isomerase +EC 5.3.1.35: 2-dehydrotetronate isomerase +EC 5.3.1.36: D-apiose isomerase + +=== EC 5.3.2: Interconverting Keto- and Enol-Groups === +EC 5.3.2.1: phenylpyruvate tautomerase +EC 5.3.2.2: oxaloacetate tautomerase +EC 5.3.2.3: TDP-4-oxo-6-deoxy-α-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-galactopyranose-forming) +EC 5.3.2.4: TDP-4-oxo-6-deoxy-α-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-glucopyranose-forming) +EC 5.3.2.5: 2,3-diketo-5-methylthiopentyl-1-phosphate enolase +EC 5.3.2.6: 2-hydroxymuconate tautomerase +EC 5.3.2.7: ascopyrone tautomerase +EC 5.3.2.8: 4-oxalomesaconate tautomerase + +=== EC 5.3.3: Transposing C=C Bonds === +EC 5.3.3.1: steroid Δ-isomerase +EC 5.3.3.2: isopentenyl-diphosphate Δ-isomerase +EC 5.3.3.3: vinylacetyl-CoA Δ-isomerase +EC 5.3.3.4: muconolactone Δ-isomerase +EC 5.3.3.5: cholestenol Δ-isomerase +EC 5.3.3.6: methylitaconate Δ-isomerase +EC 5.3.3.7: aconitate Δ-isomerase +EC 5.3.3.8: Δ3-Δ2-enoyl-CoA isomerase +EC 5.3.3.9: prostaglandin-A1 Δ-isomerase +EC 5.3.3.10: 5-carboxymethyl-2-hydroxymuconate Δ-isomerase +EC 5.3.3.11: isopiperitenone Δ-isomerase +EC 5.3.3.12: L-dopachrome isomerase +EC 5.3.3.13: polyenoic fatty acid isomerase +EC 5.3.3.14: trans-2-decenoyl-[acyl-carrier protein] isomerase +EC 5.3.3.15: Now EC 5.3.2.7, ascopyrone tautomerase +EC 5.3.3.16: Now EC 5.3.2.8, 4-oxalomesaconate tautomerase +EC 5.3.3.17: trans-2,3-dihydro-3-hydroxyanthranilate isomerase +EC 5.3.3.18: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase +EC 5.3.3.19: 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase +EC 5.3.3.20: Now EC 5.4.99.64, 2-hydroxyisobutanoyl-CoA mutase +EC 5.3.3.21: Δ3,5-Δ2,4-dienoyl-CoA isomerase +EC 5.3.3.22: lutein isomerase +EC 5.3.3.23: S-methyl-5-thioribulose 1-phosphate isomerase + +=== EC 5.3.4: Transposing S-S Bonds === +EC 5.3.4.1: protein disulfide-isomerase + +=== EC 5.3.99: Other Intramolecular Oxidoreductases === +EC 5.3.99.1: deleted, reaction due to combined action of EC 4.2.1.92 (hydroperoxide dehydratase) and EC 5.3.99.6 (allene-oxide cyclase) +EC 5.3.99.2: prostaglandin-D synthase +EC 5.3.99.3: prostaglandin-E synthase +EC 5.3.99.4: prostaglandin-I synthase +EC 5.3.99.5: thromboxane-A synthase +EC 5.3.99.6: allene-oxide cyclase +EC 5.3.99.7: styrene-oxide isomerase +EC 5.3.99.8: capsanthin/capsorubin synthase +EC 5.3.99.9: neoxanthin synthase +EC 5.3.99.10: thiazole tautomerase +EC 5.3.99.11: 2-keto-myo-inositol isomerase +EC 5.3.99.12: lachrymatory factor synthase + +== EC 5.4: Intramolecular Transferases == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-1.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-1.md new file mode 100644 index 000000000..2526b96eb --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)-1.md @@ -0,0 +1,194 @@ +--- +title: "List of EC numbers (EC 5)" +chunk: 2/2 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_5)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:10.997779+00:00" +instance: "kb-cron" +--- + +=== EC 5.4.1: Transferring Acyl Groups === +EC 5.4.1.1: lysolecithin acylmutase +EC 5.4.1.2: Now EC 5.4.99.61, precorrin-8X methylmutase +EC 5.4.1.3: 2-methylfumaryl-CoA isomerase +EC 5.4.1.4: D-galactarolactone isomerase + +=== EC 5.4.2: Phosphotransferases (Phosphomutases) === +EC 5.4.2.1: Now recognized as two separate enzymes EC 5.4.2.11, phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) and EC 5.4.2.12, phosphoglycerate mutase (2,3-diphosphoglycerate-independent) +EC 5.4.2.2: phosphoglucomutase (α-D-glucose-1,6-bisphosphate-dependent) +EC 5.4.2.3: phosphoacetylglucosamine mutase +EC 5.4.2.4: bisphosphoglycerate mutase +EC 5.4.2.5: phosphoglucomutase (glucose-cofactor) +EC 5.4.2.6: β-phosphoglucomutase +EC 5.4.2.7: phosphopentomutase +EC 5.4.2.8: phosphomannomutase +EC 5.4.2.9: phosphoenolpyruvate mutase +EC 5.4.2.10: phosphoglucosamine mutase +EC 5.4.2.11: phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) +EC 5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent) +EC 5.4.2.13: phosphogalactosamine mutase + +=== EC 5.4.3: Transferring Amino Groups === +EC 5.4.3.1: deleted; this reaction was due to a mixture of EC 5.1.1.12 (ornithine racemase) and EC 5.4.3.5 (D-ornithine 4,5-aminomutase) +EC 5.4.3.2: lysine 2,3-aminomutase +EC 5.4.3.3: lysine 5,6-aminomutase +EC 5.4.3.4: Now included in EC 5.4.3.3, lysine 5,6-aminomutase +EC 5.4.3.5: D-ornithine 4,5-aminomutase +EC 5.4.3.6: tyrosine 2,3-aminomutase +EC 5.4.3.7: leucine 2,3-aminomutase +EC 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase +EC 5.4.3.9: glutamate 2,3-aminomutase +EC 5.4.3.10: phenylalanine aminomutase (L-β-phenylalanine forming) +EC 5.4.3.11: phenylalanine aminomutase (D-β-phenylalanine forming) + +=== EC 5.4.4: Transferring hydroxy groups === +EC 5.4.4.1: (hydroxyamino)benzene mutase +EC 5.4.4.2: isochorismate synthase +EC 5.4.4.3: 3-(hydroxyamino)phenol mutase +EC 5.4.4.4: geraniol isomerase +EC 5.4.4.5: 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase +EC 5.4.4.6: 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase +EC 5.4.4.7: hydroperoxy icosatetraenoate isomerase +EC 5.4.4.8: linalool isomerase +EC 5.4.4.9: pyrogallol hydroxytransferase + +=== EC 5.4.99: Transferring Other Groups === +EC 5.4.99.1: methylaspartate mutase +EC 5.4.99.2: methylmalonyl-CoA mutase +EC 5.4.99.3: 2-acetolactate mutase +EC 5.4.99.4: 2-methyleneglutarate mutase +EC 5.4.99.5: chorismate mutase +EC 5.4.99.6: Now EC 5.4.4.2, isochorismate synthase +EC 5.4.99.7: lanosterol synthase +EC 5.4.99.8: cycloartenol synthase +EC 5.4.99.9: UDP-galactopyranose mutase +EC 5.4.99.10: Now included with EC 5.4.99.11, isomaltulose synthase +EC 5.4.99.11: isomaltulose synthase +EC 5.4.99.12: tRNA pseudouridine38-40 synthase +EC 5.4.99.13: isobutyryl-CoA mutase +EC 5.4.99.14: 4-carboxymethyl-4-methylbutenolide mutase +EC 5.4.99.15: (1→4)-α-D-glucan 1-α-D-glucosylmutase +EC 5.4.99.16: maltose α-D-glucosyltransferase +EC 5.4.99.17: squalene—hopene cyclase +EC 5.4.99.18: 5-(carboxyamino)imidazole ribonucleotide mutase +EC 5.4.99.19: 16S rRNA pseudouridine516 synthase +EC 5.4.99.20: 23S rRNA pseudouridine2457 synthase +EC 5.4.99.21: 23S rRNA pseudouridine2604 synthase +EC 5.4.99.22: 23S rRNA pseudouridine2605 synthase +EC 5.4.99.23: 23S rRNA pseudouridine1911/1915/1917 synthase +EC 5.4.99.24: 23S rRNA pseudouridine955/2504/2580 synthase +EC 5.4.99.25: tRNA pseudouridine55 synthase +EC 5.4.99.26: tRNA pseudouridine65 synthase +EC 5.4.99.27: tRNA pseudouridine13 synthase +EC 5.4.99.28: RNA pseudouridine32 synthase +EC 5.4.99.29: 23S rRNA pseudouridine746 synthase +EC 5.4.99.30: UDP-arabinopyranose mutase +EC 5.4.99.31: thalianol synthase +EC 5.4.99.32: protostadienol synthase +EC 5.4.99.33: cucurbitadienol synthase +EC 5.4.99.34: germanicol synthase +EC 5.4.99.35: taraxerol synthase +EC 5.4.99.36: isomultiflorenol synthase +EC 5.4.99.37: dammaradiene synthase +EC 5.4.99.38: camelliol C synthase +EC 5.4.99.39: β-amyrin synthase +EC 5.4.99.40: α-amyrin synthase +EC 5.4.99.41: lupeol synthase +EC 5.4.99.42: tRNA pseudouridine31 synthase +EC 5.4.99.43: 21S rRNA pseudouridine2819 synthase +EC 5.4.99.44: mitochondrial tRNA pseudouridine27/28 synthase +EC 5.4.99.45: tRNA pseudouridine38/39 synthase +EC 5.4.99.46: shionone synthase +EC 5.4.99.47: parkeol synthase +EC 5.4.99.48: achilleol B synthase +EC 5.4.99.49: glutinol synthase +EC 5.4.99.50: friedelin synthase +EC 5.4.99.51: baccharis oxide synthase +EC 5.4.99.52: α-seco-amyrin synthase +EC 5.4.99.53: marneral synthase +EC 5.4.99.54: β-seco-amyrin synthase +EC 5.4.99.55: δ-amyrin synthase +EC 5.4.99.56: tirucalladienol synthase +EC 5.4.99.57: baruol synthase +EC 5.4.99.58: methylornithine synthase +EC 5.4.99.59: dTDP-fucopyranose mutase +EC 5.4.99.60: cobalt-precorrin-8 methylmutase +EC 5.4.99.61: precorrin-8X methylmutase +EC 5.4.99.62: D-ribose pyranase +EC 5.4.99.63: ethylmalonyl-CoA mutase +EC 5.4.99.64: 2-hydroxyisobutanoyl-CoA mutase +EC 5.4.99.65: pre-α-onocerin synthase +EC 5.4.99.66: α-onocerin synthase +EC 5.4.99.67: 4-amino-4-deoxychorismate mutase + +== EC 5.5: Intramolecular Lyases == + +=== EC 5.5.1: Intramolecular lyases (only sub-subclass identified to date) === +EC 5.5.1.1: muconate cycloisomerase +EC 5.5.1.2: 3-carboxy-cis,cis-muconate cycloisomerase +EC 5.5.1.3: tetrahydroxypteridine cycloisomerase +EC 5.5.1.4: inositol-3-phosphate synthase +EC 5.5.1.5: carboxy-cis,cis-muconate cyclase +EC 5.5.1.6: chalcone isomerase +EC 5.5.1.7: chloromuconate cycloisomerase +EC 5.5.1.8: (+)-bornyl diphosphate synthase +EC 5.5.1.9: cycloeucalenol cycloisomerase +EC 5.5.1.10: α-pinene-oxide decyclase +EC 5.5.1.11: dichloromuconate cycloisomerase +EC 5.5.1.12: copalyl diphosphate synthase +EC 5.5.1.13: ent-copalyl diphosphate synthase +EC 5.5.1.14: syn-copalyl-diphosphate synthase +EC 5.5.1.15: terpentedienyl-diphosphate synthase +EC 5.5.1.16: halimadienyl-diphosphate synthase +EC 5.5.1.17: (S)-β-macrocarpene synthase +EC 5.5.1.18: lycopene ε-cyclase +EC 5.5.1.19: lycopene β-cyclase +EC 5.5.1.20: prosolanapyrone-III cycloisomerase +EC 5.5.1.21: [[copal-8-ol diphosphate synthase. The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. See EC 4.2.1.133, copal-8-ol diphosphate hydratase]] +EC 5.5.1.22: (–)-bornyl diphosphate synthase +EC 5.5.1.23: aklanonic acid methyl ester cyclase +EC 5.5.1.24: tocopherol cyclase +EC 5.5.1.25: 3,6-anhydro-L-galactonate cycloisomerase +EC 5.5.1.26: nogalonic acid methyl ester cyclase +EC 5.5.1.27: D-galactarolactone cycloisomerase +EC 5.5.1.28: (–)-kolavenyl diphosphate synthase +EC 5.5.1.29: (+)-kolavenyl diphosphate synthase +EC 5.5.1.30: labda-7,13-dienyl diphosphate synthase +EC 5.5.1.31: hapalindole H synthase +EC 5.5.1.32: 12-epi-hapalindole U synthase +EC 5.5.1.33: 12-epi-fischerindole U synthase +EC 5.5.1.34: (+)-cis,trans-nepetalactol synthase +EC 5.5.1.35: (+)-cis,cis-nepetalactol synthase +EC 5.5.1.36: hapalindole U synthase +EC 5.5.1.37: catharanthine synthase +EC 5.5.1.38: tabersonine synthase + +== EC 5.6: Isomerases altering macromolecular conformation == + +=== EC 5.6.1: Enzymes altering polypeptide conformation or assembly === +EC 5.6.1.1: microtubule-severing ATPase +EC 5.6.1.2: dynein ATPase +EC 5.6.1.3: plus-end-directed kinesin ATPase +EC 5.6.1.4: minus-end-directed kinesin ATPase +EC 5.6.1.5: proteasome ATPase +EC 5.6.1.6: channel-conductance-controlling ATPase +EC 5.6.1.7: chaperonin ATPase +EC 5.6.1.8: myosin ATPase +EC 5.6.1.9: (R)-2-hydroxyacyl-CoA dehydratase activating ATPase + +=== EC 5.6.2: Enzymes altering nucleic acid conformation === +EC 5.6.2.1: DNA topoisomerase +EC 5.6.2.2: DNA topoisomerase (ATP-hydrolyzing) +EC 5.6.2.3: DNA 5'-3' helicase +EC 5.6.2.4: DNA 3'-5' helicase + +== EC 5.99: Other Isomerases == + +=== EC 5.99.1: Sole sub-subclass for isomerases that do not belong in the other subclasses === +EC 5.99.1.1: thiocyanate isomerase +EC 5.99.1.2: Now EC 5.6.2.1, DNA topoisomerase +EC 5.99.1.3: Now EC 5.6.2.2, DNA topoisomerase (ATP-hydrolysing) +EC 5.99.1.4: 2-hydroxychromene-2-carboxylate isomerase + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-0.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-0.md new file mode 100644 index 000000000..88460d43b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-0.md @@ -0,0 +1,161 @@ +--- +title: "List of EC numbers (EC 6)" +chunk: 1/2 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:12.205809+00:00" +instance: "kb-cron" +--- + +This list contains a list of EC numbers for the sixth group, EC 6, ligases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. + +== EC 6.1: Forming Carbon-Oxygen Bonds == + +=== EC 6.1.1: Ligases Forming Aminoacyl-tRNA and Related Compounds (Aminoacyl tRNA synthetase) === +EC 6.1.1.1: tyrosine—tRNA ligase +EC 6.1.1.2: tryptophan—tRNA ligase +EC 6.1.1.3: threonine—tRNA ligase +EC 6.1.1.4: leucine—tRNA ligase +EC 6.1.1.5: isoleucine—tRNA ligase +EC 6.1.1.6: +lysine—tRNA ligase +EC 6.1.1.7: alanine—tRNA ligase +EC 6.1.1.8: Deleted +EC 6.1.1.9: valine—tRNA ligase +EC 6.1.1.10: methionine—tRNA ligase +EC 6.1.1.11: serine—tRNA ligase +EC 6.1.1.12: aspartate—tRNA ligase +EC 6.1.1.13: D-alanine—poly(phosphoribitol) ligase +EC 6.1.1.14: glycine—tRNA ligase +EC 6.1.1.15: proline—tRNA ligase +EC 6.1.1.16: cysteine—tRNA ligase +EC 6.1.1.17: glutamate—tRNA ligase +EC 6.1.1.18: glutamine—tRNA ligase +EC 6.1.1.19: arginine—tRNA ligase +EC 6.1.1.20: phenylalanine—tRNA ligase +EC 6.1.1.21: histidine—tRNA ligase +EC 6.1.1.22: asparagine—tRNA ligase +EC 6.1.1.23: aspartate—tRNAAsn ligase +EC 6.1.1.24: glutamate—tRNAGln ligase +EC 6.1.1.25: The tRNAPyl is now known only to be charged with pyrrolysine (cf. EC 6.1.1.26) +EC 6.1.1.26: pyrrolysine—tRNAPyl ligase +EC 6.1.1.27: O-phospho-L-serine—tRNA ligase +EC 6.1.1.28: "proline/cysteine—tRNA ligase". Later published work having demonstrated that this was not a genuine enzyme, EC 6.1.1.28 was withdrawn at the public-review stage before being made official. + +=== EC 6.1.2: Acid—alcohol ligases (ester synthases) === +EC 6.1.2.1: D-alanine—(R)-lactate ligase +EC 6.1.2.2: nebramycin 5′ synthase + +=== EC 6.1.3: Cyclo-ligases === +EC 6.1.3.1: olefin β-lactone synthetase + +== EC 6.2: Forming Carbon-Sulfur Bonds == + +=== EC 6.2.1: Acid-Thiol Ligases === +EC 6.2.1.1: acetate—CoA ligase +EC 6.2.1.2: medium-chain acyl-CoA ligase +EC 6.2.1.3: long-chain-fatty-acid—CoA ligase +EC 6.2.1.4: succinate—CoA ligase (GDP-forming) +EC 6.2.1.5: succinate—CoA ligase (ADP-forming) +EC 6.2.1.6: glutarate—CoA ligase +EC 6.2.1.7: cholate—CoA ligase +EC 6.2.1.8: oxalate—CoA ligase +EC 6.2.1.9: malate—CoA ligase +EC 6.2.1.10: carboxylic acid—CoA ligase (GDP-forming) +EC 6.2.1.11: biotin—CoA ligase +EC 6.2.1.12: 4-coumarate—CoA ligase +EC 6.2.1.13: acetate—CoA ligase (ADP-forming) +EC 6.2.1.14: 6-carboxyhexanoate—CoA ligase +EC 6.2.1.15: arachidonate—CoA ligase +EC 6.2.1.16: acetoacetate—CoA ligase +EC 6.2.1.17: propionate—CoA ligase +EC 6.2.1.18: citrate—CoA ligase +EC 6.2.1.19: long-chain-fatty-acid—protein ligase +EC 6.2.1.20: long-chain-fatty-acid—[acyl-carrier-protein] ligase +EC 6.2.1.21: Activity covered by EC 6.2.1.30, phenylacetate—CoA ligase +EC 6.2.1.22: [citrate (pro-3S)-lyase] ligase +EC 6.2.1.23: dicarboxylate—CoA ligase +EC 6.2.1.24: phytanate—CoA ligase +EC 6.2.1.25: benzoate—CoA ligase +EC 6.2.1.26: o-succinylbenzoate—CoA ligase +EC 6.2.1.27: 4-hydroxybenzoate—CoA ligase +EC 6.2.1.28: 3α,7α-dihydroxy-5β-cholestanate—CoA ligase +EC 6.2.1.29: Deleted, identical to EC 6.2.1.7, cholate—CoA ligase +EC 6.2.1.30: phenylacetate—CoA ligase +EC 6.2.1.31: 2-furoate—CoA ligase +EC 6.2.1.32: anthranilate—CoA ligase +EC 6.2.1.33: 4-chlorobenzoate—CoA ligase +EC 6.2.1.34: trans-feruloyl—CoA synthase +EC 6.2.1.35: acetate—[acyl-carrier protein] ligase +EC 6.2.1.36: 3-hydroxypropionyl-CoA synthase +EC 6.2.1.37: 3-hydroxybenzoate—CoA ligase +EC 6.2.1.38: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase +EC 6.2.1.39: [butirosin acyl-carrier protein]—L-glutamate ligase +EC 6.2.1.40: 4-hydroxybutyrate—CoA ligase (AMP-forming) +EC 6.2.1.41: 3-[(3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl]propanoate—CoA ligase +EC 6.2.1.42: 3-oxocholest-4-en-26-oate—CoA ligase +EC 6.2.1.43: 2-hydroxy-7-methoxy-5-methyl-1-naphthoate—CoA ligase +EC 6.2.1.44: 3-(methylthio)propionyl—CoA ligase +EC 6.2.1.45: E1 ubiquitin-activating enzyme +EC 6.2.1.46: L-allo-isoleucine—holo-[CmaA peptidyl-carrier protein] ligase +EC 6.2.1.47: medium-chain-fatty-acid—[acyl-carrier-protein] ligase +EC 6.2.1.48: carnitine—CoA ligase +EC 6.2.1.49: long-chain fatty acid adenylyltransferase FadD28 +EC 6.2.1.50: 4-hydroxybenzoate adenylyltransferase FadD22 +EC 6.2.1.51: 4-hydroxyphenylalkanoate adenylyltransferase FadD29 +EC 6.2.1.52: L-firefly luciferin—CoA ligase +EC 6.2.1.53: L-proline—[L-prolyl-carrier protein] ligase +EC 6.2.1.54: D-alanine—[D-alanyl-carrier protein] ligase +EC 6.2.1.55: E1 SAMP-activating enzyme +EC 6.2.1.56: 4-hydroxybutyrate—CoA ligase (ADP-forming) +EC 6.2.1.57: long-chain fatty acid adenylase/transferase FadD23 +EC 6.2.1.58: isophthalate—CoA ligase +EC 6.2.1.59: long-chain fatty acid adenylase/transferase FadD26 +EC 6.2.1.60: marinolic acid—CoA ligase +EC 6.2.1.61: salicylate—[aryl-carrier protein] ligase +EC 6.2.1.62: 3,4-dihydroxybenzoate—[aryl-carrier protein] ligase +EC 6.2.1.63: L-arginine—[L-arginyl-carrier protein] ligase +EC 6.2.1.64: E1 NEDD8-activating enzyme +EC 6.2.1.65: salicylate—CoA ligase +EC 6.2.1.66: glyine—[glycyl-carrier protein] ligase +EC 6.2.1.67: L-alanine—[L-alanyl-carrier protein] ligase +EC 6.2.1.68: L-glutamate—[L-glutamyl-carrier protein] ligase +EC 6.2.1.69: L-cysteine—[L-cysteinyl-carrier protein] ligase +EC 6.2.1.70: L-threonine—[L-threonyl-carrier protein] ligase +EC 6.2.1.71: 2,3-dihydroxybenzoate—[aryl-carrier protein] ligase +EC 6.2.1.72: L-serine—[L-seryl-carrier protein] ligase +EC 6.2.1.73: L-tryptophan—[L-tryptophyl-carrier protein] ligase +EC 6.2.1.74: 3-amino-5-hydroxybenzoate—[acyl-carrier protein] ligase +EC 6.2.1.75: indoleacetate—CoA ligase +EC 6.2.1.76: malonate—CoA ligase * + +=== EC 6.2.2: Amide—thiol ligases === +EC 6.2.2.1: thioglycine synthase +EC 6.2.2.2: oxazoline synthase +EC 6.2.2.3: thiazoline synthase + +== EC 6.3: Forming Carbon-Nitrogen Bonds == + +=== EC 6.3.1: Acid—Ammonia (or Amine) Ligases (Amide Synthases) === +EC 6.3.1.1: aspartate—ammonia ligase +EC 6.3.1.2: glutamine synthetase +EC 6.3.1.3: Now EC 6.3.4.13, phosphoribosylamine—glycine ligase +EC 6.3.1.4: aspartate—ammonia ligase (ADP-forming) +EC 6.3.1.5: NAD+ synthase +EC 6.3.1.6: glutamate—ethylamine ligase +EC 6.3.1.7: 4-methyleneglutamate—ammonia ligase +EC 6.3.1.8: glutathionylspermidine synthase +EC 6.3.1.9: trypanothione synthase +EC 6.3.1.10: adenosylcobinamide-phosphate synthase +EC 6.3.1.11: glutamate—putrescine ligase +EC 6.3.1.12: D-aspartate ligase +EC 6.3.1.13: L-cysteine:1D-myo-inositol 2-amino-2-deoxy-α-D-glucopyranoside ligase +EC 6.3.1.14: diphthine—ammonia ligase +EC 6.3.1.15: 8-demethylnovobiocic acid synthase +EC 6.3.1.16: [[The enzyme was discovered at the public-review stage to have been misclassified and so was withdrawn. See EC 6.3.3.6, carbapenam-3-carboxylate synthase]] +EC 6.3.1.17: β-citrylglutamate synthase +EC 6.3.1.18: γ-glutamylanilide synthase +EC 6.3.1.19: prokaryotic ubiquitin-like protein ligase +EC 6.3.1.20: lipoate—protein ligase +EC 6.3.1.21: phosphoribosylglycinamide formyltransferase 2 \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-1.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-1.md new file mode 100644 index 000000000..02544dded --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)-1.md @@ -0,0 +1,164 @@ +--- +title: "List of EC numbers (EC 6)" +chunk: 2/2 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_6)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:12.205809+00:00" +instance: "kb-cron" +--- + +=== EC 6.3.2: Acid—Amino-Acid Ligases (Peptide Synthases) === +EC 6.3.2.1: pantoate—β-alanine ligase (AMP-forming) +EC 6.3.2.2: glutamate—cysteine ligase +EC 6.3.2.3: glutathione synthase +EC 6.3.2.4: D-alanine—D-alanine ligase +EC 6.3.2.5: phosphopantothenate—cysteine ligase (CTP) +EC 6.3.2.6: phosphoribosylaminoimidazolesuccinocarboxamide synthase +EC 6.3.2.7: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—L-lysine ligase +EC 6.3.2.8: UDP-N-acetylmuramate—L-alanine ligase +EC 6.3.2.9: UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase +EC 6.3.2.10: UDP-N-acetylmuramoyl-tripeptide—D-alanyl-D-alanine ligase +EC 6.3.2.11: carnosine synthase +EC 6.3.2.12: dihydrofolate synthase +EC 6.3.2.13: +UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—2,6-diaminopimelate ligase +EC 6.3.2.14: enterobactin synthase +EC 6.3.2.15: Deleted, The activity observed is due to EC 6.3.2.10, UDP-N-acetylmuramoyl-tripeptideD-alanyl-D-alanine ligase +EC 6.3.2.16: D-alanine—alanyl-poly(glycerolphosphate) ligase +EC 6.3.2.17: tetrahydrofolate synthase +EC 6.3.2.18: γ-glutamylhistamine synthase +EC 6.3.2.19: The ubiquitinylation process is now known to be performed by several enzymes in sequence, starting with EC 6.2.1.45 (ubiquitin-activating enzyme E1) and followed by several transfer reactions, including those of EC 2.3.2.23 (E2 ubiquitin-conjugating enzyme) and EC 2.3.2.27 (RING-type E3 ubiquitin transferase) +EC 6.3.2.20: indoleacetate—lysine synthetase +EC 6.3.2.21: [[The reaction is performed by the sequential action of EC 6.2.1.45 (ubiquitin-activating enzyme E1), several ubiquitin transferases and finally by EC 2.3.2.27 (ubiquitin transferase RING E3 (calmodulin-selective))|The reaction is performed by the sequential action of EC 6.2.1.45 (ubiquitin-activating enzyme E1), several ubiquitin transferases and finally by EC 2.3.2.27 [ubiquitin transferase RING E3 (calmodulin-selective)]]] +EC 6.3.2.22: Now EC 6.3.1.14, diphthine—ammonia ligase. +EC 6.3.2.23: homoglutathione synthase +EC 6.3.2.24: tyrosine—arginine ligase +EC 6.3.2.25: tubulin—tyrosine ligase +EC 6.3.2.26: N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase +EC 6.3.2.27: [[The activity is covered by two independent enzymes, EC 6.3.2.38 N^2-citryl-N^6-acetyl-N^6-hydroxylysine synthase, and EC 6.3.2.39, aerobactin synthase|The activity is covered by two independent enzymes, EC 6.3.2.38 N2-citryl-N6-acetyl-N6-hydroxylysine synthase, and EC 6.3.2.39, aerobactin synthase]] +EC 6.3.2.28: Now EC 6.3.2.49, L-alanine-L-anticapsin ligase +EC 6.3.2.29: cyanophycin synthase (L-aspartate-adding) +EC 6.3.2.30: cyanophycin synthase (L-arginine-adding) +EC 6.3.2.31: coenzyme F420-0:L-glutamate ligase +EC 6.3.2.32: coenzyme γ-F420-2:α-L-glutamate ligase +EC 6.3.2.33: tetrahydrosarcinapterin synthase +EC 6.3.2.34: coenzyme F420-0:L-glutamate ligase +EC 6.3.2.35: D-alanine—D-serine ligase +EC 6.3.2.36: 4-phosphopantoate—β-alanine ligase +EC 6.3.2.37: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate—D-lysine ligase +EC 6.3.2.38: N2-citryl-N6-acetyl-N6-hydroxylysine synthase +EC 6.3.2.39: aerobactin synthase +EC 6.3.2.40: cyclopeptine synthase +EC 6.3.2.41: N-acetylaspartylglutamate synthase +EC 6.3.2.42: N-acetylaspartylglutamylglutamate synthase +EC 6.3.2.43: [amino-group carrier protein]—L-2-aminoadipate ligase +EC 6.3.2.44: pantoate—β-alanine ligase (ADP-forming) +EC 6.3.2.45: UDP-N-acetylmuramate—L-alanyl-γ-D-glutamyl-meso-2,6-diaminoheptanedioate ligase +EC 6.3.2.46: fumarate—(S)-2,3-diaminopropanoate ligase +EC 6.3.2.47: dapdiamide synthase +EC 6.3.2.48: L-arginine-specific L-amino acid ligase +EC 6.3.2.49: L-alanine—L-anticapsin ligase +EC 6.3.2.50: tenuazonic acid synthetase +EC 6.3.2.51: phosphopantothenate—cysteine ligase (ATP) +EC 6.3.2.52: jasmonoyl—L-amino acid ligase +EC 6.3.2.53: UDP-N-acetylmuramoyl-L-alanine—L-glutamate ligase +EC 6.3.2.54: L-2,3-diaminopropanoate—citrate ligase +EC 6.3.2.55: 2-[(L-alanin-3-ylcarbamoyl)methyl]-3-(2-aminoethylcarbamoyl)-2-hydroxypropanoate synthase +EC 6.3.2.56: staphyloferrin B synthase +EC 6.3.2.57: staphyloferrin A synthase +EC 6.3.2.58: D-ornithine—citrate ligase +EC 6.3.2.59: 3-methyl-D-ornithine—L-lysine ligase +EC 6.3.2.60: glutamate—[amino group carrier protein] ligase +EC 6.3.2.61: tubulin-glutamate ligase +EC 6.3.2.62: β-tubulin-glutamate ligase + +=== EC 6.3.3: Cyclo-Ligases === +EC 6.3.3.1: phosphoribosylformylglycinamidine cyclo-ligase +EC 6.3.3.2: 5-formyltetrahydrofolate cyclo-ligase +EC 6.3.3.3: dethiobiotin synthase +EC 6.3.3.4: (carboxyethyl)arginine β-lactam-synthase +EC 6.3.3.5: O-ureido-D-serine cyclo-ligase +EC 6.3.3.6: carbapenam-3-carboxylate synthase +EC 6.3.3.7: Ni-sirohydrochlorin a,c-diamide reductive cyclase + +=== EC 6.3.4: Other Carbon-Nitrogen Ligases === +EC 6.3.4.1: Now included in EC 6.3.5.2, GMP synthase (glutamine-hydrolysing) +EC 6.3.4.2: CTP synthase (glutamine hydrolysing) +EC 6.3.4.3: formate—tetrahydrofolate ligase +EC 6.3.4.4: adenylosuccinate synthase +EC 6.3.4.5: argininosuccinate synthase +EC 6.3.4.6: urea carboxylase +EC 6.3.4.7: ribose-5-phosphate—ammonia ligase +EC 6.3.4.8: imidazoleacetate—phosphoribosyldiphosphate ligase +EC 6.3.4.9: biotin—[methylmalonyl-CoA-carboxytransferase] ligase +EC 6.3.4.10: biotin—[methylmalonyl-CoA-carboxytransferase] ligase +EC 6.3.4.11: biotin—[methylcrotonoyl-CoA-carboxylase] ligase +EC 6.3.4.12: glutamate—methylamine ligase +EC 6.3.4.13: phosphoribosylamine—glycine ligase +EC 6.3.4.14: biotin carboxylase +EC 6.3.4.15: biotin—[biotin carboxyl-carrier protein] ligase +EC 6.3.4.16: carbamoyl-phosphate synthase (ammonia) +EC 6.3.4.17: formate—dihydrofolate ligase +EC 6.3.4.18: 5-(carboxyamino)imidazole ribonucleotide synthase +EC 6.3.4.19: tRNAIle-lysidine synthase +EC 6.3.4.20: 7-cyano-7-deazaguanine synthase +EC 6.3.4.21: nicotinate phosphoribosyltransferase +EC 6.3.4.22: tRNAIle2-agmatinylcytidine synthase +EC 6.3.4.23: formate—phosphoribosylaminoimidazolecarboxamide ligase +EC 6.3.4.24: tyramine—L-glutamate ligase +EC 6.3.4.25: 2-amino-2′-deoxyadenylo-succinate synthase + +=== EC 6.3.5: Carbon-nitrogen ligases with glutamine as amido-N-donor === +EC 6.3.5.1: NAD+ synthase (glutamine-hydrolysing) +EC 6.3.5.2: GMP synthase (glutamine-hydrolysing) +EC 6.3.5.3: phosphoribosylformylglycinamidine synthase +EC 6.3.5.4: asparagine synthase (glutamine-hydrolysing) +EC 6.3.5.5: carbamoyl-phosphate synthase (glutamine-hydrolysing) +EC 6.3.5.6: asparaginyl-tRNA synthase (glutamine-hydrolysing) +EC 6.3.5.7: glutaminyl-tRNA synthase (glutamine-hydrolysing) +EC 6.3.5.8: Now EC 2.6.1.85, aminodeoxychorismate synthase. As ATP is not hydrolysed during the reaction, the classification of the enzyme as a ligase was incorrect +EC 6.3.5.9: hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) +EC 6.3.5.10: adenosylcobyric acid synthase (glutamine-hydrolysing) +EC 6.3.5.11: cobyrinate a,c-diamide synthase +EC 6.3.5.12: Ni-sirohydrochlorin a,c-diamide synthase +EC 6.3.5.13: lipid II isoglutaminyl synthase (glutamine-hydrolysing) + +== EC 6.4: Forming Carbon-Carbon Bonds == + +=== EC 6.4.1: Ligases that form carbon-carbon bonds (only sub-subclass identified to date) === +EC 6.4.1.1: pyruvate carboxylase +EC 6.4.1.2: acetyl-CoA carboxylase +EC 6.4.1.3: propionyl-CoA carboxylase +EC 6.4.1.4: methylcrotonoyl-CoA carboxylase +EC 6.4.1.5: geranoyl-CoA carboxylase +EC 6.4.1.6: acetone carboxylase +EC 6.4.1.7: 2-oxoglutarate carboxylase +EC 6.4.1.8: acetophenone carboxylase +EC 6.4.1.9: coenzyme F430 synthetase + +== EC 6.5: Forming Phosphoric Ester Bonds == + +=== EC 6.5.1: Ligases that form phosphoric-ester bonds (only sub-subclass identified to date) === +EC 6.5.1.1: DNA ligase (ATP) +EC 6.5.1.2: DNA ligase (NAD+) +EC 6.5.1.3: RNA ligase (ATP) +EC 6.5.1.4: RNA 3′-terminal-phosphate cyclase (ATP) +EC 6.5.1.5: RNA 3′-terminal-phosphate cyclase (GTP) +EC 6.5.1.6: DNA ligase (ATP or NAD+) +EC 6.5.1.7: DNA ligase (ATP, ADP or GTP) +EC 6.5.1.8: 3′-phosphate/5′-hydroxy nucleic acid ligase +EC 6.5.1.9: cyclic 2,3-diphosphoglycerate synthase + +== EC 6.6: Forming Nitrogen-Metal Bonds == + +=== EC 6.6.1: Forming Coordination Complexes === +EC 6.6.1.1: magnesium chelatase +EC 6.6.1.2: cobaltochelatase + +== EC 6.7: Forming nitrogen-nitrogen bonds == + +=== EC 6.7.1: Forming diazo bonds === +EC 6.7.1.1: 3-amino-2-hydroxy-4-methoxybenzoate + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_7)-0.md b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_7)-0.md new file mode 100644 index 000000000..b31299d50 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_EC_numbers_(EC_7)-0.md @@ -0,0 +1,158 @@ +--- +title: "List of EC numbers (EC 7)" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_EC_numbers_(EC_7)" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:13.488832+00:00" +instance: "kb-cron" +--- + +This list contains a list of sub-classes for the seventh group of Enzyme Commission numbers, EC 7, translocases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. All official information is tabulated at the website of the committee. The database is developed and maintained by Andrew McDonald. + + +== EC 7.1: Catalysing the translocation of hydrons == +NOTE: Hydron is a generic term that includes all isotopes of H+, i.e. not only 1H+ but also 2H+ (D+) and 3H+ (T+). + + +=== EC 7.1.1: Linked to oxidoreductase reactions === +EC 7.1.1.1: proton-translocating NAD(P)+ transhydrogenase +EC 7.1.1.2: NADH:ubiquinone reductase (H+-translocating) +EC 7.1.1.3: ubiquinol oxidase (H+-transporting) +EC 7.1.1.4: caldariellaquinol oxidase (H+-transporting) +EC 7.1.1.5: menaquinol oxidase (H+-transporting) +EC 7.1.1.6: plastoquinol—plastocyanin reductase +EC 7.1.1.7: quinol oxidase (electrogenic, proton-motive force generating) +EC 7.1.1.8: quinol—cytochrome-c reductase +EC 7.1.1.9: cytochrome-c oxidase +EC 7.1.1.10: ferredoxin—quinone oxidoreductase (H+-translocating) +EC 7.1.1.11: ferredoxin—NAD+ oxidoreductase (H+-transporting) + + +=== EC 7.1.2: Linked to the hydrolysis of a nucleoside triphosphate === +EC 7.1.2.1: P-type H+-exporting transporter +EC 7.1.2.2: H+-transporting two-sector ATPase + + +=== EC 7.1.3: Linked to the hydrolysis of diphosphate === +EC 7.1.3.1: H+-exporting diphosphatase +EC 7.1.3.2: Na+-exporting diphosphatase + + +== EC 7.2: catalysing the translocation of inorganic cations and their chelates == + + +=== EC 7.2.1: Linked to oxidoreductase reactions === +EC 7.2.1.1: NADH:ubiquinone reductase (NAD+-transporting) +EC 7.2.1.2: ferredoxin—NAD+ oxidoreductase (NAD+-transporting) +EC 7.2.1.3: ascorbate ferrireductase (transmembrane) + + +=== EC 7.2.2: Linked to the hydrolysis of a nucleoside triphosphate === +EC 7.2.2.1: Na+-transporting two-sector ATPase +EC 7.2.2.2: ABC-type Cd2+ transporter +EC 7.2.2.3: P-type Na+ transporter +EC 7.2.2.4: ABC-type Na+ transporter +EC 7.2.2.5: ABC-type Mn2+ transporter +EC 7.2.2.6: P-type K+ transporter +EC 7.2.2.7: ABC-type Fe2+ transporter +EC 7.2.2.8: P-type Cu+ transporter +EC 7.2.2.9: P-type Cu2+ transporter +EC 7.2.2.10: P-type Ca2+ transporter +EC 7.2.2.11: ABC-type Ni2+ transporter +EC 7.2.2.12: P-type Zn2+ transporter +EC 7.2.2.13: Na+/K+-exchanging ATPase +EC 7.2.2.14: P-type Mg2+ transporter +EC 7.2.2.15: P-type Ag+ transporter +EC 7.2.2.16: ABC-type ferric hydroxamate transporter +EC 7.2.2.17: ABC-type ferric enterobactin transporter +EC 7.2.2.18: ABC-type ferric citrate transporter +EC 7.2.2.19: H+/K+-exchanging ATPase +EC 7.2.2.20: ABC-type Zn2+ transporter +EC 7.2.2.21: Cd2+-exporting ATPase +EC 7.2.2.22: P-type Mn2+ transporter + + +=== EC 7.2.4: Linked to decarboxylation === +EC 7.2.4.1: carboxybiotin decarboxylase +EC 7.2.4.2: oxaloacetate decarboxylase (Na+ extruding) +EC 7.2.4.3: (S)-methylmalonyl-CoA decarboxylase (sodium-transporting) +EC 7.2.4.4: biotin-dependent malonate decarboxylase +EC 7.2.4.5: glutaconyl-CoA decarboxylase * + + +== EC 7.3: Catalysing the translocation of inorganic anions == + + +=== EC 7.3.2: Linked to the hydrolysis of a nucleoside triphosphate === +EC 7.3.2.1: ABC-type phosphate transporter +EC 7.3.2.2: ABC-type phosphonate transporter +EC 7.3.2.3: ABC-type sulfate transporter +EC 7.3.2.4: ABC-type nitrate transporter +EC 7.3.2.5: ABC-type molybdate transporter +EC 7.3.2.6: ABC-type tungstate transporter +EC 7.3.2.7: arsenite-transporting ATPase + + +== EC 7.4: Catalysing the translocation of amino acids and peptides == + + +=== EC 7.4.2: Linked to the hydrolysis of a nucleoside triphosphate === +EC 7.4.2.1: ABC-type polar-amino-acid transporter +EC 7.4.2.2: ABC-type nonpolar-amino-acid transporter +EC 7.4.2.3: mitochondrial protein-transporting ATPase +EC 7.4.2.4: chloroplast protein-transporting ATPase +EC 7.4.2.5: bacterial ABC-type protein transporter +EC 7.4.2.6: ABC-type oligopeptide transporter +EC 7.4.2.7: ABC-type α-factor-pheromone transporter +EC 7.4.2.8: protein-secreting ATPase +EC 7.4.2.9: ABC-type dipeptide transporter +EC 7.4.2.10: ABC-type glutathione transporter +EC 7.4.2.11: ABC-type methionine transporter +EC 7.4.2.12: ABC-type cystine transporter +EC 7.4.2.13: ABC-type tyrosine transporter +EC 7.4.2.14: ABC-type antigen peptide transporter + + +== EC 7.5: Catalysing the translocation of carbohydrates and their derivatives == + + +=== EC 7.5.2: Linked to the hydrolysis of a nucleoside triphosphate === +EC 7.5.2.1: ABC-type maltose transporter +EC 7.5.2.2: ABC-type oligosaccharide transporter +EC 7.5.2.3: ABC-type β-glucan transporter +EC 7.5.2.4: ABC-type teichoic-acid transporter +EC 7.5.2.5: ABC-type lipopolysaccharide transporter +EC 7.5.2.6: ABC-type lipid A-core oligosaccharide transporter +EC 7.5.2.7: ABC-type D-ribose transporter +EC 7.5.2.8: ABC-type D-allose transporter +EC 7.5.2.9: ABC-type D-galactofuranose transporter +EC 7.5.2.10: ABC-type D-xylose transporter +EC 7.5.2.11: ABC-type D-galactose transporter +EC 7.5.2.12: ABC-type L-arabinose transporter +EC 7.5.2.13: ABC-type D-xylose/L-arabinose transporter + + +== EC 7.6: Catalysing the translocation of other compounds == + + +=== EC 7.6.2: Linked to the hydrolysis of a nucleoside triphosphate === +EC 7.6.2.1: P-type phospholipid transporter +EC 7.6.2.2: ABC-type xenobiotic transporter +EC 7.6.2.3: ABC-type glutathione-S-conjugate transporter +EC 7.6.2.4: ABC-type fatty-acyl-CoA transporter +EC 7.6.2.5: ABC-type heme transporter +EC 7.6.2.6: ABC-type guanine transporter +EC 7.6.2.7: ABC-type taurine transporter +EC 7.6.2.8: ABC-type vitamin B12 transporter +EC 7.6.2.9: ABC-type quaternary amine transporter +EC 7.6.2.10: ABC-type glycerol 3-phosphate transporter +EC 7.6.2.11: ABC-type polyamine transporter +EC 7.6.2.12: ABC-type capsular-polysaccharide transporter +EC 7.6.2.13: ABC-type autoinducer-2 transporter +EC 7.6.2.14: ABC-type aliphatic sulfonate transporter +EC 7.6.2.15: ABC-type thiamine transporter +EC 7.6.2.16: ABC-type putrescine transporter + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Falconiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Falconiformes_by_population-0.md new file mode 100644 index 000000000..f3c51f0bb --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Falconiformes_by_population-0.md @@ -0,0 +1,31 @@ +--- +title: "List of Falconiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Falconiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:32.455872+00:00" +instance: "kb-cron" +--- + +This is a list of Falconiformes species by global population. While members of Falconiformes were once classified with the hawks, eagles, vultures, and kites of order Accipitriformes, recent genetic analysis indicates they are not close relatives of these birds. Version 15.1 of the IOC World Bird List describes 65 species within Falconiformes, two of which are extinct. As of December 2025, BirdLife International has assessed 64 of these species (excepting rock kestrel). While not all of these species have had their populations quantified, species without estimates are also listed below in a separate table. +While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +There are two species listed as members of Falconiformes which are extinct. They are as follows: + +Guadalupe caracara (Caracara lutosa) - last recorded in 1903. +Réunion kestrel (Falco duboisi) - species is mentioned by early explorers, but went extinct sometime after 1674. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Galliformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Galliformes_by_population-0.md new file mode 100644 index 000000000..82a45f1bc --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Galliformes_by_population-0.md @@ -0,0 +1,36 @@ +--- +title: "List of Galliformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Galliformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:34.023513+00:00" +instance: "kb-cron" +--- + +This is a list of Galliformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +Not all Galliformes have had their populations quantified, but species without population estimates are included in a secondary table below. +The IOC World Bird List (version 15.1) recognizes 307 species of Galliformes, one of which is extinct. As of January 2026, the IUCN has assessed 303 of these species (excepting red grouse, chestnut-headed chachalaca, Yungas guan, and Dulit partridge). +This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +One member of Galliformes is extinct: + +New Zealand quail (Coturnix novaezelandiae) - last individual died in 1875. + + +== Species by global population == + + +== Species without population estimates == + + +== Populations of domestic Galliformes == +Note that domestic subspecies are not evaluated by the IUCN. + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Gaviiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Gaviiformes_by_population-0.md new file mode 100644 index 000000000..8dbbfc916 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Gaviiformes_by_population-0.md @@ -0,0 +1,24 @@ +--- +title: "List of Gaviiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Gaviiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:35.196986+00:00" +instance: "kb-cron" +--- + +This is a list of Gaviiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list follows IUCN classifications for species names. Where IUCN classifications differ from other ornithological authorities, alternative names are noted. The IOC World Bird List (version 15.1) recognizes 5 species of Gaviiformes. IUCN/BirdLife International have assessed the populations of all members of this order. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Gruiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Gruiformes_by_population-0.md new file mode 100644 index 000000000..aba97789f --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Gruiformes_by_population-0.md @@ -0,0 +1,52 @@ +--- +title: "List of Gruiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Gruiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:36.548865+00:00" +instance: "kb-cron" +--- + +This is a list of Gruiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +Not all Gruiformes have had their numbers quantified, but species without population estimates are included in a secondary table below. +The IOC World Bird List (version 15.1) recognizes 190 species of Gruiformes, 21 of which are extinct. Species status within Gruiformes is particularly unresolved compared to other orders. As of December 2025, IOC lists six species which are considered subspecies by IUCN/BirdLife International. Similarly, IUCN/BirdLife International list four species which still have subspecies status in IOC taxonomies. See 'Notes' column of included tables for more information on these taxonomic disputes. +This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +Several species included as members of Gruiformes are extinct: + +Réunion rail (Dryolimnas augusti) - last observed circa 1670. +Hawkin's rail (Diaphorapteryx hawkinsi) - went extinct in the latter half of 19th century. +Chatham Islands rail (Cabalus modestus) - last observed between 1895-1900. +Bar-winged rail (Hypotaenidia poeciloptera) - last observed in 1890. +Dieffenbach's rail (Hypotaenidia dieffenbachii) - last observed in 1840. +Tahiti rail (Hypotaenidia pacifica) - went extinct some time during the 1930s. +Wake Island rail (Hypotaenidia wakensis) - last observed in 1945. +Tristan moorhen (Gallinula nesiotis) - last observed in 1861. +Mascarene coot (Fulica newtonii) - extinct since early 1700s. +White swamphen (Porphyrio albus) - extinct by 1834. +Marquesan swamphen (Porphyrio paepae) - extinct by 1937. +North island takahē (Porphyrio mantelli) - last observed in 1894. +Ascension crake (Mundia elpenor) - only record comes from 1656. Extinct by 1700. +St. Helena rail (Aphanocrex podarces) - extinct by end of 16th century. +St. Helena crake (Zapornia astrictocarpus) - extinct soon after discovery of St. Helena, ca. 1502. +Kosrae crake (Zapornia monasa) - last observed in 1828; extinct by end of 19th century. +Miller's rail or Tahiti crake (Zapornia nigra) - last observed in 1784. +Hawaiian rail (Zapornia sandwichensis) - extinct by end of 1860s. +Laysan rail (Zapornia palmeri) - extinct in 1944. +Red rail (Aphanapteryx bonasia) - extinct by end of 17th century. +Rodrigues rail (Erythromachus leguati) - last recorded in 1726, extinct by 1761. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Musophagiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Musophagiformes_by_population-0.md new file mode 100644 index 000000000..e6ecc1617 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Musophagiformes_by_population-0.md @@ -0,0 +1,23 @@ +--- +title: "List of Musophagiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Musophagiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:38.414195+00:00" +instance: "kb-cron" +--- + +This is a list of Musophagiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. This list is not comprehensive, as not all species of this order has had their global populations estimated. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_OBO_Foundry_ontologies-0.md b/data/en.wikipedia.org/wiki/List_of_OBO_Foundry_ontologies-0.md new file mode 100644 index 000000000..e1539161a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_OBO_Foundry_ontologies-0.md @@ -0,0 +1,17 @@ +--- +title: "List of OBO Foundry ontologies" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_OBO_Foundry_ontologies" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:31.492650+00:00" +instance: "kb-cron" +--- + +This is a list of ontologies that are part of the OBO Foundry as of January 2020. + + +== OBO Foundry ontologies == + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Otidiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Otidiformes_by_population-0.md new file mode 100644 index 000000000..3eae2e934 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Otidiformes_by_population-0.md @@ -0,0 +1,28 @@ +--- +title: "List of Otidiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Otidiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:39.713652+00:00" +instance: "kb-cron" +--- + +This is a list of Otidiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The IOC World Bird List (version 15.1) recognizes 26 species of Otidiformes. IUCN/BirdLife International have assessed all members of this order, with population estimates provided for 11 (42%) species. +This list follows IUCN classifications for species names. Where IUCN classifications differ from other ornithological authorities, alternative names are noted. While not all of these species have had their populations quantified, species without estimates are also listed below in a separate table. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Passeriformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Passeriformes_by_population-0.md new file mode 100644 index 000000000..3c79177d4 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Passeriformes_by_population-0.md @@ -0,0 +1,27 @@ +--- +title: "List of Passeriformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Passeriformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:41.096536+00:00" +instance: "kb-cron" +--- + +This is a list of Passeriforme species by global population. While numbers are estimates, they have been made by the experts in their fields. +Passeriformes is the taxonomic order to which the perching birds belong. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Pelecaniformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Pelecaniformes_by_population-0.md new file mode 100644 index 000000000..ee27d09c0 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Pelecaniformes_by_population-0.md @@ -0,0 +1,36 @@ +--- +title: "List of Pelecaniformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Pelecaniformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:42.420582+00:00" +instance: "kb-cron" +--- + +This is a list of Pelecaniformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The IOC World Bird List (version 15.1) recognizes 118 species of Pelecaniformes, seven of which are extinct. As of December 2025, IUCN/BirdLife International have assessed 111 of these species (excepting dimorphic egret, splits from striated heron, the split of cattle egret, and the extinct Ascension night heron). This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names/taxonomic statuses are noted. +Several species listed as members of Pelecaniformes are extinct: + +Réunion ibis (Threskiornis solitarius) - last seen in 1763. +New Zealand bittern (Botaurus novaezealandiae) - last seen in 1890. IUCN/BirdLife International place this bird in genus Ixobrychus. +Bermuda night heron (Nyctanassa carcinocatactes) - last seen in 1610. Likely extinct shortly afterward. +Ascension night heron (Nycticorax olsoni) - likely went extinct circa 1500. Not listed by IUCN/BirdLife International. +Réunion night heron (Nycticorax duboisi) - likely went extinct in early 1700s. +Mauritius night heron (Nycticorax mauritianus) - likely went extinct in early 1700s. +Rodrigues night heron (Nycticorax megacephalus) - likely extinct circa 1761. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Phoenicopteriformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Phoenicopteriformes_by_population-0.md new file mode 100644 index 000000000..ea490e706 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Phoenicopteriformes_by_population-0.md @@ -0,0 +1,25 @@ +--- +title: "List of Phoenicopteriformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Phoenicopteriformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:43.610694+00:00" +instance: "kb-cron" +--- + +This is a list of Phoenicopteriformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. + +This list follows IUCN guidance for species names. Where IUCN classifications differ from other ornithological authorities, alternative names are noted. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Piciformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Piciformes_by_population-0.md new file mode 100644 index 000000000..8ee544822 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Piciformes_by_population-0.md @@ -0,0 +1,31 @@ +--- +title: "List of Piciformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Piciformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:44.781583+00:00" +instance: "kb-cron" +--- + +This is a list of Piciformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is not comprehensive, as not all Piciformes have had their numbers quantified. +The IOC World Bird List (version 15.1) recognizes 448 species of Piciformes, one of which is extinct. This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +One member of Piciformes is extinct: + +Bermuda flicker (Colaptes oceanicus) - likely went extinct by mid-17th century. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Podicipediformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Podicipediformes_by_population-0.md new file mode 100644 index 000000000..8b65f5f57 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Podicipediformes_by_population-0.md @@ -0,0 +1,29 @@ +--- +title: "List of Podicipediformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Podicipediformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:45.969454+00:00" +instance: "kb-cron" +--- + +This is a list of Podicipediformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The IOC World Bird List (version 15.1) recognizes 23 species of Podicipediformes, three of which are extinct. IUCN/BirdLife International have assessed and quantified population sizes for 22 of these species, excepting tricolored grebe. Additionally, IUCN/BirdLife International recognize a split in silvery grebe into northern and southern species. +There are three species listed as members of Podicipediformes which are extinct. They are as follows: + +Alaotra grebe (Tachybaptus rufolavatus) - declared extinct in 2010, but last sighted in 1985. +Atitlán grebe (Podilymbus gigas) - species declared extinct in 1986, following rapid decline. +Colombian grebe (Podiceps andinus) - last confirmed sighting in 1977. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Procellariiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Procellariiformes_by_population-0.md new file mode 100644 index 000000000..776d939e2 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Procellariiformes_by_population-0.md @@ -0,0 +1,32 @@ +--- +title: "List of Procellariiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Procellariiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:47.483091+00:00" +instance: "kb-cron" +--- + +This is a list of Procellariiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The IOC World Bird List (version 15.1) recognizes 149 species of Procellariiformes, two of which are extinct. As of January 2026, IUCN/BirdLife International have assessed 144 members, and provided population estimates for 143 members of the order. While not all Procellariiformes have population estimates, species with unknown populations are listed in a secondary table below. +This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +Two members of Procellariiformes are extinct: + +St. Helena petrel, or large St. Helena petrel (Pterodroma rupinarum) - last seen in 1502. +Olson's petrel, or small St. Helena petrel (Bulweria bifax) - last seen in 1502. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Psittaciformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Psittaciformes_by_population-0.md new file mode 100644 index 000000000..874db2344 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Psittaciformes_by_population-0.md @@ -0,0 +1,45 @@ +--- +title: "List of Psittaciformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Psittaciformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:49.240678+00:00" +instance: "kb-cron" +--- + +This is a list of Psittaciformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is not comprehensive, as not all Psittaciformes have had their numbers quantified. All numbers, unless explicitly stated in the notes, only count individuals in the wild; IUCN does not consider species held in captivity in its population estimates. +The IOC World Bird List (version 15.1) recognizes 406 species of Psittaciformes, 14 of which are extinct. +This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +Some members of Psittaciformes are extinct: + +Norfolk Island kākā (Nestor productus) - extinct by 1850s due to habitat destruction and hunting. +Carolina parakeet (Conuropsis carolinensis) - last recorded in 1910. +Cuban macaw (Ara tricolor) - last reported in 1885; extinct due to hunting pressures. +Puerto Rican parakeet (Psittacara maugei) - extinct by 1892. Considered a subspecies of the Hispaniolan parakeet (P. chloropterus) by IUCN/BirdLife International. +Mascarene parrot (Mascarinus mascarin) - last reported in 1775; extinct due to hunting pressures. +Oceanic eclectus (Eclectus infectus) - last observed in 1793; extinct due to hunting and predation pressures. +Seychelles parakeet (Palaeornis wardi) - last observed in 1893; extinct due to hunting pressures. +Rodrigues parakeet, or Newton's parakeet (Psittacula exsul) - extinct by 1876, due to hunting pressures, habitat loss, and inclement weather. IUCN/BirdLife International place species in genus Alexandrinus. +Mauritius grey parrot, or Mascarene grey parakeet (Psittacula bensoni) - extinct by end of 1750s due to deforestation. IUCN/BirdLife International place species in genus Lophopsittacus. +Paradise parrot (Psephotellus pulcherrimus) - last observed in 1927; extinct due to drought and overgrazing. +Black-fronted parakeet (Cyanoramphus zealandicus) - last observed in 1844; extinct due to hunting and predation pressures, deforestation. +Raiatea parakeet (Cyanoramphus ulietanus) - likely extinct by end of 1770s due to predation by invasive species and deforestation. +Broad-billed parrot (Lophopsittacus mauritianus) - extinct ca. 1674 due to introduced predators. +Rodrigues parrot (Necropsittacus rodricanus) - last observed in 1761; extinct due to hunting and predation pressures, deforestation. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Pterocliformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Pterocliformes_by_population-0.md new file mode 100644 index 000000000..6221d8f7a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Pterocliformes_by_population-0.md @@ -0,0 +1,28 @@ +--- +title: "List of Pterocliformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Pterocliformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:50.525126+00:00" +instance: "kb-cron" +--- + +This is a list of Pterocliformes species by global population. Pterocliformes is a monotypic order which contains the sandgrouse family (Pteroclidae). While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +Not all Pterocliformes have had their numbers quantified, but species without population estimates are included in a secondary table below. +The IOC World Bird List (version 15.1) recognizes 16 species of Pterocliformes. As of January 2026, IUCN/BirdLife International have assessed all members of the order, though only two have population estimates. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Sphenisciformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Sphenisciformes_by_population-0.md new file mode 100644 index 000000000..7e47a8a5c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Sphenisciformes_by_population-0.md @@ -0,0 +1,26 @@ +--- +title: "List of Sphenisciformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Sphenisciformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:51.816172+00:00" +instance: "kb-cron" +--- + +This is a list of Sphenisciformes species by global population. While numbers are estimates, they have been made by experts in their fields. +Sphenisciformes (from the Latin for "wedge-shaped") is the taxonomic order to which penguins belong. The IOC World Bird List recognizes 19 species of Sphenisciformes. BirdLife International has assessed 18 species (95% of total species), all of which have had their population estimated. This list follows IUCN classifications for species names and taxonomy. Where IUCN classifications differ from other ornithological authorities, alternative names and taxonomies are noted. +A variety of methods are used for counting penguins, including the first census from space in April 2012, when imagery from Ikonos, QuickBird-2, and WorldView-2 satellites were used to count emperor penguins in Antarctica. Most maritime surveys use strip transect and distance sampling to measure penguin species density; this is then extrapolated over the animal's range. The Galapagos penguin has been counted annually since 1961 by the Galápagos National Park Service. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +Extinct species from this order include the Waitaha penguin, which went extinct between 1300–1500 (soon after the Polynesian arrival to New Zealand), and the Chatham penguin, which is only known through subfossils; however, an extant individual may have been kept in captivity by researchers sometime between 1867 and 1872. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Struthioniformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Struthioniformes_by_population-0.md new file mode 100644 index 000000000..935c979e9 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Struthioniformes_by_population-0.md @@ -0,0 +1,24 @@ +--- +title: "List of Struthioniformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Struthioniformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:53.140870+00:00" +instance: "kb-cron" +--- + +This is a list of Struthioniformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +The IOC World Bird List (version 15.1) recognizes 2 species of Struthioniformes. As of December 2025, IUCN/BirdLife International have assessed 1/2 (50%) members of this order. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Suliformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Suliformes_by_population-0.md new file mode 100644 index 000000000..c3ecdc1d7 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Suliformes_by_population-0.md @@ -0,0 +1,31 @@ +--- +title: "List of Suliformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Suliformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:54.531826+00:00" +instance: "kb-cron" +--- + +This is a list of Suliformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +Suliformes include the following families: Sulidae (gannets and boobies), Fregatidae (frigatebirds), Phalacrocoracidae (cormorants), Anhingidae (darters), and the Plotopteridae (flightless seabirds of the North Pacific that went extinct in the Miocene). +The IOC World Bird List (version 15.1) recognizes 60 species of Suliformes, one of which is extinct. As of December 2025, IUCN/BirdLife International have assessed 54 of these species (excepting Cocos booby and Imperial shag complex splits), 44 of which have population estimates. This list follows IUCN classifications for species names. Where IUCN classifications differ from other ornithological authorities, alternative names are noted. +Some members included in Suliformes are extinct: + +Spectacled cormorant (Urile perspicillatus) - largest known cormorant species, extinct since 1850s. + + +== Species by global population == + + +== Species without population estimates == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Tinamiformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Tinamiformes_by_population-0.md new file mode 100644 index 000000000..f16809479 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Tinamiformes_by_population-0.md @@ -0,0 +1,24 @@ +--- +title: "List of Tinamiformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Tinamiformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:55.826046+00:00" +instance: "kb-cron" +--- + +This is a list of Tinamiformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is not comprehensive, as not all Tinamiformes have had their numbers quantified. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_Trogoniformes_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_Trogoniformes_by_population-0.md new file mode 100644 index 000000000..df5fdf068 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_Trogoniformes_by_population-0.md @@ -0,0 +1,24 @@ +--- +title: "List of Trogoniformes by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_Trogoniformes_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:56.970433+00:00" +instance: "kb-cron" +--- + +This is a list of Trogoniformes species by global population. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. +This list is not comprehensive, as not all Trogoniformes have had their numbers quantified. + + +== Species by global population == + + +== See also == + +Lists of birds by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_aging_processes-0.md b/data/en.wikipedia.org/wiki/List_of_aging_processes-0.md new file mode 100644 index 000000000..11f77d324 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_aging_processes-0.md @@ -0,0 +1,32 @@ +--- +title: "List of aging processes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_aging_processes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:01.877588+00:00" +instance: "kb-cron" +--- + +Accumulation of lipofuscin +Aging brain +Calorie restriction +Cross-link +Crosslinking of DNA +Degenerative disease +DNA damage theory of aging +Exposure to ultraviolet light +Free-radical damage +Glycation +Life expectancy +Longevity +Maximum life span +Senescence +Stem cell theory of aging + + +== See also == +Index of topics related to life extension + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_anatomical_isthmi-0.md b/data/en.wikipedia.org/wiki/List_of_anatomical_isthmi-0.md new file mode 100644 index 000000000..51cb66321 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_anatomical_isthmi-0.md @@ -0,0 +1,25 @@ +--- +title: "List of anatomical isthmi" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_anatomical_isthmi" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:03.096283+00:00" +instance: "kb-cron" +--- + +In anatomy, "isthmus" refers to a constriction between organs. This is a list of anatomical isthmi: + +Aortic isthmus, section of the aortic arch +Cavo-tricuspid isthmus of the right atrium of the heart, a body of fibrous tissue in the lower atrium between the inferior vena cava and the tricuspid valve +Isthmus, the ear side of the eustachian tube +Isthmus, the narrowed part between the trunk and the splenium of the corpus callosum +Isthmus, formation of the shell membrane in birds' oviducts +Isthmus lobe, a lobe in the prostate +Isthmus of cingulate gyrus +Isthmus of fauces, opening at the back of the mouth into the throat +Isthmus organizer, a secondary organizer region at the junction of the midbrain and metencephalon +Isthmus tubae uterinae, which links the fallopian tube to the uterus +Kronig isthmus, a band of resonance representing the apex of the lung +Thyroid isthmus, a thin band of tissue connecting some of the lobes that make up the thyroid +Uterine isthmus, the inferior-posterior part of the uterus \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_animals_by_number_of_legs-0.md b/data/en.wikipedia.org/wiki/List_of_animals_by_number_of_legs-0.md new file mode 100644 index 000000000..14e21a11c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_animals_by_number_of_legs-0.md @@ -0,0 +1,20 @@ +--- +title: "List of animals by number of legs" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_animals_by_number_of_legs" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:58.669142+00:00" +instance: "kb-cron" +--- + +The following is a list of selected animals in order of increasing number of legs, from 0 legs to 653 pairs of legs, the maximum recorded in the animal kingdom. Each entry provides the relevant taxa up to the rank of phylum. Each entry also provides the common name of the animal. If the relevant taxon includes different animals with different common names, then the entry provides the common name of a familiar example. +If juveniles have fewer legs than adults, then the animal is listed by the number of legs recorded in mature adults. If this number varies among adults within the taxon, then this variation is noted in a comment. In counting legs, this list follows conventions adopted in the relevant literature. For example, millipedes with gonopods are listed by numbers that exclude leg pairs that become gonopods, but numbers for millipedes with telopods include leg pairs that become telopods. +Animals have been selected so that each number from 0 to 55 leg pairs has one example listed. Each of these examples is listed by a number closely associated with the relevant taxon, either because that number is the one most commonly observed in that taxon or because that number is one of only a few recorded for the taxon. Beyond 55 leg pairs, intraspecific variation in leg number increases, and the association between species and any particular number breaks down. Beyond 55 leg pairs, examples are listed only if they represent especially significant maximum numbers (e.g., most legs in the animal kingdom) or exhibit relatively little intraspecific variation in leg number. +This list draws examples from three broad groups of animals: tetrapods (with 0 to 2 leg pairs, providing three examples), velvet worms (with 13 to 43 leg pairs, providing ten examples), and arthropods (adults with 3 to 653 leg pairs, providing all the other examples). Four classes of arthropods each provide multiple examples, including sea spiders (adults with 4 to 6 leg pairs, providing two examples) and pauropods (adults with 8 to 11 leg pairs, providing four examples), but most of the examples listed are either millipedes (adults with 11 to 653 leg pairs) or centipedes (adults with 15 to 191 leg pairs). Most of the millipede examples come from two orders, Polydesmida (flat-backed millipedes, providing four examples) and Chordeumatida (sausage millipedes, providing eight examples), each with some variation in leg number among species but little variation within species. Nearly all of the centipede examples come from only one order, Geophilomorpha (soil centipedes), which exhibits wide variation in leg number among species (from 27 to 191 leg pairs). Nearly all of the examples from the order Geophilomorpha come from three families of soil centipedes (Mecistocephalidae, Schendylidae, and Geophilidae) that exhibit relatively little intraspecific variation in leg number. + + +== List of animals by number of legs == + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_animals_by_number_of_neurons-0.md b/data/en.wikipedia.org/wiki/List_of_animals_by_number_of_neurons-0.md new file mode 100644 index 000000000..61f98c138 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_animals_by_number_of_neurons-0.md @@ -0,0 +1,39 @@ +--- +title: "List of animals by number of neurons" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_animals_by_number_of_neurons" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:07.697406+00:00" +instance: "kb-cron" +--- + +The following are two lists of animals ordered by the size of their nervous system. The first list shows number of neurons in their entire nervous system. The second list shows the number of neurons in the structure that has been found to be representative of animal intelligence. The human brain contains 86 billion neurons, with 16 billion neurons in the cerebral cortex. +Neuron counts constitute an important source of insight on the topic of neuroscience and intelligence: the question of how the evolution of a set of components and parameters (~1011 neurons, ~1014 synapses) of a complex system leads to the phenomenon of intelligence. + + +== Overview == +Neurons are the cells that transmit information in an animal's nervous system so that it can sense stimuli from its environment and behave accordingly. Not all animals have neurons; Trichoplax and sponges lack nerve cells altogether. +Neurons may be packed to form structures such as the brain of vertebrates or the neural ganglions of insects. +The number of neurons and their relative abundance in different parts of the brain is a determinant of neural function and, consequently, of behavior. + + +== Whole nervous system == + +All numbers for neurons (except Caenorhabditis and Ciona), and all numbers for synapses (except Ciona) are estimations. + + +== Forebrain (cerebrum or pallium) only == +Proxies for animal intelligence have varied over the centuries. One early suggestion was brain size (or weight, which provides the same ordering.) A second proposal was brain-to-body-mass ratio, and a third was encephalization quotient, sometimes referred to as EQ. The current best predictor is number of neurons in the forebrain, based on Herculano-Houzel's improved neuron counts. This accounts for variation in the number of neurons in the rest of the brain, for which no link to intelligence has been established. Elephants, for example, have an exceptionally large cerebellum, while birds make do with a much smaller one. +Differing methods have been used to count neurons, and these may differ in degree of reliability. The primary methods are the optical fractionator, an application of stereology and the isotropic fractionator, a recent methodological innovation. Most numbers in the list are the result of studies using the newer isotropic fractionator. A variation of the optical fractionator was responsible for the previous total human brain neuron count of 100,000,000,000 neurons, which has been revised down to 86,000,000,000 by the use of the isotropic fractionator. This is in part why it may be considered to be less reliable. Finally, some numbers are the result of estimations based on correlations observed between number of cortical neurons and brain mass within closely related taxa. +The following table gives information on the number of neurons estimated to be in the sensory-associative structure: the cerebral cortex (aka pallium) for mammals, the dorsal ventricular ridge ("DVR" or "hypopallium") of the pallium for birds, and the corpora pedunculata ("mushroom bodies") for insects. + + +== See also == + + +== Notes == +Reference 56 cited for all dog neuron numbers on this Wikipedia page is a Univerzita Karlova student review of a single 2017 study by Suzana Herculano-Houzel (a self avowed "dog person") which has not been independently replicated. + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_animals_that_produce_silk-0.md b/data/en.wikipedia.org/wiki/List_of_animals_that_produce_silk-0.md new file mode 100644 index 000000000..e3de0de7b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_animals_that_produce_silk-0.md @@ -0,0 +1,53 @@ +--- +title: "List of animals that produce silk" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_animals_that_produce_silk" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:05.476182+00:00" +instance: "kb-cron" +--- + +Silk is produced by a variety of animals, for different purposes, with various types being produced. + + +== Insects == +Silkworms produce silk when undergoing larval to adult metamorphosis. +Raspy crickets produce silk to form nests. +Honeybee and bumblebee larvae produce silk to strengthen the wax cells in which they pupate. +Bulldog ants spin cocoons to protect themselves during pupation. +Weaver ants use silk to connect leaves together to make communal nests. +Caddisfly larvae produce silk. +Webspinners have silk glands on their front legs. +Hornets +Silverfish +Mayflies +Thrips +Leafhoppers produce silk nests under the leaves of the trees where they live, to protect them against predators. +Beetles +Lacewings +Fleas +Flies +Midges +Caterpillars of many butterfly species use silk to create shelters or attach to substrates for pupation. +Parasitic wasps such as braconids use silk cocoons for pupation. + + +== Other animals == +The family Projapygidae in the order Diplura have cerci that contain silk glands. +The mussel Pinna nobilis creates silk to bond itself to rocks. It is used to make sea silk. +Spiders make spider silk for various purposes such as weaving their webs, protecting their eggs or as a safety line. +The amphipod Peramphithoe femorata uses silk to make a nest out of kelp blades. Another amphipod, Crassicorophium bonellii, use silk to build shelter. +Carp produce fibroin units, a component of silk, to attach their eggs to rocks. +Spider mites make webs that protects them against predators. +Symphyla produce silk through a pair of spinnerets, which is used for nest building, escape and defense. +Pseudoscorpions make silk chambers in which they molt. +Goats have been genetically modified to produce milk containing extractable silk proteins. +Dulichia rhabdoplastis + + +== References == + + +== External links == +US National Library of Medicine, National Institutes of Health, documentation about various animals that produce silk and why. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_bacterial_disulfide_oxidoreductases-0.md b/data/en.wikipedia.org/wiki/List_of_bacterial_disulfide_oxidoreductases-0.md new file mode 100644 index 000000000..e517b9d8b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_bacterial_disulfide_oxidoreductases-0.md @@ -0,0 +1,17 @@ +--- +title: "List of bacterial disulfide oxidoreductases" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_bacterial_disulfide_oxidoreductases" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:09.015235+00:00" +instance: "kb-cron" +--- + +Bacterial thiol disulfide oxidoreductases (TDOR) are bacterial enzymes that participate in redox reactions involving cysteine residues. Along with unfolded proteins, they are secreted from bacterial cells into periplasmic spaces or extracellularly, and may have membrane anchors. Some have functions in promoting processes of adhesion and biofilm development, and generally disease development. + + +== Table == + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_biodiversity_databases-0.md b/data/en.wikipedia.org/wiki/List_of_biodiversity_databases-0.md new file mode 100644 index 000000000..3a42c4a8a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_biodiversity_databases-0.md @@ -0,0 +1,26 @@ +--- +title: "List of biodiversity databases" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_biodiversity_databases" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:12.044065+00:00" +instance: "kb-cron" +--- + +This is a list of biodiversity databases. Biodiversity databases store taxonomic information alone or more commonly also other information like distribution (spatial) data and ecological data, which provide information on the biodiversity of a particular area or group of living organisms. They may store specimen-level information, species-level information, information on nomenclature, or any combination of the above. Most are available online. +Specimen-focused databases contain data about individual specimens, as represented by vouchered museum specimens, collections of specimen photographs, data on field-based specimen observations and morphological or genetic data. Species-focused databases contain information summarised at the species-level. Some species-focused databases attempt to compile comprehensive data about particular species (FishBase), while others focus on particular species attributes, such as checklists of species in a given area (FEOW) or the conservation status of species (CITES or IUCN Red List). Nomenclators act as summaries of taxonomic revisions and set a key between specimen-focused and species-focused databases. They do this because taxonomic revisions use specimen data to determine species limits. + + +== See also == +Taxonomic database +Biodiversity informatics +Global biodiversity + + +== References == + + +== External links == +List of species databases at the Catalogue of Life Archived 17 September 2020 at the Wayback Machine +List of biodiversity databases at Biodiversity Tools \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_bioinformatics_institutions-0.md b/data/en.wikipedia.org/wiki/List_of_bioinformatics_institutions-0.md new file mode 100644 index 000000000..0891c5090 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_bioinformatics_institutions-0.md @@ -0,0 +1,38 @@ +--- +title: "List of bioinformatics institutions" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_bioinformatics_institutions" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:13.409161+00:00" +instance: "kb-cron" +--- + +This is a list of major bioinformatics institutions. + +National Center for Biotechnology Information (NCBI) +European Bioinformatics Institute (EMBL-EBI) +Australia Bioinformatics Resource (EMBL-ABR) +Swiss Institute of Bioinformatics (SIB) +Scripps Research Institute (TSRI) +European Molecular Biology Laboratory (EMBL) +Wellcome Trust Sanger Institute (WTSI) +Computational Biology Department +Broad Institute +Whitehead Institute +The Institute for Genomic Research +Center for Biomolecular Science and Engineering +Netherlands Bioinformatics Centre +COSBI + Institute of Bioinformatics (IOB) +Max Planck Institute for Molecular Cell Biology and Genetics (MPI-CBG) +Partner Institute for Computational Biology +Flatiron Institute +DDBJ Center (DDBJ) +Bioinformatics Institute (Singapore) +Database Center for Life Science (DBCLS) + + +== References == + +Benue state university department of Anatomy \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_biological_databases-0.md b/data/en.wikipedia.org/wiki/List_of_biological_databases-0.md new file mode 100644 index 000000000..7d85cb8fd --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_biological_databases-0.md @@ -0,0 +1,177 @@ +--- +title: "List of biological databases" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_biological_databases" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:02.226012+00:00" +instance: "kb-cron" +--- + +Biological databases are stores of biological information. The journal Nucleic Acids Research regularly publishes special issues on biological databases and has a list of such databases. The 2018 issue has a list of about 180 such databases and updates to previously described databases. Omics Discovery Index can be used to browse and search several biological databases. Furthermore, the NIAID Data Ecosystem Discovery Portal developed by the National Institute of Allergy and Infectious Diseases (NIAID) enables searching across databases. + + +== Meta databases == +Meta databases are databases of databases that collect data about data to generate new data. They are capable of merging information from different sources and making it available in a new and more convenient form, or with an emphasis on a particular disease or organism. Originally, metadata was only a common term referring simply to data about data such as tags, keywords, and markup headers. + +bio.tools: a community-driven registry of bioinformatics software and data resources +ConsensusPathDB: a molecular functional interaction database, integrating information from 12 others +Entrez search system at the National Center for Biotechnology Information (NCBI) link +Expert Protein Analysis System (ExPASy) link +Neuroscience Information Framework (University of California, San Diego): integrates hundreds of neuroscience relevant resources; many are listed below +Resources at the Health Sciences Library System (HSLS) of the University of Pittsburgh +MolBio Information Service +OBRC: Online Bioinformatics Resources Collection +HSLS MolBio Available Software +Databases A-Z + + +== Model organism databases == +Model organism databases provide in-depth biological data for intensively studied organisms. + +PomBase: the knowledgebase for the fission yeast Schizosaccharomyces pombe +SubtiWiki: integrated database for the model bacterium Bacillus subtilis +TAIR: the knowledgebase for the plant Arabidopsis thaliana + + +== Nucleic acid databases == + + +=== DNA databases === + +The primary databases make up the International Nucleotide Sequence Database (INSD). The include: + +DNA Data Bank of Japan (National Institute of Genetics) +EMBL (European Bioinformatics Institute) +GenBank (National Center for Biotechnology Information) +DDBJ (Japan), GenBank (USA) and European Nucleotide Archive (Europe) are repositories for nucleotide sequence data from all organisms. All three accept nucleotide sequence submissions, and then exchange new and updated data on a daily basis to achieve optimal synchronisation between them. These three databases are primary databases, as they house original sequence data. They collaborate with Sequence Read Archive (SRA), which archives raw reads from high-throughput sequencing instruments. +Secondary databases are: + +HapMap +OMIM (Online Mendelian Inheritance in Man): inherited diseases +RefSeq +1000 Genomes Project: launched in January 2008. The genomes of more than a thousand anonymous participants from a number of different ethnic groups were analyzed and made publicly available. +EggNOG Database: a hierarchical, functionally and phylogenetically annotated orthology resource based on 5090 organisms and 2502 viruses. It provides multiple sequence alignments and maximum-likelihood trees, as well as broad functional annotation. +Other databases + +Nucleosome positioning region database + + +=== Gene expression databases === +Generic gene expression databases +Microarray gene expression databases + + +=== Genome databases === +These databases collect genome sequences, annotate and analyze them, and provide public access. Some add curation of experimental literature to improve computed annotations. These databases may hold many species genomes, or a single model organism genome. + + +=== Phenotype databases === +PHI-base: pathogen-host interaction database. It links gene information to phenotypic information from microbial pathogens on their hosts. Information is manually curated from peer-reviewed literature. +RGD Rat Genome Database: genomic and phenotype data for Rattus norvegicus +PomBase database: manually curated phenotypic data for the yeast Schizosaccharomyces pombe + + +=== RNA databases === + +miRBase: the microRNA database +PolymiRTS: a database of DNA variations in putative microRNA target sites +PolyQ: database of polyglutamine repeats in disease and non-disease associated proteins +Rfam: a database of RNA families +IRESbase: A comprehensive database of experimentally validated internal ribosome entry sites. + + +== Amino acid and protein databases == +(See also: List of proteins in the human body) +Several publicly available data repositories and resources have been developed to support and manage protein related information, biological knowledge discovery and data-driven hypothesis generation. The databases in the table below are selected from the databases listed in the Nucleic Acids Research (NAR) databases issues and database collection and the databases cross-referenced in the UniProtKB. Most of these databases are cross-referenced with UniProt / UniProtKB so that identifiers can be mapped to each other. +Proteins in human: +There are about ~20,000 protein coding genes in the standard human genome. (Roughly ~1200 already have Wikipedia articles - the Gene Wiki - about them) if we are Including splice variants, there could be as many as 500,000 unique human proteins + + +=== Different types of Protein databases === + + +== Other protein database links == +The Pfam (proteins families) database link +The Worldwide Protein Data Bank (wwPDB) link and the related foundation link + + +== Signal transduction pathway databases == +NCI-Nature Pathway Interaction Database +Netpath: curated resource of signal transduction pathways in humans +Reactome: navigable map of human biological pathways, ranging from metabolic processes to hormonal signalling (Ontario Institute for Cancer Research, European Bioinformatics Institute, NYU Langone Medical Center, Cold Spring Harbor Laboratory) +WikiPathways + + +== Metabolic pathway and protein function databases == + + +== Taxonomic databases == + +Numerous databases collect information about species and other taxonomic categories. The Catalogue of Life is a special case as it is a meta-database of about 150 specialized "global species databases" (GSDs) that have collected the names and other information on (almost) all described and thus "known" species. + +BacDive: bacterial metadatabase that provides strain-linked information about bacterial and archaeal biodiversity, including taxonomy information +Catalogue of Life: a meta-database of all species on earth +EzTaxon-e: database for the identification of prokaryotes based on 16S ribosomal RNA gene sequences +NCBI Taxonomy: a taxonomic database operated by NCBI and concentrating on all taxa for which DNA sequences are available (those sequences are stored by GenBank, another database operated by NCBI). + + +== Image databases == +Images play a critical role in biomedicine, ranging from images of anthropological specimens to zoology. However, there are relatively few databases dedicated to image collection, although some projects such as iNaturalist collect photos as a main part of their data. A special case of "images" are 3-dimensional images such as protein structures or 3D-reconstructions of anatomical structures. Image databases include, among others: + +Allen Brain Atlas +Digital Brain Bank +Electron Microscopy Public Image Archive (EMPIAR) +FlyExpress +Image Data Resource +Morphobank +Morphosource + + +=== Radiologic databases === +The Cancer Imaging Archive (TCIA) +Neuroimaging Informatics Tools and Resources Clearinghouse + + +== Additional databases == + + +=== Exosomal databases === +ExoCarta +Extracellular RNA Atlas: a repository of small RNA-seq and qPCR-derived exRNA profiles from human and mouse biofluids + + +=== Mathematical model databases === +Biomodels Database: published mathematical models describing biological processes +MorpheusML Model Repository: published, community-contributed, and educational multi-scale and multicellular models for systems biology + + +=== Databases on antimicrobial resistance rates and antibiotic consumption === +CIPARS +EARS-Net +ESAC-Net + + +=== Databases on antimicrobial resistance mechanisms === + + +== Wiki-style databases == +Gene Wiki +WikiSpecies +WikiProfessional + + +== Specialized databases == + + +== References == + + +== External links == +The Bioregistry database system link +The Database of Molecular Motions link +The ELIXIR coordination project link +The National Center for Biotechnology Information (NCBI) link +Nucleic Acid Research (NAR) Database Summary Paper Category List + +Nucleic Acid Research Molecular Biology Database Collection – over 1,600 databases \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_birds_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_birds_by_population-0.md new file mode 100644 index 000000000..c7f529284 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_birds_by_population-0.md @@ -0,0 +1,35 @@ +--- +title: "List of birds by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_birds_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:22.368442+00:00" +instance: "kb-cron" +--- + +This is a set of lists of bird species by global population, divided by avian order. While numbers are estimates, they have been made by the experts in their fields. For more information on how these estimates were ascertained, see Wikipedia's articles on population biology and population ecology. Contributing organizations include the IUCN, BirdLife International, and Partners in Flight. +The global population of all mature birds is estimated to be 50 – 100 billion individuals. Total species population, including immature individuals, is higher during the breeding season of each species. +These lists are incomplete, because experts have not estimated all bird populations. For example, the spectacled flowerpecker was only discovered in 2010, and did not receive its scientific name (Dicaeum dayakorum) until 2019, adding to the other 73 new bird species described by ornithologists from 2000 – 2009. Global population estimates for many of these at this time would lack accuracy. +All numbers are estimates, because they are made via bird surveys (e.g., point counting) and extrapolating species density estimates made via observation data over a species' known range. Population estimates should be interpreted with a margin of error, even when only one value is provided. +The number of species within a order corresponds to IOC guidance unless otherwise noted. IUCN/Birdlife International taxonomic classifications often differ from the IOC; for specific disagreements, see Order specific pages. + + +== By taxonomy == + + +== See also == + +Lists of mammals by population +Lists of organisms by population + + +== Notes == +1.^Denominator (Total Species in Order) from IOC List of Birds (version 15.1). +2.^Number of species with population estimates includes estimates for Northern New Zealand dotterel, common white tern, and little white tern, which are considered full species by IUCN/BirdLife International, but subspecies by the IOC. +3.^Values include the common pheasant's estimated population across its introduced range. +4.^Number of species with population estimates includes estimates for black-winged trumpeter and Junin crake, which are considered full species by IUCN/BirdLife International, but subspecies by the IOC. +5.^IOC recognizes tricolored grebe as a full species; IUCN/BirdLife International do not. The latter splits silvery grebe into two species (northern/southern silvery grebe); which the former retains as one species. This results in 23 total species regardless, and 22 species with populations quantified. + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md b/data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md new file mode 100644 index 000000000..50a79b843 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md @@ -0,0 +1,82 @@ +--- +title: "List of brown seaweeds of the Cape Peninsula and False Bay" +chunk: 1/2 +source: "https://en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:45.220951+00:00" +instance: "kb-cron" +--- + +This is a list of brown seaweeds recorded from the oceans bordering The Cape Peninsula in South Africa from Melkbosstrand on the West Coast to Cape Hangklip on the South Coast. +This list comprises locally used common names, scientific names with author citation and recorded ranges. Ranges specified may not be the entire known range for the species, but should include the known range within the waters surrounding the Republic of South Africa. +Brown seaweed refers to thousands of species of macroscopic, multicellular, marine algae in the taxon Phaeophyta +The marine ecology is unusually varied for an area of this size, as a result of the meeting of two major oceanic water masses near Cape Point, and the park extends into two coastal marine bioregions. The ecology of the west or "Atlantic Seaboard" side of the Cape Peninsula is noticeably different in character and biodiversity to that of the east, or "False Bay" side. Both sides are classified as temperate waters, but there is a significant difference in average temperature, with the Atlantic side being noticeably colder on average. +List ordering and taxonomy complies where possible with the current usage in Algaebase, and may differ from the cited source, as listed citations are primarily for range or existence of records for the region. +Sub-taxa within any given taxon are arranged alphabetically as a general rule. +Details of each species may be available through the relevant internal links. Synonyms may be listed where useful. + +== Class: Phaeophyceae == + +=== Order: Cutleriales === + +==== Family Cutleriaceae ==== +Aglaozonia sp. (Muizenberg, False Bay. Brandfontein. Bird Island, eastern Cape) + +=== Order: Desmarestiales === + +==== Family Desmarestiaceae ==== +Acid weed Desmarestia herbacea subsp. firma (C.Agardh) A.F.Peters, E.C.Yang, F.C.Küpper & Prud'Homme van Reine, 2014, recorded as syn. Desmarestia firma (C.Agardh) Skottsberg in Nordenskjöld 1907, syn. Sporochnus herbaceus var. firma C.Agardh 1824, (Möwe Bay, Namibia to Betty's Bay. Doubtful record for Cape Agulhas) + +=== Order: Dictyotales === + +==== Family Dictyotaceae ==== +Dictyota dichotoma (Hudson) J.V.Lamouroux 1809, syn. Ulva dichotoma Hudson 1762, Zonaria dichotoma (Hudson) C.Agardh 1817, Fucus dichotomus (Hudson) Bertolini 1819, Haliseris dichotoma (Hudson) Sprengel 1827, Dichophyllium dichotomum (Hudson) Kützing 1843,(Langebaan and False Bay to Natal. D. dichotoma var. intricata (C.Agardh) Greville 1830, common at Kalk Bay and Dalebrook, and occurring more or less throughout the range of the species) +Dictyota liturata J.Agardh 1848, (Kommetjie on Cape Peninsula to Umhlali in KwaZulu-Natal) +Spotted dictyota Dictyota naevosa (Suhr) Montagne 1840, syn. Zonaria naevosa Suhr 1834, Cutleria naevosa (Suhr) Hering ex Krauss 1846, (Die Walle to Umhlali, KwaZulu-Natal)(Cape Peninsula eastward into KwaZulu-Natal as far as Mission Rocks) +Intricate dictyota, Dictyota spp. +Multi-fanned zonaria Exallosorus harveyanus (Pappe ex Kützing) J.A.Phillips, 1997. Syn. Zonaria harveyana (Pappe ex Kützing) Areschoug 1851, (Platbank, False Bay to KwaZulu-Natal as far north as Park Rynie. Endemic) +Articulated zonaria, Zonaria subarticulata (J.V.Lamouroux) Papenfuss, 1944. + +=== Order: Ectocarpales === + +==== Family: Acinetosporaceae ==== +Acinetospora crinita (Carmichael) Sauvageau 1899, syn. Acinetospora pusilla var. crinita (Carmichael) Batters, Ectocarpus crinitus Carmichael 1833, (False Bay, Eastern Cape) +Feldmannia irregularis (Kützing) G.Hamel 1939, syn. Ectocarpus irregularis Kützing 1845, Giffordia irregularis (Kützing) Joly 1965, Hincksia irregularis (Kützing) Amsler 1991, (Cape Peninsula, Langebaan lagoon and Eastern Cape) +Hincksia granulosa (Smith) P.C.Silva in P.C.Silva, E.G.Meñez & R.L.Moe 1987, Conferva granulosa Smith 1811, Ectocarpus granulosus (Smith) C.Agardh 1828, Giffordia granulosa (Smith) G.Hamel 1939, (Muizenberg and Oudekraal, also Namibia) + +==== Family Chordariaceae ==== +Asperococcus compressus A.W.Griffiths ex W.J.Hooker 1833, (Table Bay) +Furry slime strings, Chordariaceae spp. +Brown brains Leathesia marina (Lyngbye) Decaisne 1842, syn. Chaetophora marina Lyngbye 1819, Leathesia difformis (Linnaeus) J.E. Areschoug 1847, (All South African coasts: common on west coast, intermittent in eastern Cape and KwaZulu-Natal) +Myriocladia capensis J. Agardh 1848, (Port Nolloth to De Hoop Nature Reserve, endemic) +Myriogloea abbreviata Kylin 1940, (Sea Point to Port Nolloth, endemic) +Myriogloea papenfussii Kylin 1940, (False Bay to Melkbosstrand, endemic) +Myrionema cf. magnusii (Sauvageau) Loiseaux 1967, syn. Ascocyclus magnusii Sauvageau 1927, (Glencairn) +Papenfussiella gracilis Kylin 1940, (Platboombaai to Swakopmund, Namibia. Endemic to southern Africa) +Zeacarpa leiomorpha Anderson, Simons & Bolton 1988, (Yzerfontein to Dalebrook, Probably more widespread) + +==== Family Chordariopsidaceae ==== +Cape cord weed Chordariopsis capensis (C.Agardh) Kylin 1940, syn. Chordaria flagelliformis var. capensis C.Agardh 1824, (Cape Frio, Namibia to at least Arniston) + +==== Family Ectocarpaceae ==== +Ectocarpus acutus Setchell & Gardner 1922c, (Olifantsbos to Hondeklipbaai) +Ectocarpus fasciculatus Harvey 1841, (Melkbosstrand to De Hoop) +Ectocarpus siliculosus (Dillwyn) Lyngbye 1819, syn. Conferva siliculosa Dillwyn 1809, Ceramium siliculosum (Dillwyn) C.Agardh 1811, Ectocarpus confervoides f. siliculosus (Dillwyn) Kjellman 1872, Ectocarpus confervoides var. siliculosus (Dillwyn) Farlow 1881, (Port Nolloth to Eastern Cape) +Ectocarpus spp. + +==== Family: Pylaiellaceae ==== +Bachelotia antillarum (Grunow) Gerloff 1959, syn. Ectocarpus antillarum Grunow 1867, Pylaiella antillarum (Grunow) De Toni 1895, (False Bay to KwaZulu-Natal) + +==== Family Scytosiphonaceae ==== +Oyster thief Colpomenia sinuosa (Mertens ex Roth) Derbès & Solier in Castagne 1851, syn. Ulva sinuosa Mertens ex Roth 1806, Encoelium sinuosum (Mertens ex Roth) C.Agardh 1820, Stilophora sinuosa (Mertens ex Roth) C.Agardh 1827, Asperococcus sinuosus (Mertens ex Roth) Bory de Saint-Vincent 1832, Asperococcus sinuosus (C.Agardh) Zanardini 1841, Hydroclathrus sinuosus (Mertens) ex Roth) Zanardini 1843, (Throughout South Africa) +Compsonema cf. sessile Setchell & Gardner 1922a, (Oudekraal) +Starred cushion Iyengaria stellata (Børgesen) Børgesen 1939, syn. Rosenvingea stellata Børgesen 1928, Colpomenia stellata (Børgesen) Børgesen 1930, (Southern Cape Peninsula to KwaZulu-Natal) +Petalonia binghamiae (J.Agardh) K.L.Vinogradova, 1973, also recorded as syn. Endarachne binghamiae J.Agardh 1896, (False Bay eastwards to KwaZulu-Natal as far as Port Edward) +Petalonia fascia (O.F.Müller) Kuntze 1898, syn. Fucus fascia O.F.Müller 1778, Laminaria fascia (O.F.Müller) C.Agardh 1817, Ulva fascia (O.F.Müller) Lyngbye 1819, Ilea fascia (O.F.Müller) Fries 1835, Phyllitis fascia (O.F.Müller) Kützing 1843, Saccharina fascia (O.F.Müller) Kuntze 1891, (Yzerfontein to Soetwater) +Sausage skins, Scytosiphon lomentaria (Lyngbye) Link 1833, Chorda lomentaria Lyngbye 1819, Scytosiphon filum var. lomentarius (Lyngbye) C.Agardh 1820, Fucus lomentarius (Lyngbye) Sommerfelt 1826, Scytosiphon simplicissimus (Clemente) Cremades 1990, Ulva simplicissima Clemente 1807, (Simon's Town to Lüderitz) + +=== Order: Fucales === + +==== Family Bifurcariopsidaceae ==== +Upright wrack Bifurcariopsis capensis (Areschoug) Papenfuss 1940a, syn. Fucodium capense Areschoug 1854, (Cape Infanta to Groen River) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md b/data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md new file mode 100644 index 000000000..64fd6b9fc --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md @@ -0,0 +1,68 @@ +--- +title: "List of brown seaweeds of the Cape Peninsula and False Bay" +chunk: 2/2 +source: "https://en.wikipedia.org/wiki/List_of_brown_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:45.220951+00:00" +instance: "kb-cron" +--- + +==== Family Sargassaceae ==== +Long-leafed sargassum Anthophycus longifolius (Turner) Kützing, 1849 syn. Fucus longifolius Turner 1809, Sargassum longifolium (Turner) C.Agardh 1820, Carpophyllum longifolium (Turner) De Toni 1895, (Platboombaai eastwards as far as Uvongo in southern KwaZulu-Natal) +Constricted axils Axillariella constricta (J.Agardh) P.C.Silva 1959b, syn. Fucodium constrictum J.Agardh 1848, Ascophyllum constricta (J.Agardh) Kuntze 1891, Ascophylla constricta (Kützing) Kuntze 1891, (Cape Peninsula to Cape Columbine) +Hanging wrack Brassicophycus brassicaeformis (Kützing) Draisma, Ballesteros, F.Rousseau & T.Thibaut 2010, syn. Pycnophycus brassicaeformis Kützing 1860, Bifurcaria brassicaeformis (Kützing) E.S.Barton 1893, (Cape Agulhas to Sea Point) +Cystophora fibrosa Simons, 1970, (De Walle to Koppie Allen, and Platboom) +Sargassum elegans Suhr, 1840, (False Bay to Mozambique. Endemic to southern Africa) +Different-leafed sargassum, Sargassum incisifolium (Turner) C.Agardh 1820, syn. Fucus incisifolius Turner 1811, Sargassum heterophyllum (Turner) C.Agardh, 1820, (False Bay eastward into Mozambique. Restricted to Southern Africa and Madagascar) + +=== Order: Laminariales === + +==== Family Laminariaceae ==== +Split-fan kelp Laminaria pallida Greville in J. Agardh 1848, Hafgygia pallida (Greville) Areschchoug 1883, Saccharina pallida (Greville) Kuntze 1891, (Danger Point to Cape Nolloth, as the schinzii form to at least Rocky Point in northern Namibia) +Bladder kelp Macrocystis pyrifera (Linnaeus) C.Agardh, 1820, also recorded as syn. Macrocystis angustifolia Bory de Saint-Vincent 1826, (Occasional in drift in False Bay. Attached from Cape Point to Paternoster) + +==== Family Lessoniaceae ==== +Sea bamboo Ecklonia maxima (Osbeck) Papenfuss 1940b, syn. Fucus maximus Osbeck 1757, (Papenkuilsfontein 10 km west of Cape Agulhas to north of Lüderitz, Namibia) +Spined kelp Ecklonia radiata (C.Agardh) J.Agardh 1848, Laminaria radiata C.Agardh 1817, Capea radiata (C.Agardh) Endlicher 1843, (Forms with long stipes and rugose blades in False Bay, Spinose forms common at Die Dam, Otherwise species common from Koppie Allen to Southern Natal. Longer stiped smooth bladed form as far east as parts of Zululand)(Deep water populations extend to Sodwana Bay at depths up to 60m) + +=== Order: Ralfsiales === + +==== Family Neoralfsiaceae ==== +Neoralfsia expansa (J.Agardh) P.-E.Lim & H.Kawai ex Kraft 2009, syn. Myrionema expansum J.Agardh 1847, Ralfsia expansa (J.Agardh) J.Agardh 1848, (unclear distribution) + +==== Family Ralfsiaceae ==== +Ralfsia Ralfsia verrucosa (Areschoug) J.Agardh 1848, syn. Cruoria verrucosa Areschoug 1843, (Common on all west coast shores and probably throughout the Agulhas marine province) + +=== Order: Scytothamnales === + +==== Family Splachnidiaceae ==== +Dead man's fingers, Splachnidium rugosum (Linnaeus) Greville 1830, (Dominant in mid-shore throughout west coast, Lüderitz, Namibia to eastern Cape) + +=== Order: Sphacelariales === + +==== Family Sphacelariaceae ==== +Sphacelaria brachygonia Montagne 1843, (St. James and Strandfontein, False Bay, More frequent on south coast as far as Transkei) +Sphacelaria rigidula Kützing 1843, (Kalk Bay in False Bay to at least Transkei) + +==== Family Stypocaulaceae ==== +Broom-weed, Halopteris funicularis (Montagne) Sauvageau, 1904, also recorded as syn. Stypocaulon funiculare (Montagne) Kützing 1849, (Port Nolloth to Cape Agulhas and Tsitsikamma) + +=== Order: Sporochnales === + +==== Family Sporochnaceae ==== +Carpomitra costata (Stackhouse) Batters 1902, (Algoa Bay. Vulcan Rock, Hout Bay) +Sporochnus pedunculatus (Hudson) C. Agardh 1820, (Strandfontein) + +== Geographical position of places mentioned in species ranges == + +== See also == +Helderberg Marine Protected Area – Marine conservation area in the Western Cape in South Africa +List of marine animals of the Cape Peninsula and False Bay +List of brown seaweeds of South Africa +Marine geology of the Cape Peninsula and False Bay +Table Mountain National Park – Nature conservation area on the Cape Peninsula in Cape Town, South Africa +Table Mountain National Park Marine Protected Area – Marine conservation area around the Cape Peninsula in South Africa +False Bay – Bay of the Atlantic Ocean at South Africa + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_camouflage_methods-0.md b/data/en.wikipedia.org/wiki/List_of_camouflage_methods-0.md new file mode 100644 index 000000000..bba30fac9 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_camouflage_methods-0.md @@ -0,0 +1,36 @@ +--- +title: "List of camouflage methods" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_camouflage_methods" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:58.240717+00:00" +instance: "kb-cron" +--- + +Camouflage is the concealment of animals or objects of military interest by any combination of methods that helps them to remain unnoticed. This includes the use of high-contrast disruptive patterns as used on military uniforms, but anything that delays recognition can be used as camouflage. Camouflage involves deception, whether by looking like the background or by resembling something else, which may be plainly visible to observers. This article lists methods used by animals and the military to escape notice. + + +== Conventions used == + +Different camouflage methods employed by terrestrial, aerial, and aquatic animals, and in military usage, are compared in the table. Several methods are often combined, so for example the Bushbuck is both countershaded over its whole body, and disruptively coloured with small pale spots. Until the discovery of countershading in the 1890s, protective coloration was considered to be mainly a matter of colour matching, but while this is certainly important, a variety of other methods are used to provide effective camouflage. +When an entry is marked Dominant, that method is used widely in that environment, in most cases. For example, countershading is very common among land animals, but not for military camouflage. The dominant camouflage methods on land are countershading and disruptive coloration, supported by less frequent usage of many other methods. The dominant camouflage methods in the open ocean are transparency, reflection, and counterillumination. Transparency and reflectivity are dominant in the top 100 metres (330 ft) of the ocean; counterillumination is dominant from 100 metres (330 ft) down to 1,000 metres (3,300 ft). Most animals of the open sea use one or more of these methods. Military camouflage relies predominantly on disruptive patterns, though methods such as outline disruption are also used, and others have been prototyped. +In 1890 the English zoologist Edward Bagnall Poulton categorised animal colours by their uses, which cover both camouflage and mimicry. Poulton's categories were largely followed by Hugh Cott in 1940. Relevant Poulton categories are listed in the table. Where Poulton's definition covers a method but does not name it explicitly, the category is named in parentheses. + + +== Comparisons == + + +== References == + + +== Bibliography == +Barkas, Geoffrey; Barkas, Natalie (1952). The Camouflage Story (from Aintree to Alamein). Cassell. +Beddard, Frank Evers (1892). Animal Coloration: an account of the principal facts and theories relating to the colours and markings of animals. Swan Sonnenschein. +Cott, Hugh (1940). Adaptive Coloration in Animals. Oxford University Press. +Forbes, Peter (2009). Dazzled and Deceived: Mimicry and Camouflage. Yale. ISBN 978-0-300-12539-9. +Herring, Peter (2002). The Biology of the Deep Ocean. Oxford University Press. ISBN 978-0-198-54956-7. +Newark, Tim (2007). Camouflage. Thames and Hudson. ISBN 978-0-500-51347-7. +Poulton, Edward Bagnall (1890). The Colours of Animals: their meaning and use especially considered in the case of insects. Kegan Paul, Trench, Trübner. +Stevens, Martin; Merilaita, Sami (2011). Animal Camouflage. Cambridge University Press. ISBN 978-0-521-19911-7. +Wickler, Wolfgang (1968). Mimicry in plants and animals. McGraw-Hill. ISBN 978-1-114-82438-6 \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_carnivorans_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_carnivorans_by_population-0.md new file mode 100644 index 000000000..934a3b8a7 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_carnivorans_by_population-0.md @@ -0,0 +1,26 @@ +--- +title: "List of carnivorans by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_carnivorans_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:10.038322+00:00" +instance: "kb-cron" +--- + +This is a list of estimated global populations of Carnivora species. This list is not comprehensive, as not all carnivorans have had their numbers quantified. + + +== List == + + +== Species without population estimates == + + +== See also == + +Lists of organisms by population +Lists of mammals by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_chordate_orders-0.md b/data/en.wikipedia.org/wiki/List_of_chordate_orders-0.md new file mode 100644 index 000000000..639b1f061 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_chordate_orders-0.md @@ -0,0 +1,333 @@ +--- +title: "List of chordate orders" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_chordate_orders" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:59.583549+00:00" +instance: "kb-cron" +--- + +This article contains a list of all of the classes and orders that are located in the Phylum Chordata. +The subphyla Tunicata and Vertebrata are in the unranked Olfactores clade, while the subphylum Cephalochordata is not. Animals in Olfactores are characterized as having a more advanced olfactory system than animals not in it. +The only extinct classes shown are Placodermi and Acanthodii. Many other extinct chordate groups are not shown here. + + +== Subphylum Cephalochordata == + + +=== Class Leptocardii: Lancelets === + +Order Amphioxiformes + + +== Subphylum Tunicata == + + +=== Class Ascidiacea: Sessile tunicates === + +Order Enterogona +Order Pleurogona +Order Aspiraculata + + +=== Class Thaliacea: Pelagic tunicates === +Order Doliolida +Order Pyrosomida +Order Salpida: salps + + +=== Class Appendicularia: Solitary, free-swimming tunicates === +Order Copelata + + +== Subphylum Vertebrata == + + +=== Infraphylum Agnatha: Jawless vertebrates === + + +==== Superclass Cyclostomata: Extant jawless vertebrates ==== + + +===== Class Myxini: Hagfish ===== +Order Myxiniformes + + +===== Class Hyperoartia: Lampreys ===== +Order Petromyzontiformes + + +=== Infraphylum Gnathostomata: Jawed vertebrates === + + +==== Class Placodermi: Armoured fish † ==== +Order Acanthothoraci +Order Arthrodira +Order Antiarchi +Order Brindabellaspida +Order Petalichthyida +Order Phyllolepida +Order Ptyctodontida +Order Rhenanida +Order Pseudopetalichthyida (The placement of this order is debated.) +Order Stensioellida (The placement of this monotypic order is debated.) + + +==== Class Chondrichthyes: Cartilaginous fish ==== + + +Subclass Elasmobranchii +Superorder Batoidea +Order Rajiformes: rays and skates +Order Rhinopristiformes: sawfishes +Order Torpediniformes: electric rays +Order Myliobatiformes: (sting)rays +Superorder Selachimorpha (sharks) +Order Heterodontiformes: bullhead sharks +Order Orectolobiformes: carpet sharks +Order Carcharhiniformes: ground sharks +Order Lamniformes: mackerel sharks +Order Hexanchiformes: frilled and cow sharks +Order Squaliformes: dogfish sharks +Order Squatiniformes: angel sharks +Order Pristiophoriformes: saw sharks +Subclass Holocephali +Order Chimaeriformes: chimaeras + + +==== Class Acanthodii: Spiny sharks † ==== + +Order Climatiiformes +Order Ischnacanthiformes +Order Acanthodiformes + + +==== Superclass Osteichthyes: Bony fish ==== + + +===== Class Actinopterygii: Ray-finned fish ===== + +Order Asarotiformes † +Order Discordichthyiformes † +Order Paphosisciformes † +Order Scanilepiformes † +Order Cheirolepidiformes † +Order Paramblypteriformes † +Order Rhadinichthyiformes † +Order Palaeonisciformes † +Order Tarrasiiformes † +Order Pachycormiformes † +Order Ptycholepiformes † +Order Redfieldiiformes † +Order Haplolepidiformes † +Order Aeduelliformes † +Order Platysomiformes † +Order Dorypteriformes † +Order Eurynotiformes † +Subclass Cladistii +Order Polypteriformes +Subclass Chondrostei +Order Acipenseriformes: sturgeons and paddlefishes +Subclass Neopterygii + +Infraclass Holostei +Order Lepisosteiformes, the gars +Order Amiiformes, the bowfins +Infraclass Teleostei +Superorder Osteoglossomorpha +Order Osteoglossiformes, the bony-tongued fishes +Order Hiodontiformes, including the mooneye and goldeye +Order Lycopteriformes +Order Ichthyodectiformes † +Superorder Elopomorpha +Order Elopiformes, including the ladyfishes and tarpon +Order Albuliformes, the bonefishes +Order Notacanthiformes, including the halosaurs and spiny eels +Order Anguilliformes, the true eels and gulpers +Order Saccopharyngiformes, including the gulper eel +Superorder Clupeomorpha +Order Clupeiformes, including herrings and anchovies +Superorder Ostariophysi +Order Gonorynchiformes, including the milkfishes +Order Cypriniformes, including barbs, carp, danios, goldfishes, loaches, minnows, rasboras +Order Characiformes, including characins, pencilfishes, hatchetfishes, piranhas, tetras. +Order Gymnotiformes, including electric eels and knifefishes +Order Siluriformes, the catfishes +Superorder Protacanthopterygii +Order Salmoniformes, including salmon and trout +Order Esociformes the pike +Order Osmeriformes, including the smelts and galaxiids +Superorder Stenopterygii +Order Ateleopodiformes, the jellynose fish +Order Stomiiformes, including the bristlemouths and marine hatchetfishes +Superorder Cyclosquamata +Order Aulopiformes, including the Bombay duck and lancetfishes +Superorder Scopelomorpha +Order Myctophiformes, including the lanternfishes +Superorder Lampridiomorpha +Order Lampriformes, including the oarfish, opah and ribbonfishes +Superorder Polymyxiomorpha +Order Polymixiiformes, the beardfishes +Superorder Paracanthopterygii +Order Percopsiformes, including the cavefishes and trout-perches +Order Batrachoidiformes, the toadfishes +Order Lophiiformes, including the anglerfishes +Order Gadiformes, including cods +Order Ophidiiformes, including the pearlfishes +Superorder Acanthopterygii +Order Mugiliformes, the mullets +Order Atheriniformes, including silversides and rainbowfishes +Order Beloniformes, including the flyingfishes +Order Cetomimiformes, the whalefishes +Order Cyprinodontiformes, including livebearers, killifishes +Order Stephanoberyciformes, including the ridgeheads +Order Beryciformes, including the fangtooths and pineconefishes +Order Zeiformes, including the dories +Order Gobiesociformes, the clingfishes +Order Gasterosteiformes including sticklebacks, pipefishes, seahorses +Order Syngnathiformes, including the seahorses and pipefishes +Order Synbranchiformes, including the swamp eels +Order Tetraodontiformes, including the filefishes and pufferfish +Order Pleuronectiformes, the flatfishes +Order Scorpaeniformes, including scorpionfishes and the sculpins +Order Perciformes 40% of all fish including anabantids, centrarchids (incl. bass and sunfish), cichlids, gobies, gouramis, mackerel, perches, scats, whiting, wrasses + + +===== Class Sarcopterygii: Lobe-finned fish ===== + +Subclass Actinistia (coelacanths) +Order Coelacanthiformes +Subclass Dipnoi (lungfish) +Order Ceratodontiformes + + +==== Superclass Tetrapoda: Four-limbed vertebrates ==== + + +===== Class Amphibia: Amphibians ===== + +Order Urodela or Caudata (salamanders) +Order Anura (frogs and toads) +Order Gymnophiona or Apoda (caecilians) + + +===== Class Reptilia: Reptiles ===== + + +Subclass Diapsida +Infraclass Archosauromorpha +Superorder Crocodylomorpha +Order Crocodilia (crocodilians) +Infraclass Lepidosauromorpha +Superorder Lepidosauria +Order Rhynchocephalia (tuataras) +Order Squamata (lizards, snakes) +Subclass Anapsida +Order Testudines (turtles and their kin) + + +===== Class Aves: Birds ===== + + +Subclass Neornithes +Infraclass Palaeognathae +Order Apterygiformes, kiwis +Order Casuariiformes, cassowaries and emu +Order Dinornithiformes †, moas +Order Rheiformes, rheas +Order Struthioniformes, ostriches +Order Tinamiformes, tinamous +Infraclass Neognathae +Superorder Galloanserae (fowl) +Order Anseriformes, waterfowl +Order Gastornithiformes †, gastornis and mihirungs +Order Galliformes, fowl +Superorder Neoaves +Order Sphenisciformes, penguins +Order Gaviiformes, loons +Order Podicipediformes, grebes +Order Procellariiformes, albatrosses, petrels, and allies +Order Pelecaniformes, pelicans and allies +Order Ciconiiformes, storks and allies +Order Phoenicopteriformes, flamingos +Order Accipitriformes, eagles, hawks and allies (taxonomists have traditionally placed these groups in the Falconiformes) +Order Falconiformes, falcons +Order Cariamiformes, seriemas and terror birds +Order Opisthocomiformes, hoatzin (this enigmatic bird was traditionally treated as a family within either the Galliformes or Cuculiformes) +Order Gruiformes, cranes and allies +Order Charadriiformes, plovers and allies +Order Pterocliformes, sandgrouse (this enigmatic group was traditionally treated as a family in any of three different orders: Charadriiformes, Ciconiiformes, and Columbiformes) +Order Columbiformes, doves, pigeons and dodos +Order Psittaciformes, parrots and allies +Order Cuculiformes, cuckoos +Order Strigiformes, owls +Order Caprimulgiformes, nightjars and allies +Order Apodiformes, swifts +Order Coliiformes, mousebirds +Order Trogoniformes, trogons +Order Coraciiformes, kingfishers +Order Piciformes, woodpeckers and allies +Order Passeriformes, passerines + + +===== Class Mammalia: Mammals ===== + +Subclass Prototheria +Order Monotremata, monotremes (platypus and echidnas) +Subclass Theria +Infraclass Marsupialia +Order Didelphimorphia, opossums +Order Paucituberculata, rat opossums +Order Microbiotheria, monito del monte +Order Dasyuromorphia, marsupial carnivores (quolls, numbats, Tasmanian devils and thylacines) +Order Peramelemorphia, marsupial omnivores (bandicoots and bilbies) +Order Notoryctemorphia, marsupial moles +Order Diprotodontia, marsupial herbivores; kangaroos, wallabies, possums, koalas and allies +Order Polydolopimorphia +Infraclass Eutheria +Magnorder Atlantogenata +Superorder Afrotheria +Grandorder Afrosoricida +Order Afrosoricida, tenrecs and golden moles +Order Macroscelidea, elephant shrews +Order Tubulidentata, aardvark +Grandorder Paenungulata +Order Hyracoidea, hyraxes +Mirorder Tethytheria +Order Proboscidea, elephants +Order Sirenia, manatees and dugongs +Superorder Xenarthra +Order Cingulata, armadillos +Order Pilosa, sloths and anteaters +Magnorder Boreoeutheria +Superorder Laurasiatheria +Order Eulipotyphla, hedgehogs, shrews, moles +Grandorder Ferungulata +Order Artiodactyla, cetaceans (dolphins and whales) and even-toed ungulates (giraffes, camels, pigs, cattles and deers) +Clade Pegasoferae +Order Chiroptera, bats +Mirorder Zooamata +Order Perissodactyla, odd-toed ungulates; horses, rhinos, tapirs +Clade Ferae +Order Pholidota, pangolins +Order Carnivora, carnivores; cats, dogs, bears, racoons, seals, and others +Order †Creodonta hyaenodontidae hyeanodon, dissopsalis, sarkastostodon, and megistotherium. +Superorder Euarchontoglires +Grandorder Euarchonta +Mirorder Sundatheria +Order Dermoptera, colugos +Order Scandentia, treeshrews +Mirorder Primatomorpha +Order Primates, lemurs, monkeys, apes and allies +Grandorder Glires +Order Rodentia, rodents (rats, squirrels, capybaras and beavers) +Order Lagomorpha, rabbits, hares and pikas + + +== See also == + +List of animal classes + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_clinically_important_bacteria-0.md b/data/en.wikipedia.org/wiki/List_of_clinically_important_bacteria-0.md new file mode 100644 index 000000000..a2b6791ff --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_clinically_important_bacteria-0.md @@ -0,0 +1,261 @@ +--- +title: "List of clinically important bacteria" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_clinically_important_bacteria" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:00.983680+00:00" +instance: "kb-cron" +--- + +This is a list of bacteria that are significant in medicine. For a list of clinically important viruses, see the table of viral diseases. + + +== A == +Acinetobacter baumannii +Actinomyces israelii +Agrobacterium radiobacter +Agrobacterium tumefaciens +Anaplasma +Anaplasma phagocytophilum +Azorhizobium caulinodans +Azotobacter vinelandii + + +== B == +Bacillus +Bacillus anthracis +Bacillus brevis +Bacillus cereus +Bacillus fusiformis +Bacillus licheniformis +Bacillus megaterium +Bacillus mycoides +Bacillus stearothermophilus +Bacillus subtilis +Bacillus thuringiensis +Bacteroides +Bacteroides fragilis +Bacteroides gingivalis +Bartonella +Bartonella henselae +Bartonella quintana +Bordetella +Bordetella bronchiseptica +Bordetella parapertussis +Bordetella pertussis +Borrelia burgdorferi +Brucella +Brucella abortus +Brucella melitensis +Brucella suis +Burkholderia +Burkholderia mallei +Burkholderia pseudomallei +Burkholderia cepacia + + +== C == +Calymmatobacterium granulomatis +Campylobacter +Campylobacter coli +Campylobacter fetus +Campylobacter jejuni +Capnocytophaga canimorsus +Cardiobacterium hominis +Chlamydia +Chlamydia trachomatis +Chlamydophila +Chlamydophila pneumoniae (formerly Chlamydia pneumoniae) +Chlamydophila psittaci (formerly Chlamydia psittaci) +Citrobacter +Citrobacter freundii +Citrobacter koseri +Clostridioides difficile (also known as C. diff) +Clostridium +Clostridium botulinum +Clostridium perfringens (formerly Clostridium welchii) +Clostridium tetani +Corynebacterium +Corynebacterium diphtheriae (formerly Mycobacterium diphtheriae) +Coxiella burnetii +Cutibacterium acnes (formerly Propionibacterium acnes) + + +== E == +Ehrlichia chaffeensis +Ehrlichia ewingii +Eikenella corrodens +Enterobacter cloacae +Enterococcus +Enterococcus avium +Enterococcus casseliflavus +Enterococcus durans +Enterococcus faecalis +Enterococcus faecium +Enterococcus gallinarum +Enterococcus malodoratus +Escherichia coli O157:H7 + + +== F == +Francisella tularensis (formerly Pasteurella tularensis) +Fusobacterium necrophorum +Fusobacterium nucleatum (formerly Corynebacterium fusiforme) +Frateuria aurantia (formerly Acetobacter aurantius) + + +== G == +Gardnerella vaginalis + + +== H == +Haemophilus +Haemophilus ducreyi +Haemophilus influenzae +Haemophilus parainfluenzae +Haemophilus pertussis +Haemophilus vaginalis +Helicobacter pylori + + +== K == +Kingella kingae +Klebsiella +Klebsiella granulomatis +Klebsiella pneumoniae + + +== L == +Lactobacillus +Lactobacillus acidophilus +Lactobacillus bulgaricus +Lactobacillus casei +Lactococcus lactis +Legionella pneumophila +Leptospira interrogans +Leptospira noguchii +Listeria monocytogenes + + +== M == +Methanobacterium extroquens +Micrococcus luteus +Moraxella catarrhalis +Morganella morganii +Mycobacterium +Mycobacterium avium +Mycobacterium bovis +Mycobacterium intracellulare +Mycobacterium leprae +Mycobacterium lepraemurium +Mycobacterium phlei +Mycobacterium smegmatis +Mycobacterium tuberculosis +Mycoplasma +Mycoplasma fermentans +Mycoplasma genitalium +Mycoplasma hominis +Mycoplasma penetrans +Mycoplasma pneumoniae + + +== N == +Neisseria +Neisseria gonorrhoeae +Neisseria meningitidis +Nocardia +Nocardia asteroides +Nocardia brasiliensis +Nocardia cyriacigeorgica +Nocardia farcinica + + +== P == +Pasteurella multocida +Peptostreptococcus +Porphyromonas gingivalis +Prevotella melaninogenica (formerly Bacteroides melaninogenicus) +Proteus +Proteus mirabilis +Proteus penneri +Proteus vulgaris +Pseudomonas aeruginosa + + +== R == +Rhizobium radiobacter +Rickettsia +Rickettsia prowazekii +Rickettsia psittaci +Rickettsia quintana +Rickettsia rickettsii +Rickettsia trachomae +Rochalimaea +Rochalimaea henselae +Rochalimaea quintana +Rothia dentocariosa + + +== S == +Salmonella +Salmonella enteritidis +Salmonella typhi +Salmonella typhimurium +Serratia marcescens +Shigella dysenteriae +Spirillum volutans +Staphylococcus +Staphylococcus aureus (specifically Methicillin-resistant Staphylococcus aureus) +Staphylococcus epidermidis +Stenotrophomonas maltophilia +Streptococcus +Streptococcus agalactiae +Streptococcus anginosus +Streptococcus avium +Streptococcus bovis +Streptococcus constellatus +Streptococcus cricetus +Streptococcus ferus +Streptococcus intermedius +Streptococcus lactis +Streptococcus mitior +Streptococcus mitis +Streptococcus mutans +Streptococcus oralis +Streptococcus pneumoniae +Streptococcus pyogenes +Streptococcus rattus +Streptococcus salivarius +Streptococcus sanguis +Streptococcus sobrinus +Streptomyces avermitilis + + +== U == +Ureaplasma urealyticum + + +== V == +Vibrio +Vibrio cholerae +Vibrio parahaemolyticus +Vibrio vulnificus +Viridans streptococci + + +== W == +Wolbachia + + +== Y == +Yersinia +Yersinia enterocolitica +Yersinia pestis +Yersinia pseudotuberculosis + + +== See also == +List of bacterial orders +List of bacteria genera +List of human diseases associated with infectious pathogens \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_elephant_species_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_elephant_species_by_population-0.md new file mode 100644 index 000000000..ce128d85a --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_elephant_species_by_population-0.md @@ -0,0 +1,20 @@ +--- +title: "List of elephant species by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_elephant_species_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:11.308171+00:00" +instance: "kb-cron" +--- + +This is a list of estimated global populations of elephant species (including delineated subspecies of Asian elephant). This list is generally comprehensive, but there is also uncertainty to some estimations. + + +== See also == + +Lists of organisms by population +Lists of mammals by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_endemic_species_of_Clipperton_Island-0.md b/data/en.wikipedia.org/wiki/List_of_endemic_species_of_Clipperton_Island-0.md new file mode 100644 index 000000000..450523662 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_endemic_species_of_Clipperton_Island-0.md @@ -0,0 +1,26 @@ +--- +title: "List of endemic species of Clipperton Island" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_endemic_species_of_Clipperton_Island" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:59.962941+00:00" +instance: "kb-cron" +--- + +Clipperton Island, also known as Île de la Passion, is an uninhabited French atoll in the eastern Pacific Ocean. + + +== Algae == + + +== Fish == + + +== Invertebrates == + + +== Vertebrates == + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_enzymes-0.md b/data/en.wikipedia.org/wiki/List_of_enzymes-0.md new file mode 100644 index 000000000..06e19e5b8 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_enzymes-0.md @@ -0,0 +1,209 @@ +--- +title: "List of enzymes" +chunk: 1/3 +source: "https://en.wikipedia.org/wiki/List_of_enzymes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:14.761189+00:00" +instance: "kb-cron" +--- + +Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system: + +== Category:Oxidoreductases (EC 1) (Oxidoreductase) == +Dehydrogenase +Luciferase +DMSO reductase + +=== Category:EC 1.1 (act on the CH-OH group of donors) === +Category:EC 1.1.1 (with NAD+ or NADP+ as acceptor) +Alcohol Dehydrogenase (NAD) EC 1.1.1.1 +Alcohol Dehydrogenase (NADP) EC 1.1.1.2 +Homoserine Dehydrogenase EC 1.1.1.3 +Aminopropanol Oxidoreductase EC 1.1.1.4 +Diacetyl Reductase EC 1.1.1.5 +Glycerol Dehydrogenase EC 1.1.1.6 +Propanediol-Phosphate Dehydrogenase EC 1.1.1.7 +Glycerol-3-Phoshitiendopene Dehydrogenase (NAD+) EC 1.1.1.8 +D-xylulose reductase EC 1.1.1.9 +L-xylulose reductase EC 1.1.1.10 +Lactate dehydrogenase EC 1.1.1.27 +Malate dehydrogenase EC 1.1.1.37 +Isocitrate dehydrogenase EC 1.1.1.42 +HMG-CoA reductase EC 1.1.1.88 +Category:EC 1.1.2 (with a cytochrome as acceptor) +Category:EC 1.1.3 (with oxygen as acceptor) +Glucose oxidase EC 1.1.3.4 +L-Gulonolactone oxidase EC 1.1.3.8 +Thiamine oxidase EC 1.1.3.23 +Xanthine oxidase EC 1.1.3.32 +Category:EC 1.1.4 (with a disulfide as acceptor) +Category:EC 1.1.5 (with a quinone or similar compound as acceptor) +Category:EC 1.1.99 (with other acceptors) + +=== Category:EC 1.2 (act on the aldehyde or oxo group of donors) === +Category:EC 1.2.1 (with NAD+ or NADP+ as acceptor) +Acetaldehyde dehydrogenase EC 1.2.1.10 +Glyceraldehyde 3-phosphate dehydrogenase EC 1.2.1.12 +Pyruvate dehydrogenase EC 1.2.1.51 +Category:EC 1.2.4 +Oxoglutarate dehydrogenase EC 1.2.4.2 + +=== Category:EC 1.3 (act on the CH-CH group of donors) === +Category:EC 1.3.1 (with NAD+ or NADP+ as acceptor) +Biliverdin reductase EC 1.3.1.24 +Category:EC 1.3.2 (with a cytochrome as acceptor) +Category:EC 1.3.3 (with oxygen as acceptor) +Protoporphyrinogen oxidase EC 1.3.3.4 +Category:EC 1.3.5 (with a quinone or similar compound as acceptor) +Category:EC 1.3.7 (with an iron–sulfur protein as acceptor) +Category:EC 1.3.99 (with other acceptors) + +=== Category:EC 1.4 (act on the CH-NH2 group of donors) === +Category:EC 1.4.3 +Monoamine oxidase EC 1.4.3.4 + +=== Category:EC 1.5 (act on CH-NH group of donors) === +Category:EC 1.5.1 (with NAD+ or NADP+ as acceptor) +Dihydrofolate reductase EC 1.5.1.3 +Methylenetetrahydrofolate reductase EC 1.5.1.20 +Category:EC 1.5.3 (with oxygen as acceptor) +Sarcosine oxidase EC 1.5.3.1 +(R)-6-hydroxynicotine oxidase EC 1.5.3.6 +Dihydrobenzophenanthridine oxidase EC 1.5.3.12 +Category:EC 1.5.4 (with a disulfide as acceptor) +Category:EC 1.5.5 (with a quinone or similar compound as acceptor) +Category:EC 1.5.7 (with an iron–sulfur protein as acceptor) +Category:EC 1.5.8 (with a flavin as acceptor) +Category:EC 1.5.99 (with other acceptors) + +=== Category:EC 1.6 (act on NADH or NADPH) === +Category:EC 1.6.1 (with NAD+ or NADP+ as acceptor) +Category:EC 1.6.2 (with a cytochrome as acceptor) +Category:EC 1.6.3 (with oxygen as acceptor) +Category:EC 1.6.4 now Category:EC 1.8.1 +Category:EC 1.6.5 (with a quinone or similar compound as acceptor) +NADH dehydrogenase EC 1.6.5.3 +Category:EC 1.6.6 (with a nitrogenous group as acceptor) +Category:EC 1.6.7 now Category:EC 1.18.1 +Category:EC 1.6.8 now Category:EC 1.5.1 +Category:EC 1.6.99 (with other acceptors) + +=== Category:EC 1.7 (act on other nitrogenous compounds as donors) === +Category:EC 1.7.1 (with NAD+ or NADP+ as acceptor) +Category:EC 1.7.2 (with a cytochrome as acceptor) +Category:EC 1.7.3 (with oxygen as acceptor) +Urate oxidase EC 1.7.3.3 +Category:EC 1.7.7 (with an iron–sulfur protein as acceptor) +Category:EC 1.7.99 (with other acceptors) +Nitrite reductase EC 1.7.99.3 +Nitrate reductase EC 1.7.99.4 + +=== Category:EC 1.8 (act on a sulfur group of donors) === +Category:EC 1.8.1 (with NAD+ or NADP+ as acceptor) +Glutathione reductase EC 1.8.1.7 +Thioredoxin reductase EC 1.8.1.9 +Category:EC 1.8.2 (with a cytochrome as acceptor) +Category:EC 1.8.3 (with oxygen as acceptor) +Sulfite oxidase EC 1.8.3.1 +Category:EC 1.8.4 (with a disulfide as acceptor) +Category:EC 1.8.5 (with a quinone or similar compound as acceptor) +Category:EC 1.8.6 deleted, included in EC 2.5.1.18 +Category:EC 1.8.7 (with an iron–sulfur protein as acceptor) +Category:EC 1.8.98 (with other, known, acceptors) +Category:EC 1.8.99 (with other acceptors) + +=== Category:EC 1.9 (act on a heme group of donors) === +Category:EC 1.9.3 (with oxygen as acceptor) +Cytochrome c oxidase EC 1.9.3.1 +Category:EC 1.9.6 (with a nitrogenous as acceptor) +Category:EC 1.9.99 transferred, now EC 1.9.98.1 + +=== Category:EC 1.10 (act on diphenols and related substances as donors) === +Category:EC 1.10.1(with NAD+ or NADP+ as acceptor) +Category:EC 1.10.2 (with a cytochrome as acceptor) +Coenzyme Q - cytochrome c reductase EC 1.10.2.2 +Category:EC 1.10.3 (with oxygen as acceptor) +Catechol oxidase EC 1.10.3.1 +Laccase EC 1.10.3.2 +Category:EC 1.10.99 (with other acceptors) + +=== Category:EC 1.11 (act on peroxide as an acceptor -- peroxidases) === +Category:EC 1.11.1 (peroxidases) +Cytochrome c peroxidase EC 1.11.1.5 +Catalase EC 1.11.1.6 +Myeloperoxidase EC 1.11.1.7 +Thyroid peroxidase EC 1.11.1.8 +Glutathione peroxidase EC 1.11.1.9 + +=== Category:EC 1.12 (act on hydrogen as a donor) === +Category:EC 1.12.1 (with NAD+ or NADP+ as acceptor) +Category:EC 1.12.2 (with a cytochrome as acceptor) +Category:EC 1.12.5 (with a quinone or similar compound as acceptor) +Category:EC 1.12.7 (with an iron–sulfur protein as acceptor) +Category:EC 1.12.98 (with other known acceptors) +Category:EC 1.12.99 (with other acceptors) + +=== Category:EC 1.13 (act on single donors with incorporation of molecular oxygen) === +Category:EC 1.13.11 (With incorporation of two atoms of oxygen) +4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) +Category:EC 1.13.12 (With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)) +Renilla-luciferin 2-monooxygenase EC 1.13.12.5 +Cypridina-luciferin 2-monooxygenase EC 1.13.12.6 +Firefly luciferase EC 1.13.12.7 +Watasenia-luciferin 2-monooxygenase EC 1.13.12.8 +Oplophorus-luciferin 2-monooxygenase EC 1.13.12.13 + +=== Category:EC 1.14 (act on paired donors with incorporation of molecular oxygen) === +Cytochrome P450 oxidase +Category:Cytochrome P450 +Aromatase EC 1.14.14.1 +CYP2D6 EC 1.14.14.1 +CYP2E1 EC 1.14.14.1 +CYP3A4 EC 1.14.14.1 +Cytochrome P450 oxidase +Category:EC 1.14.12 +Nitric oxide dioxygenase +Category:EC 1.14.13 +Nitric oxide synthase EC 1.14.13.39 +Category:EC 1.14.14 +Aromatase EC 1.14.14.1 +CYP2D6 EC 1.14.14.1 +CYP2E1 EC 1.14.14.1 +CYP3A4 EC 1.14.14.1 +Category:EC 1.14.16 +Phenylalanine hydroxylase EC 1.14.16.1 +Category:EC 1.14.18 +Tyrosinase EC 1.14.18.1 + +=== Category:EC 1.15 (act on superoxide radicals as acceptors) === +Category:EC 1.15.1 +Superoxide dismutase EC 1.15.1.1 + +=== Category:EC 1.16 (oxidize metal ions) === +Category:EC 1.16.3 +Ceruloplasmin EC 1.16.3.1 + +=== Category:EC 1.17 (act on CH or CH2 groups) === +Category:EC 1.17.1 +Leucoanthocyanidin reductase EC 1.17.1.3 +Xanthine dehydrogenase EC 1.17.1.4 +Nicotinate dehydrogenase EC 1.17.1.5 +4-hydroxy-tetrahydrodipicolinate reductase EC 1.17.1.8 +Category:EC 1.17.2 +Nicotinate dehydrogenase (cytochrome) EC 1.17.2.1 +Category:EC 1.17.3 +Xanthine oxidase EC 1.17.3.2 +Category:EC 1.17.4 +Ribonucleotide reductase EC 1.17.4.1 +Ribonucleoside-triphosphate reductase EC 1.17.4.2 +Vitamin K epoxide reductase +Vitamin-K-epoxide reductase (warfarin-sensitive) EC 1.17.4.4 +Vitamin-K-epoxide reductase (warfarin-insensitive) EC 1.17.4.5 +RRM1 +RRM2 +RRM2B +Category:EC 1.17.5 +Caffeine dehydrogenase EC 1.17.5.2 +Category:EC 1.17.7 +Category:EC 1.17.99 \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_enzymes-1.md b/data/en.wikipedia.org/wiki/List_of_enzymes-1.md new file mode 100644 index 000000000..694fb5fa5 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_enzymes-1.md @@ -0,0 +1,223 @@ +--- +title: "List of enzymes" +chunk: 2/3 +source: "https://en.wikipedia.org/wiki/List_of_enzymes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:14.761189+00:00" +instance: "kb-cron" +--- + +=== Category:EC 1.18 (act on iron–sulfur proteins as donors) === +Category:EC 1.18.6 +Nitrogenase EC 1.18.6.1 + +=== Category:EC 1.19 (act on reduced flavodoxin as donor) === +Category:EC 1.19.6 +Nitrogenase (flavodoxin) EC 1.19.6.1 + +=== Category:EC 1.20 (act on phosphorus or arsenic as donors) === +Category:EC 1.20.1 +Category:EC 1.20.2 +Category:EC 1.20.4 +Arsenate reductase (glutaredoxin) EC 1.20.4.1 +Glutaredoxin +Category:EC 1.20.9 +Category:EC 1.20.99 + +=== Category:EC 1.21 (act on X-H and Y-H to form an X-Y bond) === +Category:EC 1.21.1 +Iodotyrosine deiodinase EC 1.21.1.1 +Category:EC 1.21.3 +Isopenicillin N synthase EC 1.21.3.1 +Tetrahydrocannabinolic acid synthase EC 1.21.3.7 +Category:EC 1.21.4 +Category:EC 1.21.99 +Thyroxine 5-deiodinase EC 1.21.99.3 +Iodothyronine deiodinase EC 1.21.99.3 and EC 1.21.99.4 + +=== Category:EC 1.97 (other oxidoreductases) === +Category:EC 1.97.1 +Deiodinase EC 1.97.1.10 + +== Category:Transferases (EC 2) (Transferase) == +Glutathione S-transferase + +=== Category:EC 2.1 (transfer one-carbon groups, Methylase) === +Category:EC 2.1.1 +Catechol-O-methyl transferase EC 2.1.1.6 +DNA methyltransferase EC 2.1.1.72, EC 2.1.1.113, EC 2.1.1.37 +Histone methyltransferase EC 2.1.1.43, EC 2.1.1.125 +Category:EC 2.1.3 +Aspartate transcarbamoylase EC 2.1.3.2 +Ornithine transcarbamoylase EC 2.1.3.3 + +=== Category:EC 2.2 (transfer aldehyde or ketone groups) === +Category:EC 2.2.1 +Transketolase EC 2.2.1.1 +Transaldolase EC 2.2.1.2 +Acetolactate synthase EC 2.2.1.6 +2-Succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase EC 2.2.1.9 + +=== Category:EC 2.3 (acyltransferases) === +Category:EC 2.3.1 +Aminolevulinic acid synthase EC 2.3.1.37 +Choline acetyltransferase EC 2.3.1.6 +Category:EC 2.3.2 +Factor XIII EC 2.3.2.13 +Gamma glutamyl transpeptidase EC 2.3.2.2 +Transglutaminase EC 2.3.2.13 + +=== Category:EC 2.4 (glycosyltransferases) === +Category:EC 2.4.2 +Hypoxanthine-guanine phosphoribosyltransferase EC 2.4.2.8 +Category:EC 2.5 + +Category:EC 2.5.1 +Thiaminase EC 2.5.1.2 + +=== Category:EC 2.5 (transfer alkyl or aryl groups, other than methyl groups) === +Flavin prenyltransferase EC 2.5.1.129 + +=== Category:EC 2.6 (transfer nitrogenous groups) === +Category:EC 2.6.1 +4-aminobutyrate—pyruvate transaminase EC 2.6.1.96 +Alanine transaminase EC 2.6.1.2 +Aspartate transaminase EC 2.6.1.1 + +=== Category:EC 2.7 (transfer phosphorus-containing groups) === +Category:EC 2.7.2 +Butyrate kinase (EC 2.7.2.7) + +=== Category:EC 2.8 (transfer sulfur-containing groups) === +EC 2.8.1.1: Thiosulfate sulfurtransferase +EC 2.8.1.2: 3-mercaptopyruvate sulfurtransferase +EC 2.8.1.3: Thiosulfate—thiol sulfurtransferase +EC 2.8.1.4: tRNA uracil 4-sulfurtransferase +EC 2.8.1.5: Thiosulfate—dithiol sulfurtransferase +EC 2.8.1.6: Biotin synthase +EC 2.8.1.7: Cysteine desulfurase +EC 2.8.1.8: Lipoyl synthase +EC 2.8.1.9: Molybdenum cofactor sulfurtransferase +EC 2.8.1.10: Thiazole synthase +EC 2.8.1.11: Molybdopterin synthase sulfurtransferase +EC 2.8.1.12: Molybdopterin synthase +EC 2.8.1.13: tRNA-uridine 2-sulfurtransferase +EC 2.8.1.14: tRNA-5-taurinomethyluridine 2-sulfurtransferase +EC 2.8.1.15: tRNA-5-methyluridine(54) 2-sulfurtransferase + +=== Category:EC 2.9 (transfer selenium-containing groups) === +EC 2.9.1.1: L-seryl-tRNA(Sec) selenium transferase +EC 2.9.1.2: O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase + +== Category:Hydrolases (EC 3) (Hydrolase) == +Hydrolytic enzyme + +=== Category:EC 3.1 (act on ester bonds) === +Nuclease +Endonuclease +Exonuclease +Category:EC 3.1.1 +Acid hydrolase +Phospholipase A (EC 3.1.1.4) +Acetylcholinesterase (EC 3.1.1.7) +Cholinesterase (EC 3.1.1.8) +Lipoprotein lipase (EC 3.1.1.34) +Category:EC 3.1.2 +Ubiquitin carboxy-terminal hydrolase L1 (EC 3.1.2.15) +Category:EC 3.1.3 +Phosphatase +Alkaline phosphatase (EC 3.1.3.1) +Fructose bisphosphatase (EC 3.1.3.11) +Category:EC 3.1.4 +Phospholipase C (EC 3.1.4.3) +CGMP specific phosphodiesterase type 5 (EC 3.1.4.17) +Phospholipase D (EC 3.1.4.50) +Category:EC 3.1.21 +Restriction enzyme Type 1 (EC 3.1.21.3) +Restriction enzyme Type 2 (EC 3.1.21.4) +Restriction enzyme Type 3 (EC 3.1.21.5) +Restriction enzyme Type 4 (?) +Deoxyribonuclease I (EC 3.1.21.1) +Category:EC 3.1.26 +RNase H (EC 3.1.26.4) +Category:EC 3.1.27 +Ribonuclease + +=== Category:EC 3.2 (act on sugars - glycosylases) === +Category:EC 3.2.1 +Amylase (EC 3.2.1.1) +Sucrase (EC 3.2.1.10) +Chitinase (EC 3.2.1.14) +Lysozyme (EC 3.2.1.17) +Maltase (EC 3.2.1.20) +Lactase (EC 3.2.1.23) +Beta-galactosidase (EC 3.2.1.23) +Hyaluronidase (EC 3.2.1.35) + +=== Function and clinical importance of some enzymes in category 3.2.1 === + +==== Amylase ==== +Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. +Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is Sollpura (liprotamase), which help in the breakdown of saccharides into simple sugars. + +==== Lysozyme ==== +Function: An enzyme that is produced by animals that forms part of the innate immune system and is abundant in the secretions of saliva, human milk, tears, and mucus. It functions as an antimicrobial agent by splitting the peptidoglycan component of bacterial cell walls, which then leads to cell death. +Clinical Significance: Toxic levels of blood are caused by the excessive production of lysozyme's by cancer cells. Lysozyme's have also been associated with Bronchopulmonary dysplasia (BPD) in newborns and is a key factor in providing the immunology of infants during breast feeding. + +==== Sucrase ==== +Function: Sucrase is a stomachs related protein that mobilizes hydrolysis to convert sucrose into glucose and fructose. +Clinical Significance: Low amounts of Sucrose also known as Sucrose intolerance happens when sucrose isn't being discharged in the small digestive tract. A result of this is extra gas. + +==== Lactase ==== +Function: lactase is located in the small digestives system of people and other creatures such as mammals. Lactase is the bases of the total absorption of milk. +Clinical Significance: People who are lactose intolerant have medicine that can help with the digestion. When you are lactose intolerant you might experience gas, bloating, and pain along with other symptoms regarding your digestive system. + +=== Category:EC 3.3 (act on ether bonds) === +Category:EC 3.3 +Adenosylmethionine hydrolase +S-adenosyl-L-homocysteine hydrolase +Alkenylglycerophosphocholine hydrolase +Alkenylglycerophosphoethanolamine hydrolase +Cholesterol-5,6-oxide hydrolase +Hepoxilin-epoxide hydrolase +Isochorismatase +Leukotriene-A4 hydrolase +Limonene-1,2-epoxide hydrolase +Microsomal epoxide hydrolase +Trans-epoxysuccinate hydrolase + +=== Category:EC 3.4 (act on peptide bonds - Peptidase) === +Category:EC 3.4.11 +Alanine aminopeptidase +Category:EC 3.4.15 +Angiotensin converting enzyme +Category:EC 3.4.21 +Serine protease +Chymotrypsin (EC 3.4.21.1) +Trypsin (EC 3.4.21.4) +Thrombin (EC 3.4.21.5) +Factor X (EC 3.4.21.6) +Plasmin (EC 3.4.21.7) +Acrosin (EC 3.4.21.10) +Factor VII (EC 3.4.21.21) +Factor IX (EC 3.4.21.22) +Prolyl oligopeptidase (EC 3.4.21.26) +Factor XI (EC 3.4.21.27) +Elastase (EC 3.4.21.37) +Factor XII (EC 3.4.21.38) +Proteinase K (EC 3.4.21.64) +Tissue plasminogen activator (EC 3.4.21.68) +Protein C (EC 3.4.21.69) +Category:EC 3.4.22 +Separase (EC 3.4.22.49) +Category:EC 3.4.23 +Pepsin (EC 3.4.23.1) +Rennet (EC 3.4.23.4) +Renin (EC 3.4.23.15) +Trypsinogen (EC 3.4.23.18) and (20/21/23/24/26) +Plasmepsin (EC 3.4.23.39) +Category:EC 3.4.24 +Matrix metalloproteinase (EC 3.4.24.7) +Category:EC 3.4.25 +Metalloendopeptidase \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_enzymes-2.md b/data/en.wikipedia.org/wiki/List_of_enzymes-2.md new file mode 100644 index 000000000..d223132d5 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_enzymes-2.md @@ -0,0 +1,244 @@ +--- +title: "List of enzymes" +chunk: 3/3 +source: "https://en.wikipedia.org/wiki/List_of_enzymes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:14.761189+00:00" +instance: "kb-cron" +--- + +=== Category:EC 3.5 (act on carbon–nitrogen bonds, other than peptide bonds) === +Category:EC 3.5.1 (In linear amides) +Urease (EC 3.5.1.5) +Category:EC 3.5.2 (In cyclic amides) +Beta-lactamase (EC 3.5.2.6) +Category:EC 3.5.3 (In linear amidines) +Arginase (EC 3.5.3.1) +Category:EC 3.5.4 (In cyclic amidines) +Adenosine deaminase (EC 3.5.4.4) +GTP cyclohydrolase I (EC 3.5.4.16) +Category:EC 3.5.5 (In nitriles) +Nitrilase (EC 3.5.5.1) + +=== Category:EC 3.6 (act on acid anhydrides) === +Category:EC 3.6.1 +Helicase +DnaB helicase +RecQ helicase +Category:EC 3.6.3 +ATPase +NaKATPase (EC 3.6.3.9) +ATP synthase (EC 3.6.3.14) + +=== Category:EC 3.7 (act on carbon–carbon bonds) === +Kynureninase EC 3.7.1.3 + +=== Category:EC 3.8 (act on halide bonds) === +EC 3.8.1.3 Haloacetate dehalogenase + +=== Category:EC 3.9 (act on phosphorus–nitrogen bonds) === +EC 3.9.1.1: Phosphoamidase +EC 3.9.1.2: Protein arginine phosphatase +EC 3.9.1.3: Phosphohistidine phosphatase + +=== Category:EC 3.10 (act on sulfur–nitrogen bonds) === +EC 3.10.1.1: N-sulfoglucosamine sulfohydrolase +EC 3.10.1.2: Cyclamate sulfohydrolase + +=== Category:EC 3.11 (act on carbon–phosphorus bonds) === +EC 3.11.1.1: Phosphonoacetaldehyde hydrolase +EC 3.11.1.2: Phosphonoacetate hydrolase +EC 3.11.1.3: Phosphonopyruvate hydrolase + +=== Category:EC 3.12 (act on sulfur–sulfur bonds) === +EC 3.12.1.1: Trithionate hydrolase + +=== Category:EC 3.13 (act on carbon–sulfur bonds) === +EC 3.13.1.1: UDP-sulfoquinovose synthase +EC 3.13.1.3: 2'-hydroxybiphenyl-2-sulfinate desulfinase +EC 3.13.1.4: 3-sulfinopropanoyl—CoA desulfinase +EC 3.13.1.5: Carbon disulfide hydrolase +EC 3.13.1.6: (CysO sulfur-carrier protein)-S-L-cysteine hydrolase +EC 3.13.1.7: Carbonyl sulfide hydrolase +EC 3.13.1.8: S-adenosyl-L-methionine hydrolase (adenosine-forming) + +== Category:Lyases (EC 4) (Lyase) == + +=== Category:EC 4.1 (carbon–carbon lyases) === +Category:EC 4.1.1 +Ornithine decarboxylase (EC 4.1.1.17) +Uridine monophosphate synthetase (EC 4.1.1.23) +Aromatic-L-amino-acid decarboxylase (EC 4.1.1.28) +RubisCO (EC 4.1.1.39) +Category:EC 4.1.2 +Fructose-bisphosphate aldolase (EC 4.1.2.13) + +=== Category:EC 4.2 (carbon–oxygen lyases) === +Category:EC 4.2.1 +Carbonic anhydrase (EC 4.2.1.1) +Tryptophan synthase (EC 4.2.1.20) + +=== Category:EC 4.3 (carbon–nitrogen lyases) === +Category:EC 4.3.1 +Phenylalanine ammonia-lyase (EC 4.3.1.24) + +=== Category:EC 4.4 (carbon–sulfur lyases) === +Category:EC 4.4.1 +Cystathionine gamma-lyase +Cystathionine beta-lyase +Leukotriene C4 synthase + +=== Category:EC 4.5 (carbon–halide lyases) === +Category:EC 4.5.1 +Dichloromethane dehalogenase +Halohydrin dehalogenase + +=== Category:EC 4.6 (phosphorus–oxygen lyases) === +Category:EC 4.6.1 +Adenylate cyclase (EC 4.6.1.1) +Guanylate cyclase (EC 4.6.1.2) + +== Category:Isomerases (EC 5) (Isomerase) == + +=== Category:EC 5.1 (racemases and epimerases) === +Category:EC 5.1.1 +Amino-acid racemase: Phenylalanine racemase (ATP-hydrolysing) +Serine racemase +Category:EC 5.1.2 +Mandelate racemase +Category:EC 5.1.3 +UDP-glucose 4-epimerase +Category:EC 5.1.99 +Methylmalonyl CoA epimerase + +=== Category:EC 5.2 (cis-trans-isomerases) === +Category:EC 5.2 +FKBP: FKBP1A +FKBP1B +FKBP2 +FKBP3 +FKBP4 +FKBP5 +FKBP6 +FKBP8 +FKBP9 +FKBP10 +FKBPL +Cyclophilin +Parvulin +Prolyl isomerase +2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase +Beta-carotene isomerase +Farnesol 2-isomerase +Furylfuramide isomerase +Linoleate isomerase +Maleate isomerase +Maleylacetoacetate isomerase +Maleylpyruvate isomerase +Parvulin +Photoisomerase +Prolycopene isomerase +Prolyl isomerase +Retinal isomerase +Retinol isomerase +Zeta-carotene isomerase + +=== Category:EC 5.3 (intramolecular oxidoreductases) === +Category:EC 5.3.3 +Enoyl CoA isomerase (EC 5.3.3.8) +Category:EC 5.3.4 +Protein disulfide isomerase (EC 5.3.4.1) + +=== Category:EC 5.4 (intramolecular transferases -- mutases) === +Category:EC 5.4.2 +Phosphoglucomutase (EC 5.4.2.2) + +=== Category:EC 5.5 (intramolecular lyases) === + +=== Category:EC 5.99 (other isomerases) === +Category:EC 5.99.1 +Topoisomerase (type I: EC 5.99.1.2, type II: EC 5.99.1.3) + +== Category:Ligases (EC 6) (Ligase) == + +=== Category:EC 6.1 (form carbon–oxygen bonds) === +6-carboxytetrahydropterin synthase + +Category:EC 6.1.1 +FARSB (EC 6.1.1.20) + +=== Category:EC 6.2 (form carbon–sulfur bonds) === +EC 6.2.1.1: Acetate—CoA ligase +EC 6.2.1.2: Medium-chain acyl—CoA ligase +EC 6.2.1.3: Long-chain-fatty-acid—CoA ligase +EC 6.2.1.4: Succinate—CoA ligase (GDP-forming) +EC 6.2.1.5: Succinate—CoA ligase (ADP-forming) +EC 6.2.1.6: Glutarate—CoA ligase +EC 6.2.1.7: Cholate—CoA ligase +EC 6.2.1.8: Oxalate—CoA ligase +EC 6.2.1.9: Malate—CoA ligase +EC 6.2.1.10: Acid—CoA ligase (GDP-forming) +EC 6.2.1.11: Biotin—CoA ligase +EC 6.2.1.12: 4-Coumarate—CoA ligase +EC 6.2.1.13: Acetate—CoA ligase (ADP-forming) +EC 6.2.1.14: 6-carboxyhexanoate—CoA ligase +EC 6.2.1.15: Arachidonate—CoA ligase +EC 6.2.1.16: Acetoacetate—CoA ligase +EC 6.2.1.17: Propionate—CoA ligase +EC 6.2.1.18: Citrate—CoA ligase +EC 6.2.1.19: Long-chain-fatty-acid-luciferin-component ligase +EC 6.2.1.20: Long-chain-fatty-acid-(acyl-carrier-protein) ligase +EC 6.2.1.21: Transferred entry: 6.2.1.30 +EC 6.2.1.22: (citrate (pro-3S)-lyase) ligase +EC 6.2.1.23: Dicarboxylate—CoA ligase +EC 6.2.1.24: Phytanate—CoA ligase +EC 6.2.1.25: Benzoate—CoA ligase +EC 6.2.1.26: o-Succinylbenzoate—CoA ligase +EC 6.2.1.27: 4-hydroxybenzoate—CoA ligase +EC 6.2.1.28: 3-alpha,7-alpha-dihydroxy-5-beta-cholestanate—CoA ligase +EC 6.2.1.29: Transferred entry: 6.2.1.7 +EC 6.2.1.30: Phenylacetate—CoA ligase +EC 6.2.1.31: 2-furoate—CoA ligase +EC 6.2.1.32: Anthranilate—CoA ligase +EC 6.2.1.33: 4-chlorobenzoate—CoA ligase +EC 6.2.1.34: trans-Feruloyl—CoA synthase +EC 6.2.1.35: ACP-SH:acetate ligase +EC 6.2.1.36: 3-hydroxypropionyl-CoA synthase +EC 6.2.1.37: 3-hydroxybenzoate—CoA ligase +EC 6.2.1.38: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase +EC 6.2.1.39: (butirosin acyl-carrier protein)—L-glutamate ligase +EC 6.2.1.40: 4-Hydroxybutyrate—CoA ligase +EC 6.2.1.41: 3-((3aS,4S,7aS)-7a-methyl-1,5-dioxo-octahydro-1H-inden-4-yl)propanoate—CoA ligase +EC 6.2.1.42: 3-oxocholest-4-en-26-oate—CoA ligase +EC 6.2.1.43: 2-hydroxy-7-methoxy-5-methyl-1-naphthoate—CoA ligase +EC 6.2.1.44: 3-(methylthio)propionyl—CoA ligase +EC 6.2.1.45: E1 ubiquitin-activating enzyme +EC 6.2.1.46: L-allo-Isoleucine—holo-CmaA peptidyl-carrier protein ligase +EC 6.2.1.47: Medium-chain-fatty-acid-(acyl-carrier-protein) ligase +EC 6.2.1.48: Carnitine—CoA ligase +EC 6.2.1.49: Long-chain fatty acid adenylyltransferase FadD28 +EC 6.2.1.50: 4-hydroxybenzoate adenylyltransferase FadD22 +EC 6.2.1.51: 4-hydroxyphenylalkanoate adenylyltransferase FadD29 +EC 6.2.1.52: L-Firefly luciferin—CoA ligase +EC 6.2.1.53: L-Proline—L-prolyl-carrier protein ligase +EC 6.2.1.54: D-Alanine—D-alanyl-carrier protein ligase +EC 6.2.1.55: E1 SAMP-activating enzyme + +=== Category:EC 6.3 (form carbon–nitrogen bonds) === +Glutamine synthetase (EC 6.3.1.2) +Argininosuccinate synthetase (EC 6.3.4.5) +CTP synthase (EC 6.3.4.2) + +=== Category:EC 6.4 (form carbon–carbon bonds) === +Pyruvate carboxylase (EC 6.4.1.1) +Acetyl-CoA carboxylase (EC 6.4.1.2) + +=== Category:EC 6.5 (form phosphoric ester bonds) === +DNA ligase (EC 6.5.1.1) + +=== Category:EC 6.6 (form nitrogen–metal bonds) === + +== Other list of enzymes == +List of EC numbers (EC 5) +List of EC numbers (EC 6) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_even-toed_ungulates_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_even-toed_ungulates_by_population-0.md new file mode 100644 index 000000000..8b76b896b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_even-toed_ungulates_by_population-0.md @@ -0,0 +1,30 @@ +--- +title: "List of even-toed ungulates by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_even-toed_ungulates_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:12.564414+00:00" +instance: "kb-cron" +--- + +This is a list of even-toed ungulate species by estimated global population. This list is not comprehensive, as not all ungulates have had their numbers quantified. Note that this is only a subset of the order Artiodactyla, listing terrestrial species only. For populations of the cetaceans (infraorder Cetacea), see list of cetaceans. +Where available, population is given as number of mature individuals following IUCN reporting standards of estimating effective population size. + + +== Wild species by population == + + +== Domestic species by population == + + +== Species without population estimates == + + +== See also == + +Lists of mammals by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_genetically_modified_crops-0.md b/data/en.wikipedia.org/wiki/List_of_genetically_modified_crops-0.md new file mode 100644 index 000000000..3343904a1 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_genetically_modified_crops-0.md @@ -0,0 +1,63 @@ +--- +title: "List of genetically modified crops" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_genetically_modified_crops" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:42.484550+00:00" +instance: "kb-cron" +--- + +Genetically modified crops are plants used in agriculture, the DNA of which has been modified using genetic engineering techniques. In most cases, the aim is to introduce a new trait to the plant which does not occur naturally in the species. As of 2015, 26 plant species have been genetically modified and approved for commercial release in at least one country. The majority of these species contain genes that make them either tolerant to herbicides or resistant to insects. Other common traits include virus resistance, delayed ripening, modified flower colour or altered composition. In 2014, 28 countries grew GM crops, and 39 countries imported but did not grow them. + + +== Background == +Regulations regarding the commercialisation of genetically modified crops are mostly conducted by individual countries. For cultivation, environmental approval determines whether a crop can be legally grown. Separate approval is generally required to use GM crops in food for human consumption or as animal feed. +GM crops were first planted commercially on a large scale in 1996, in the US, China, Argentina, Canada, Australia, and Mexico. Some countries have approved but not actually cultivated GM crops, due to public uncertainty or further government restrictions, while at the same time, they may import GM foods for consumption. For example, Japan is a leading GM food importer, and permits but has not grown GM food crops. The European Union regulates importation of GM foods, while individual member states determine cultivation. In the US, separate regulatory agencies handle approval for cultivation (USDA, EPA) and for human consumption (FDA). +Two genetically modified crops have been approved for food use in some countries, but have not obtained approval for cultivation. A GM Melon engineered for delayed senescence was approved in 1999 and a herbicide tolerant GM wheat was approved in 2004. + + +== Genetically modified crops cultivated in 2014 == + +In 2014, 181.5 million hectares of genetically modified crops were planted in 28 countries. Half of all GM crops planted were genetically modified soybeans, either for herbicide tolerance or insect resistance. Eleven countries grew modified soybean, with the US, Brazil and Argentina accounting for 90% of the total hectarage. Of the 111 hectares of soybean grown worldwide in 2014, 82% was genetically modified in some way. Seventeen countries grew a total of 55.2 million hectares of genetically modified maize and fifteen grew 23.9 hectares of genetically modified cotton. Nine million hectares of genetically modified canola was grown with 8 million of those in Canada. Other GM crops grown in 2014 include Alfalfa (862 000 ha), sugar beet (494 000 ha) and papaya (7 475 ha). In Bangladesh a genetically modified eggplant was grown commercially for the first time on 12 ha. +The majority of GM crops have been modified to be resistant to selected herbicides, usually a glyphosate or glufosinate based one. In 2014, 154 million hectares were planted with a herbicide resistant crop and 78.8 million hectares had insect resistant. This include 51.4 million hectares planted in thirteen countries that contained both herbicide tolerance and insect resistance. Less than one million hectares contained other traits, which include providing virus resistance, delaying senescence, modifying flower colour and altering the plants composition. Drought tolerant maize was planted for just the second year in the USA on 275 000 hectares. + + +=== Herbicide tolerance === +Genetically modified crops engineered to resist herbicides are now more available than conventionally bred resistant varieties. They comprised 83% of the total GM crop area, equating to just under 8% of the arable land worldwide. Approval has been granted to grow crops engineered to be resistant to the herbicides 2,4-dichlorophenoxyacetic acid, dicamba, glufosinate glyphosate, sulfonylurea, oxynil mesotrione and isoxaflutole Most herbicide resistant GM crops have been engineered for glyphosate tolerance, in the USA 93% of soybeans and most of the GM maize grown is glyphosate tolerant. + + +=== Insect resistance === +Most currently available genes used to engineer insect resistance come from the Bacillus thuringiensis bacterium. Most are in the form of delta endotoxin genes known as cry proteins, while a few use the genes that encode for vegetative insecticidal proteins. Insect resistant crops target various species of coleopteran (beetles) and lepidopteran (moths). The only gene commercially used to provide insect protection that does not originate from B. thuringiensis is the Cowpea trypsin inhibitor (CpTI). CpTI was first approved for use cotton in 1999 and is currently undergoing trials in rice. + + +=== Stacked traits === +Many varieties of GM crops contain more than one resistance gene. This could be in the form of multiple insect resistant genes, multiple herbicide tolerance genes or a combination of the herbicide and insect resistant genes. Smartstax is a brand of GM maize that has eight different genes added to it, making it resistant to two types of herbicides and toxic to six different species of insects. + + +=== Other modified traits === +While most crops are engineered to resist insects or tolerate herbicides some crops have been developed for other traits. Flowers have been engineered to display colours that they cannot do so naturally (in particular the blue color in roses). A few crops, like the genetically modified papaya, are engineered to resist viruses. Other modifications alter the plants composition, with the aim of making it more nutritious, longer lasting or more industrially useful. Recently crops engineered to tolerate drought have been commercialised. + + +== Genetically modified crops that are no longer cultivated == + + +== Approved genetically modified crops that have not yet been cultivated == + + +== Genetically modified crops by country == + +The following graph shows the area planted in GM crops in the five largest GM crop producing countries. The area planted is presented along the y axis in thousands of hectares while the year is along the x axis. + + +=== See also === +AquAdvantage salmon + + +== References and notes == + + +=== Notes === + + +=== References === \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md b/data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md new file mode 100644 index 000000000..0b3c1d850 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md @@ -0,0 +1,91 @@ +--- +title: "List of green seaweeds of the Cape Peninsula and False Bay" +chunk: 1/2 +source: "https://en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:46.623106+00:00" +instance: "kb-cron" +--- + +This is a list of green seaweeds recorded from the oceans bordering the Cape Peninsula in South Africa from Melkbosstrand on the West Coast to Cape Hangklip on the South Coast. This list comprises locally used common names, scientific names with author citation and recorded ranges. Ranges specified may not be the entire known range for the species, but should include the known range within the waters surrounding the Republic of South Africa. +Green seaweed refers to thousands of species of macroscopic, multicellular, marine algae in the taxon Chlorophyta +The marine ecology is unusually varied for an area of this size, as a result of the meeting of two major oceanic water masses near Cape Point, and the area extends into two coastal marine bioregions. The ecology of the west or "Atlantic Seaboard" side of the Cape Peninsula is noticeably different in character and biodiversity to that of the east, or "False Bay" side. Both sides are classified as temperate waters, but there is a significant difference in average temperature, with the Atlantic side being noticeably colder on average. +List ordering and taxonomy complies where possible with the current usage in Algaebase, and may differ from the cited source, as listed citations are primarily for range or existence of records for the region. Sub-taxa within any given taxon are arranged alphabetically as a general rule. Details of each species may be available through the relevant internal links. Synonyms may be listed where useful. + +== Class: Bryopsidophyceae == + +=== Order: Bryopsidales === + +==== Family: Bryopsidaceae ==== +Bryopsis africana Areschoug, 1851, (Probably along the whole of the west Cape coast) +Bryopsis eckloniae Stegenga, Bolton & Anderson 1997, (Muizenberg, endemic) +Bryopsis hypnoides Lamouroux, 1809c, (False Bay) +Sea moss, Bryopsis myosuroides Kützing, 1856, (TMNPMPA). +Bryopsis plumosa (Hudson 1778) C. Agardh 1823, l syn. Ulva plumosa Hudson 1778, (False Bay and eastward) + +==== Family: Caulerpaceae ==== +Caulerpa bartoniae G. Murray, 1896, (Rare in Western Cape, Cape Hangklip and Muizenberg. Mainly from south coast. endemic) +Strap caulerpa Caulerpa filiformis (Suhr) Hering 1841, syn.Amphibolis filiformis Suhr 1834, Himandactylius filiformis (Suhr) Trevisan 1849, (False Bay to northern KwaZulu-Natal) +Feathery caulerpa Caulerpa holmesiana G. Murray, 1891, (Mainly a south coast species. the westernmost records at Cape of Good Hope, endemic) + +==== Family: Codiaceae ==== +Duthie's upright codium Codium duthieae Silva in Silva & Womersley, 1956, (Mainly a south and east coast species, westwards as far as Langebaan lagoon.)(From Namibia along the entire South African coast) +Fragile upright codium Codium fragile subsp. fragile (Suringar) Hariot 1889, syn Codium fragile (Suringar) Hariot subsp. capense Silva 1959a, Acanthocodium fragile Suringar 1867, (Whole of Cape west coast and most of Namibia, Eastward as far as Robberg, Plettenberg Bay) +Codium isaacii Silva, 1959a, (Namibia to Cape Peninsula, endemic) +Lucas' codium Codium lucasii Setchell subsp. capense Silva 1959a, (Strand, False Bay to southern Mozambique) +Codium papenfussii Silva, 1959a, (West coast of Cape Peninsula to southern KwaZulu-Natal, single specimen from Sodwana Bay, endemic) +Flat-lobed codium Codium platylobium Areschoug 1854, (False Bay to mouth of Mtwalume river in KwaZulu-Natal) +Stephens' codium Codium stephensiae Dickinson 1932, (St Helena Bay to Transkei, endemic) + +==== Family: Derbesiaceae ==== +Derbesia hollenbergii Taylor 1945, (Muizenberg and Strandfontein, False Bay, and Eastern Cape and Transkei) +Derbesia marina (Lyngbye) Solier 1846, syn. Vaucheria marina Lyngbye 1819, (Muizenberg, False Bay, and Eastern Cape and Transkei) + +==== Family: Udoteaceae ==== +Chlorodesmis sp. indet (Oudekraal, Cape Peninsula, endemic) + +== Class: Chlorophyceae == + +=== Order: Chaetophorales === + +==== Family: Chaetophoraceae ==== +Acrochaete sp. indet (Glencairn (False Bay) and De Hoop Nature Reserve) + +==== Family: Chroolepidaceae ==== +Sporocladopsis novae-zelandiae Chapman, 1949 (Yzerfonten to East London) + +== Class: Charophyceae == + +=== Order: Charales === + +==== Family: Characeae ==== +Foxtail stonewart, Lamprothamnium papulosum (K.Wallroth) J.Groves, 1916 (TMNPMPA) + +== Class: Ulvophyceae == + +=== Order: Cladophorales === + +==== Family: Cladophoraceae ==== +Chaetomorpha aerea (Dillwyn) Kützing 1849, syn. Conferva aerea Dillwyn 1806, Chloronitum aerea (Dillwyn) Gaillon 1828, (False Bay to Cape Agulhas) +Hair weed Chaetomorpha linum (O.F.Müller) Kützing 1845, syn. Conferva linum O.F.Müller 1778, Lychaete linum (O.F.Müller) Areschoug 1851, (Kalk Bay and Simon's Town harbours) +Robust hair-weed Chaetomorpha robusta (Areschoug) Papenfuss 1940, syn. Lychaete robusta Areschoug 1851, (Namibia to Hermanus) +Chaetomorpha sp. indet, (Clovelly, False Bay) +Cape cladophora Cladophora capensis (C.Agardh) De Toni 1889, syn. Conferva capensis C.Agardh 1824, (Namibia to southern Cape Peninsula) +Turf cladophora Cladophora contexta Levring 1938, (Olifantsbos to Lüderitz) +Cladophora dalmatica Kuetzing 1843, (Glencairn, False Bay) +Blue whip cladophora Cladophora flagelliformis (Suhr) Kützing 1849, syn. Conferva flagelliformis Suhr 1840, Lychaete flagelliformis (Suhr) Areschoug 1851, (Brandfontein to Namibia) +Cladophora isaacii Simons 1960, (Port Nolloth to Cape Hangklip) +Cladophora mirabilis (C.Agardh) Rabenhorst in Hohenacker 1852, syn. Conferva mirabilis C.Agardh 1820, (Cape Hangklip to Cape Fria, Namibia) +Cladophora radiosa (Suhr) Kützing 1889, syn. Conferva radiosa Suhr 1834, (Table Bay eastwards to Cape Morgan) +Cladophora sericia (Hudson) Kützing 1843, syn. Conferva sericea Hudson 1762, Chloronitum sericeum (Hudson) Gallion 1928, (Cape Peninsula north to Melkbosstrand, east to De Hoop nature reserve) +Cladophora sp. indet. (Clovelly to Buffels Bay, Cape Peninsula) +Rhizoclonium implexum (Dillwyn) Kützing 1845, SYN. Conferva implexa Dillwyn 1809, Rhizoclonium riparium var. implexum (Dillwyn) Rosenvinge 1893, (Kraalbaai, Langebaan lagoon and Clovelly, Cape Peninsula) + +=== Order: Ulotrichales === + +==== Family: Ulotrichaceae ==== +Ulothrix flacca (Dillwyn) Thuret in Le Jolis 1863, syn. Conferva flacca Dillwyn 1805, Lyngbya flacca (Dillwyn) Harvey 1849, (Cape Peninsula and False Bay) +Ulothrix speciosa (Carmichael) Kützing 1849, syn Ulothrix zonata var. speciosa (Carmichael) Stockmayer, Lyngbya speciosa Carmichael 1833, Hormotrichum speciosum (Carmichael) P.L.Crouan & H.M.Crouan 1852, Urospora speciosa (Carmichael) Leblond ex G.Hamel 1931, (Known from a single collection at Kalk Bay) + +=== Order: Ulvales === \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md b/data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md new file mode 100644 index 000000000..11cf1f2c3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md @@ -0,0 +1,40 @@ +--- +title: "List of green seaweeds of the Cape Peninsula and False Bay" +chunk: 2/2 +source: "https://en.wikipedia.org/wiki/List_of_green_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:46.623106+00:00" +instance: "kb-cron" +--- + +==== Family: Ulvaceae ==== +Blidingia minima (Nägeli ex Kützing) Kylin 1947, syn. Enteromorpha minima Nägeli ex Kützing 1849, Enteromorpha compressa var. minima (Nägeli ex Hauck) Hamel 1931, Enteromorpha nana var. minima (Nägeli ex Hauck) Sjøstedt 1939, (Kraalbaai, Langebaan lagoon to False Bay, and Eastern Cape) +Chloropelta caespitosa Tanner 1980, (Kalk Bay and Cape Hangklip) +Enteromorpha atroviridis (Levring) M.J.Wynne 1986, syn. Ulva atroviridis Levring 1938, (Namibia to Oudekraal, Cape Peninsula) +Percursaria percursa (C.Agardh) Rosenvinge 1893, syn. Zignoa percursa (C.Agardh) Trevisan, Conferva percursa C.Agardh 1817, Enteromorpha percursa (C.Agardh) J.Agardh 1842, (Cape Peninsula – Glencairn, Scarborough, Mouille Point) +Tangleweed, Ulva clathrata (Roth) C.Agardh, 1811, (TMNPMPA), +Ulva flexuosa Wulfen 1803, syn. Enteromorpha flexuosa (Wulfen) J.Agardh 1883, (Muizenberg and Dalebrook, False Bay and Eastern Cape) +Green sea intestines, Ulva intestinalis Linnaeus 1753, syn. Conferva intestinalis (Linnaeus) Roth 1797, Tetraspora intestinalis (Linnaeus) Desvaux 1818, Scytosiphon intestinalis (Linnaeus) Lyngbye 1819, Enteromorpha intestinalis (Linnaeus) Nees 1820, Fistularia intestinalis (Linnaeus) Greville 1824, Solenia intestinalis (Linnaeus) C.Agardh 1824, Ilea intestinalis (Linnaeus) Leiblein 1827, Hydrosolen intestinalis (Linnaeus) Martius 1833, Ulva enteromorpha var. intestinalis (Linnaeus) Le Jolis 1863, Ulva bulbosa var. intestinalis (Linnaeus) Hariot 1889, Enteromorpha compressa var. intestinalis (Linnaeus) Hamel 1931, (Widespread on west and south coasts, along entire South African coast) +Ulva lactuca Linnaeus 1753, syn. Phyllona lactuca (Linnaeus) F.H.Wiggers 1780, Ulva fasciata Delile 1813, (Saldanha Bay, False Bay eastwards into Mozambique) +Ulva linza Linnaeus 1753, syn. Solenia linza (Linnaeus) C.Agardh 1824, Enteronia linza (Linnaeus) Chevallier 1836, Phycoseris linza (Linnaeus) Kützing 1843, Enteromorpha linza (Linnaeus) J.Agardh 1883, (Namibia to False Bay) +Ulva prolifera O.F.Müller 1778, syn. Ulva enteromorpha f. prolifera (O.F.Müller) Van Heurck, Ulva compressa var. prolifera (O.F.Müller) C.Agardh 1823, Enteromorpha compressa var. prolifera (O.F.Müller) Greville 1830, Enteromorpha prolifera (O.F.Müller) J.Agardh 1883, (Namibia to Eastern Cape) +Ulva rhacodes (Holmes) Papenfuss 1960, syn. Enteromorpha rhacodes Holmes 1894, (False Bay to Eastern Cape) +Rigid sea lettuce Ulva rigida C.Agardh 1823, syn. Phycoseris rigida (C.Agardh) Kützing 1843, Ulva lactuca var. rigida (C.Agardh) Le Jolis 1863, (Cape Peninsula to tropical East Africa) +Ulva uncialis (Kützing) Montagne 1850, syn. Phycoseris uncialis Kützing 1849, Ulva capensis Areschoug 1851, (Namibia to Cape Agulhas) + +== Geographical position of places mentioned in species ranges == + +== See also == +Helderberg Marine Protected Area – Marine conservation area in the Western Cape in South Africa +List of marine invertebrates of the Cape Peninsula and False Bay – Regional biodiversity species list +List of marine vertebrates of the Cape Peninsula and False Bay – Regional biodiversity species list +List of brown seaweeds of the Cape Peninsula and False Bay – Regional biodiversity species list +List of green seaweeds of South Africa +List of red seaweeds of the Cape Peninsula and False Bay – Regional biodiversity species list +Geology of Cape Town +Table Mountain National Park – Nature conservation area on the Cape Peninsula in Cape Town, South Africa +Table Mountain National Park Marine Protected Area – Marine conservation area around the Cape Peninsula in South Africa +False Bay – Bay of the Atlantic Ocean at South Africa + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_habitats_of_principal_importance_in_Wales-0.md b/data/en.wikipedia.org/wiki/List_of_habitats_of_principal_importance_in_Wales-0.md new file mode 100644 index 000000000..89caae163 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_habitats_of_principal_importance_in_Wales-0.md @@ -0,0 +1,96 @@ +--- +title: "List of habitats of principal importance in Wales" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_habitats_of_principal_importance_in_Wales" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:43.643305+00:00" +instance: "kb-cron" +--- + +Wales is obliged by law to maintain lists of species and habitats of principal importance for biodiversity conservation; the other countries within the UK: Scotland, England and Northern Ireland, have their own laws for this purpose. +Public bodies, including local authorities now have a legal duty to have regard to conserving biodiversity in the exercise of their normal functions. In Wales, that obligation originally derived from section 42 of the Natural Environment and Rural Communities (NERC) Act 2006. However, this requirement for Wales has since been superseded by an almost identical requirement enshrined within the Environment (Wales) Act 2016. + + +== Selection == +The habitats that have been designated to be of "principal importance for the purpose of conserving biodiversity" derive from lists originally drawn up for the UK Biodiversity Action Plan (UK BAP). These lists were reviewed in 2007, and the total number of UK BAP habitats increased from 45 to 65, and the number of UK BAP species increased from under 600 to 1,150. +From these, the formal list just for Wales (and laid out below) now contains 53 of those 65 habitats. + + +=== Legal obligations === +Section 6 of the Environment (Wales) Act 2016 places a legal obligation on public bodies in Wales to 'maintain and enhance biodiversity' whilst carrying out their functions. Section 7 of that Act requires Welsh Ministers to publish and maintain lists of species and types of habitats in Wales that are regarded as of 'principal importance' for the purpose of maintaining and enhancing that biodiversity. This section of the Act replaces the biodiversity duty originally outlined in Section 42 of the NERC Act 2006 for both England and Wales. + + +=== Significance === +Awareness of the presence of any priority habitat or priority species identified on these lists is of importance within the local authority planning process when land is considered for development. Along with legally protected species, as well as statutory and non-statutory sites, knowledge of the presence of priority habitats and priority species is required if the impact of future development is to be avoided or mitigated. Planning Policy Wales indicates that, when determining planning applications, the existence of priority habitats are of greater status than others. By fully considering all these features in the decision-making process, a planning authority will have demonstrated that it has discharged its duty to conserve biodiversity. + + +== Habitats of 'principal importance' in Wales == +The list shows the broad habitat group, followed by name of the habitat of 'principal importance'. + + +=== Terrestrial, coastal & freshwater habitats === + +Arable and horticultural: Arable field margins +Bogs: Blanket bog +Bogs: Lowland raised bog +Fen, marsh and swamp: Lowland fens +Fen, marsh and swamp: Purple moor grass and rush pastures +Fen, marsh and swamp: Reedbeds +Fen, marsh and swamp: Upland flushes, fens and swamps +Grassland (acid): Lowland dry acid grassland +Grassland (calcareous): Lowland calcareous grassland +Grassland (calcareous): Upland calcareous grassland +Grassland (improved): Coastal and floodplain grazing marsh +Grassland (neutral): Lowland meadows +Heath: Lowland heathland +Heath: Upland heathland +Inland rock: Calaminarian grasslands +Inland rock: Inland rock outcrop and scree habitats +Inland rock: Limestone pavement +Inland rock: Open mosaic habitats on previously developed land +Montane habitats: Mountain heaths and willow scrub +Rivers and streams: Rivers +Standing open waters/canals: Aquifer-fed naturally fluctuating water bodies +Standing open waters/canals: Eutrophic standing waters +Standing open waters/canals: Mesotrophic lakes +Standing open waters/canals: Oligotrophic and dystrophic lakes +Standing open waters/canals: Ponds +Supralittoral rock: Maritime cliff and slopes +Supralittoral sediment: Coastal sand dunes +Supralittoral sediment: Coastal vegetated shingle +Woodland: Traditional orchards +Woodland: Wood pasture & parkland +Woodland: Hedgerows +Woodland: Lowland beech and yew woodland +Woodland: Lowland mixed deciduous woodland +Woodland: Upland mixed ash woodland +Woodland: Upland oak woodland +Woodland: Wet woodland + + +=== Marine habitats === +Littoral rock: Estuarine rocky habitats +Littoral rock: Intertidal boulder communities +Littoral rock: Sabellaria alveolata reefs +Littoral sediment: Coastal saltmarsh +Littoral sediment: Intertidal mudflats +Littoral sediment: Peat and clay exposures +Littoral sediment: Seagrass beds +Littoral sediment: Sheltered muddy gravels +Sublittoral rock: Carbonate reefs +Sublittoral rock: Fragile sponge & anthozoan communities on subtidal rocky habitats +Sublittoral rock: Tidal swept channels +Sublittoral sediment: Blue mussel beds +Sublittoral sediment: Horse mussel beds +Sublittoral sediment: Mixed muddy sediments +Sublittoral sediment: Mud habitats in deep water +Sublittoral sediment: Musculus discors beds +Sublittoral sediment: Subtidal sands and gravels + + +== See also == +List of species and habitats of principal importance in England + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_herbaria-0.md b/data/en.wikipedia.org/wiki/List_of_herbaria-0.md new file mode 100644 index 000000000..add96ed08 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_herbaria-0.md @@ -0,0 +1,50 @@ +--- +title: "List of herbaria" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_herbaria" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:49.087516+00:00" +instance: "kb-cron" +--- + +This is a list of active herbaria, organized first by continent where the herbarium is located, then within each continent by size of the collection. The list is based on the Index Herbariorum, a global directory of herbaria and their associated staff. + + +== Background == +A herbarium (plural "herbaria") is a collection of preserved plant specimens. These specimens may be whole plants or plant parts: these will usually be in a dried form, mounted on a sheet, but depending upon the material may also be kept in alcohol or other preservative. The same term is often used in mycology to describe an equivalent collection of preserved fungi and in phycology to describe a collection of algae. To preserve their form and color, plants collected in the field are spread flat on sheets of newsprint and dried, usually in a plant press, between blotters or absorbent paper. The specimens, which are then mounted on sheets of stiff white paper, are labeled with all essential data, such as collector, date and place found, description of the plant, elevation, and special habitat conditions. The sheet is then placed in a protective case. As a precaution against insect damage, the pressed plant is frozen or poisoned and the case disinfected. Most herbaria use a standard system of organizing their specimens into herbarium cases. Specimen sheets are stacked in groups by the species to which they belong and placed into a large lightweight folder that is labelled on the bottom edge. Groups of species folders are then placed together into larger, heavier folders by genus. The genus folders are then sorted by taxonomic family according to the standard system selected for use by the herbarium and placed into pigeonholes in herbarium cabinets. +Herbaria are essential for the study of plant taxonomy, the study of geographic distributions, and the stabilizing of nomenclature. Herbaria also preserve an historical record of change in vegetation over time. In some cases, plants become extinct in one area, or may become extinct altogether. In such cases, specimens preserved in an herbarium can represent the only record of the plant's original distribution. Environmental scientists make use of such data to track changes in climate and human impact. + + +== Africa == +FHI - Forestry Research Institute of Nigeria Herbarium (Ibadan, Nigeria), +BNRH - National Herbarium of Rwanda (Kigali, Rwanda), +BOL - Bolus Herbarium, University of Cape Town (Cape Town, South Africa), +EA - East African Herbarium (Nairobi, Kenya), +FHO - University of Ghana Herbarium (Legon, Ghana), +K - National Herbarium of Malawi (Blantyre, Malawi), +MO - National Herbarium of Tanzania (Arusha, Tanzania), +PRE - University of Pretoria Herbarium (Pretoria, South Africa) + + +== Asia == + + +== Australasia and Oceania == + + +== Europe == + + +== North America == +Includes herbaria in Central America and the West Indies. + + +== South America == + + +== See also == +List of botanical gardens + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_herbaria_in_Europe-0.md b/data/en.wikipedia.org/wiki/List_of_herbaria_in_Europe-0.md new file mode 100644 index 000000000..e27b455a3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_herbaria_in_Europe-0.md @@ -0,0 +1,97 @@ +--- +title: "List of herbaria in Europe" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_herbaria_in_Europe" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:44.957745+00:00" +instance: "kb-cron" +--- + +This is a list of herbaria in Europe, organized first by region where the herbarium is located (using the United Nations geoscheme for Europe), then within each region by size of the collection. For other continents, see List of herbaria. + + +== Eastern Europe == +The tables below list herbaria located in Eastern Europe as defined by the United Nations geoscheme for Europe. + + +=== Black Sea === +The following table includes herbaria located in countries on the Black Sea, including Bulgaria, Moldova, Romania, and Ukraine. + + +=== Czech Republic === +The following table includes herbaria located in the Czech Republic. + + +=== Hungary === +The following table includes herbaria located in Hungary. + + +=== Poland === +The following table includes herbaria located in Poland. + + +=== Russia === +The following table includes herbaria located in European Russia. + + +=== Ukraine === +National Herbarium of Ukraine (KW) + + +== Northern Europe == +The tables below list herbaria located in Northern Europe as defined by the United Nations geoscheme for Europe: Ireland, the British Isles, Baltic states, Scandinavia, and Iceland. + + +=== Baltic states === +The following table includes herbaria located in the Baltic states: Estonia, Latvia, and Lithuania. + + +=== Britain & Ireland === +The following table includes herbaria located in Britain & Ireland. + + +=== Nordic countries === +The following table includes herbaria located in the Nordic countries: + + +== Southern Europe == +The tables below list herbaria located in Southern Europe as defined by the United Nations geoscheme for Europe. + + +=== Balkans === +The following table includes herbaria located in the western and southern Balkans, including Albania, Greece and nations formerly part of Yugoslavia. + + +=== Italy === +The following table includes herbaria located in Italy, including Sicily and Sardinia. + + +=== Spain and Portugal === +The following table includes herbaria located in Spain and Portugal, including the Canary Islands. + + +=== Turkey === + + +== Western Europe == +The tables below list herbaria located in Western Europe as defined by the United Nations geoscheme for Europe: France, Germany, Austria, Switzerland, and the Low Countries. + + +=== Austria and Switzerland === +The following table includes herbaria located in Austria and Switzerland, as well as Liechtenstein. + + +=== France === +The following table includes herbaria located in France (including Corsica) and Monaco. + + +=== Germany === +The following table includes herbaria located in Germany. + + +=== Low Countries === +The following table includes herbaria located in Belgium, Luxembourg, Netherlands and Cyprus + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_herbaria_in_North_America-0.md b/data/en.wikipedia.org/wiki/List_of_herbaria_in_North_America-0.md new file mode 100644 index 000000000..425637310 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_herbaria_in_North_America-0.md @@ -0,0 +1,27 @@ +--- +title: "List of herbaria in North America" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_herbaria_in_North_America" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:46.406363+00:00" +instance: "kb-cron" +--- + +This is a list of herbaria in North America, organized first by country or region where the herbarium is located, then within each region by size of the collection. All herbarium codes follow the Index Herbariorum. For other continents, see List of herbaria. + + +== Canada == + + +== Central America and the Caribbean == +The table below lists herbaria located in Central America and the Caribbean. + + +== Mexico == + + +== United States == + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_herbaria_in_Turkey-0.md b/data/en.wikipedia.org/wiki/List_of_herbaria_in_Turkey-0.md new file mode 100644 index 000000000..36fff56a3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_herbaria_in_Turkey-0.md @@ -0,0 +1,33 @@ +--- +title: "List of herbaria in Turkey" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_herbaria_in_Turkey" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:47.752683+00:00" +instance: "kb-cron" +--- + +The following is a list of herbaria in Turkey. Herbaria are established within faculties and institutes of credible universities. Those created in departments that are concerned with natural sciences such as botany, ecology, biogeography and climatology are mostly used to do research on the genetics of the plants, to examine their distribution on specific geographical locations and to protect them for future generations, while those affiliated with more practice-based departments such as pharmacy are used as a resource for drug production techniques. +The first herbarium in Turkey was opened in 1933 within the Faculty of Science at Ankara University. Founded by Kurt Krause and Hikmet Birand, this herbarium is the oldest among its counterparts in the country and has the most number of species within its 200,000-piece collection. Therefore, it is also called Herbarium Turcicum (Turkish Herbarium). The Sugar Institute Herbarium, Atatürk University Faculty of Science Herbarium and Ege University Faculty of Pharmacy Herbarium are closed to visitors and scientific researchers. However, thanks to a specially created website, it is possible to access all the data related to the Ege University Faculty of Pharmacy Herbarium remotely. Altınbaş University Faculty of Pharmacy Herbarium, which opened in 2018, is the first herbarium to be established by a private university. In addition, Anadolu, Ankara, Ege, Marmara, Onsekiz Mart and Siirt universities have two herbaria each, while Hacettepe, Istanbul and Yüzüncü Yıl universities have three herbaria each. As of 2020, there are 55 herbaria in 34 different provinces of Turkey. + + +== Naming and abbreviation == +To create a herbarium, it is necessary to do a serious research, using archiving and preservation techniques. Although herbaria are usually established within universities' science and pharmacy faculties, institutions such as botanical gardens or natural history museums can also create their own collections. However, aside from preserving them for scientific studies and keeping records of them, it is important to share them with the universal scientific community. Therefore, information tags are assigned to recorded plant samples and the abbreviation of the herbarium within which they are stored is also included. The names and abbreviations of official herbaria are recorded in an international data system called Index Herbariorum, which has been in operation since 1935. While assigning international codes, the name of the city where the herbarium is located is taken into consideration, as well as the name of the institution to which it is affiliated. Herbarium abbreviations are always written in capital letters, consist of at least one and at most eight letters, and no period is added. +Thanks to this system, all herbaria that are active in the world only have a descriptive code of their own and the collections they host are transferred to a common information pool. The system, managed by the International Association for Plant Taxonomy between 1952 and 1974, has been operated by the New York Botanical Garden since 1974. As of 2020, approximately 3,100 herbaria from various countries of the world and more than 390 million samples in total were recorded in this system. + + +== List == + + +== Notes == + + +== Map == + + +== References == + + +== External links == +Index Herbariorum - New York Botanical Garden \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-0.md b/data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-0.md new file mode 100644 index 000000000..c3731380c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-0.md @@ -0,0 +1,51 @@ +--- +title: "List of honey bee pheromones" +chunk: 1/2 +source: "https://en.wikipedia.org/wiki/List_of_honey_bee_pheromones" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:07.461626+00:00" +instance: "kb-cron" +--- + +The pheromones of the honey bee are mixtures of chemical substances released by individual bees into the hive or environment that cause changes in the physiology and behaviour of other bees. + +== Introduction == +Honey bees (Apis mellifera) have one of the most complex pheromonal communication systems found in nature, possessing 15 known glands that produce an array of compounds. +These chemical messengers secreted by a queen, drone, worker bee or laying worker bee to elicit a response in other bees. The chemical messages are received by the bee's antenna and other body parts. They are produced as a volatile or non-volatile liquid and transmitted by direct contact as a liquid or vapor. +Honey bee pheromones can be grouped into releaser pheromones which temporarily affect the recipient's behavior, and primer pheromones which have a long-term effect on the physiology of the recipient. Releaser pheromones trigger an almost immediate behavioral response from the receiving bee. Under certain conditions a pheromone can act as both a releaser and primer pheromone. +The pheromones may either be single chemicals or a complex mixture of numerous chemicals in different percentages. + +== Types of honey bee pheromones == + +=== Alarm pheromone === +Two main alarm pheromones have been identified in honeybee workers. One is released by the Koschevnikov gland, near the sting shaft, and consists of more than 40 chemical compounds, including isopentyl acetate (IPA), butyl acetate, 1-hexanol, n-butanol, 1-octanol, hexyl acetate, octyl acetate, n-pentyl acetate and 2-nonanol. These chemical compounds have low molecular weights, are highly volatile, and appear to be the least specific of all pheromones. Alarm pheromones are released when a bee stings another animal, and attract other bees to the location and causes the other bees to behave defensively, i.e. sting or charge. The alarm pheromone emitted when a bee stings another animal smells like bananas. Smoke can mask the bees' alarm pheromone. +The other alarm pheromone is released by the mandibular glands and consists of 2-heptanone, which is also a highly volatile substance. This compound has a repellent effect and it was proposed that it is used to deter potential enemies and robber bees. The amounts of 2-heptanone increase with the age of bees and becomes higher in the case of foragers. It was therefore suggested that 2-heptanone is used by foragers to scent-mark recently visited and depleted foraging locations, which indeed are avoided by foraging bees. +However, this has recently been proven false. In a new discovery, it was determined that bees actually use 2-heptanone as an anesthetic and to paralyze intruders. After the intruders are paralyzed, the bees remove them from the hive. + +=== Brood recognition pheromone === +Another pheromone is responsible for preventing worker bees from bearing offspring in a colony that still has developing young. Both larvae and pupae emit a "brood recognition" pheromone. This inhibits ovarian development in worker bees and helps nurse bees distinguish worker larvae from drone larvae and pupae. This pheromone is a ten-component blend of fatty-acid esters, which also modulates adult caste ratios and foraging ontogeny dependent on its concentration. The components of brood pheromone have been shown to vary with the age of the developing bee. An artificial brood pheromone was invented by Yves Le Conte, Leam Sreng, Jérome Trouiller, and Serge Henri Poitou and patented in 1996. + +=== Drone pheromone === +Drone Mandibular Pheromone attracts other flying drones to suitable sites for mating with virgin queens. + +=== Dufour's gland pheromone === +The Dufour's gland (named after the French naturalist Léon Jean Marie Dufour) opens into the dorsal vaginal wall. Dufour’s gland and its secretion have been somewhat of a mystery. The gland secretes its alkaline products into the vaginal cavity, and it has been assumed to be deposited on the eggs as they are laid. Indeed, Dufour’s secretions allow worker bees to distinguish between eggs laid by the queen, which are attractive, and those laid by workers. The complex of as many as 24 chemicals differs between workers in "queenright" colonies and workers of queenless colonies. In the latter, the workers’ Dufour secretions are similar to those of a healthy queen. The secretions of workers in queenright colonies are long-chain alkanes with odd numbers of carbon atoms, but those of egg-laying queens and egg-laying workers of queenless colonies also include long chain esters. + +=== Egg marking pheromone === +This pheromone, similar to that described above, helps nurse bees distinguish between eggs laid by the queen bee and eggs laid by a laying worker. + +=== Footprint pheromone === +This pheromone is left by bees when they walk and is useful in enhancing Nasonov pheromones in searching for nectar. +In the queen, it is an oily secretion of the queen's tarsal glands that is deposited on the comb as she walks across it. This inhibits queen cell construction (thereby inhibiting swarming), and its production diminishes as the queen ages. + +=== Forager pheromone === +Ethyl oleate is released by older forager bees to slow the maturing of nurse bees. This primer pheromone acts as a distributed regulator to keep the ratio of nurse bees to forager bees in the balance that is most beneficial to the hive. + +=== Nasonov pheromone === +Nasonov pheromone is emitted by the worker bees and used for orientation and recruitment. Nasonov pheromone includes a number of terpenoids including geraniol, nerolic acid, citral and geranic acid. + +=== Other pheromones === +Other pheromones produced by most honey bees include rectal gland pheromone, tarsal pheromone, wax gland and comb pheromone, and tergite gland pheromone. + +== Types of queen honey bee pheromones == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-1.md b/data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-1.md new file mode 100644 index 000000000..a70e3bd87 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_honey_bee_pheromones-1.md @@ -0,0 +1,48 @@ +--- +title: "List of honey bee pheromones" +chunk: 2/2 +source: "https://en.wikipedia.org/wiki/List_of_honey_bee_pheromones" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:07.461626+00:00" +instance: "kb-cron" +--- + +=== Queen mandibular pheromone === +Queen mandibular pheromone (QMP), emitted by the queen, is one of the most important sets of pheromones in the bee hive. It affects social behavior, maintenance of the hive, swarming, mating behavior, and inhibition of ovary development in worker bees. The effects can be short term or long term or both. Some of the chemicals found in QMP are carboxylic acids and aromatic compounds. The following compounds have been shown to be important in retinue attraction of workers to their queen and other effects. + +(E)-9-Oxodec-2-enoic acid (9-ODA) – inhibits queen rearing as well as ovarian development in worker bees; strong sexual attractant for drones when on a nuptial flight; critical to worker recognition of the presence of a queen in the hive +(R,E)-(−)-9-Hydroxydec-2-enoic acid] (-9-HDA) promotes stability of a swarm, or a "calming" influence +(S,E)-(+)-9-Hydroxydec-2-enoic acid (+9-HDA) +Methylparaben (also known as methyl p-hydroxybenzoate) (HOB) +4-Hydroxy-3-methoxy phenylethanol (HVA) +Work on synthetic pheromones was done by Keith N. Slessor, Lori-ann Kaminski, Gaylord G. S. King, John H. Borden, and Mark L. Winston; their work was patented in 1991. Synthetic queen mandibular pheromone (QMP) is a mixture of five components: 9-ODA, (−)-9-HDA, (+)-9-HDA, HOB and HVA in a ratio of 118:50:22:10:1. + +=== Queen retinue pheromone === +The following compounds have also been identified, of which only coniferyl alcohol is found in the mandibular glands. The combination of the 5 QMP compounds and the 4 compounds below is called the queen retinue pheromone (QRP). These nine compounds are important for the retinue attraction of worker bees around their queen. + +Methyl oleate +Coniferyl alcohol +Cetyl alcohol +α-Linolenic acid + +=== Other === +The queen also contains an abundance of various methyl and ethyl fatty acid esters, very similar to the brood recognition pheromone described above. They are likely to have pheromonal functions like those found for the brood recognition pheromone. + +== References listed alphabetically by author == +Imrie, George Georg Imrie's, Pink Pages Nov. 1999 +Katzav-Gozansky Tamar (2002). "Review" (PDF). Apidologie. 33: 525–537. doi:10.1051/apido:2002035. +Blum, M.S. 1992. Honey bee pheromones in The Hive and the Honey Bee, revised edition (Dadant and Sons: Hamilton, Illinois), pages 385–389. +Boch R., Shearer D.A. (1971). "Chemical releasers of alarm behaviour on the honey-bee, Apis mellifera". Journal of Insect Physiology. 17 (12): 2277–2285. Bibcode:1971JInsP..17.2277B. doi:10.1016/0022-1910(71)90077-1. +Butler, C. 1609. The Feminine Monarchie. On a Treatise Concerning Bees, and the Due Ordering of them. Joseph Barnes: Oxford. +Free, John B., Pheromones of social bees. Ithaca, N.Y.: Comstock, 1987. +Imrie, George George Imrie's Pink Pages November 1999 accessed Feb. 2005 +Keeling C. I., Slessor K. N., Higo H. A., Winston M. L. (2003). "New components of the honey bee (Apis mellifera L.) queen retinue pheromone". Proceedings of the National Academy of Sciences. 100 (8): 4486–4491. Bibcode:2003PNAS..100.4486K. doi:10.1073/pnas.0836984100. PMC 153582. PMID 12676987.{{cite journal}}: CS1 maint: multiple names: authors list (link) +Leoncini I., Le Conte Y., Costagliola G., Plettner E., Toth A. L., Wang M., Huang Z., Bécard J.-M., Crauser D., Slessor K. N., Robinson G. E. (2004). "Regulation of behavioral maturation by a primer pheromone produced by adult worker honey bees". Proceedings of the National Academy of Sciences. 101 (50): 17559–17564. doi:10.1073/pnas.0407652101. PMC 536028. PMID 15572455.{{cite journal}}: CS1 maint: multiple names: authors list (link) +Maschwitz U (1964). "Alarm substances and alarm behavior in social Hymenoptera". Nature. 204 (4956): 324–327. Bibcode:1964Natur.204..324M. doi:10.1038/204324a0. S2CID 4271328. +Moritz, Burgin H (1987). "Group response to alarm pheromones in socialwasps and the honeybees". Ethology. 76 (1): 15–26. Bibcode:1987Ethol..76...15M. doi:10.1111/j.1439-0310.1987.tb00668.x. +Slessor K. N., Kaminski L.-A., King G. G. S., Borden J. H., Winston M. L. (1988). "Semiochemical basis of the retinue response to queen honey bees". Nature. 332 (6162): 354–356. Bibcode:1988Natur.332..354S. doi:10.1038/332354a0. S2CID 4362366.{{cite journal}}: CS1 maint: multiple names: authors list (link) +Vander Meer, R.K. et al. 1998. Pheromone Communication in Social Insects; Boulder: Westview Press +Wager B.R., Breed M.D. (2000). "Does honeybee sting alarm pheromone give orientation information to defensive bees?". Annals of the Entomological Society of America. 3 (6): 1329–1332. doi:10.1603/0013-8746(2000)093[1329:DHBSAP]2.0.CO;2. + +== Notes == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_blood_components-0.md b/data/en.wikipedia.org/wiki/List_of_human_blood_components-0.md new file mode 100644 index 000000000..afac5a041 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_blood_components-0.md @@ -0,0 +1,18 @@ +--- +title: "List of human blood components" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_blood_components" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:50.504785+00:00" +instance: "kb-cron" +--- + +In blood banking, the fractions of Whole Blood used for transfusion are also called components. + + +== See also == +Reference ranges for common blood tests + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_1-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_1-0.md new file mode 100644 index 000000000..bf89f2994 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_1-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 1" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_1" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:19.166650+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_2-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_2-0.md new file mode 100644 index 000000000..a26678ce0 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_2-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 2" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_2" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:20.987854+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_3-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_3-0.md new file mode 100644 index 000000000..b7dd4e613 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_3-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 3" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_3" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:22.458279+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_4-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_4-0.md new file mode 100644 index 000000000..0698e76cf --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_4-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 4" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_4" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:23.997279+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_5-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_5-0.md new file mode 100644 index 000000000..a532164fb --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_5-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 5" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_5" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:25.748051+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_6-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_6-0.md new file mode 100644 index 000000000..1cefec33d --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_6-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 6" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_6" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:27.481067+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_7-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_7-0.md new file mode 100644 index 000000000..cbde80878 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_7-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 7" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_7" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:29.324164+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_8-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_8-0.md new file mode 100644 index 000000000..fb6966c94 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_8-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 8" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_8" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:31.255835+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_9-0.md b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_9-0.md new file mode 100644 index 000000000..af3be372f --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_protein-coding_genes_9-0.md @@ -0,0 +1,12 @@ +--- +title: "List of human protein-coding genes 9" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_protein-coding_genes_9" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:32.804820+00:00" +instance: "kb-cron" +--- + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_human_transcription_factors-0.md b/data/en.wikipedia.org/wiki/List_of_human_transcription_factors-0.md new file mode 100644 index 000000000..0e5408827 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_human_transcription_factors-0.md @@ -0,0 +1,22 @@ +--- +title: "List of human transcription factors" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_human_transcription_factors" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:52.034125+00:00" +instance: "kb-cron" +--- + +This list of manually-curated human transcription factors is taken from Lambert, Jolma, Campitelli, et al. +More detailed information can be found in the manuscript and accompanying web site. + + +== List of human transcription factors (1639) == + + +== External links == +https://humantfs.ccbr.utoronto.ca + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_immune_cells-0.md b/data/en.wikipedia.org/wiki/List_of_immune_cells-0.md new file mode 100644 index 000000000..c7f8a359b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_immune_cells-0.md @@ -0,0 +1,14 @@ +--- +title: "List of immune cells" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_immune_cells" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:53.612657+00:00" +instance: "kb-cron" +--- + +This is a list of immune cells, also known as white blood cells, white cells, leukocytes, or leucocytes. They are cells involved in protecting the body against both infectious disease and foreign invaders. + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_institutes_and_centers_of_the_National_Institutes_of_Health-0.md b/data/en.wikipedia.org/wiki/List_of_institutes_and_centers_of_the_National_Institutes_of_Health-0.md new file mode 100644 index 000000000..201166033 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_institutes_and_centers_of_the_National_Institutes_of_Health-0.md @@ -0,0 +1,46 @@ +--- +title: "List of institutes and centers of the National Institutes of Health" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_institutes_and_centers_of_the_National_Institutes_of_Health" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:27.533947+00:00" +instance: "kb-cron" +--- + +The National Institutes of Health (NIH) is an agency of the United States Department of Health and Human Services and is the primary agency of the United States government responsible for biomedical and health-related research. It comprises 27 separate institutes and centers (ICs) that carry out its mission in different areas of biomedical research. It also includes the Office of the Director, which sets policies and coordinates activities of the 27 ICs. + + +== Institutes == + + +== Centers of the NIH == +In addition to being divided by research area, NIH has many operating groups called centers operating across all of the Institutes. + + +== Office of the Director == +The Office of the Director is the central office at NIH. The OD is responsible for setting policy for NIH and for planning, managing, and coordinating the programs and activities of all the NIH components. Program offices in the Office of the Director are responsible for stimulating specific areas of research throughout NIH and for planning and supporting research and related activities. Current program areas are: minority health, women's health, AIDS research, disease prevention, and behavioral and social sciences research. In July 2009, President Barack Obama nominated Dr. Francis S. Collins, M.D., PhD, to be the Director of the NIH. On August 7, 2009, the US Senate confirmed Collins by a unanimous vote. +Program offices within the Office of the Director fund research through the institutes: + + +== Other entities in NIH == + + +=== ARPA-H === + +The Advanced Research Projects Agency for Health (ARPA-H) is an entity formerly within the Office of the United States Secretary of Health and Human Services, which was created by Congress in the Consolidated Appropriations Act, 2022. Modeled after DARPA, HSARPA, IARPA, and ARPA-E, it is intended to pursue unconventional research projects through methods not typically used by federal agencies or private sector companies. Secretary Xavier Becerra delegated ARPA-H to the NIH on May 24, 2022. It received $1 billion in appropriations in 2022, and $1.5 billion in 2023, and as of June 2023 it is requesting $2.5 billion for 2024. + + +== See also == +List of Max Planck Institutes +Center of Advanced European Studies and Research +Ernst Strüngmann Institute +List of IBS Centers + + +== References == + + +== External links == + Media related to National Institutes of Health institutes and centers at Wikimedia Commons +Institutes at NIH \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_interstitial_cells-0.md b/data/en.wikipedia.org/wiki/List_of_interstitial_cells-0.md new file mode 100644 index 000000000..0d134294c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_interstitial_cells-0.md @@ -0,0 +1,27 @@ +--- +title: "List of interstitial cells" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_interstitial_cells" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:54.838208+00:00" +instance: "kb-cron" +--- + +Interstitial cell refers to any cell that lies in the spaces between the functional cells of a tissue. +Examples include: + +Interstitial cell of Cajal (ICC) +Leydig cells, cells present in the male testes responsible for the production of androgen (male sex hormone) +A portion of the stroma of ovary +Certain cells in the pineal gland +Renal interstitial cells +Neuroglial cells + + +== See also == +List of human cell types derived from the germ layers + + +== References == +Sybil B Parker (ed). "Interstitial cell". McGraw Hill Dictionary of Scientific and Technical Terms. Fifth Edition. International Edition. 1994. Page 1041. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-0.md b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-0.md new file mode 100644 index 000000000..0f5713f89 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-0.md @@ -0,0 +1,25 @@ +--- +title: "List of longest-living organisms" +chunk: 1/5 +source: "https://en.wikipedia.org/wiki/List_of_longest-living_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:08.624136+00:00" +instance: "kb-cron" +--- + +This is a list of the longest-living biological organisms: the individuals or clones of a species with the longest natural maximum life spans. For a given species, such a designation may include: + +The oldest known individual(s) that are currently alive, with verified ages. +Verified individual record holders, such as the longest-lived human, Jeanne Calment, or the longest-lived domestic cat, Creme Puff. +The definition of "longest-living" used in this article considers only the observed or estimated length of an individual organism's natural lifespan – that is, the duration of time between its birth or conception (or the earliest emergence of its identity as an individual organism) and its death – and does not consider other conceivable interpretations of "longest-living", such as the length of time between the earliest appearance of a species in the fossil record and the present day (the historical "age" of the species as a whole) or the time between a species' first speciation and its extinction (the phylogenetic "lifespan" of the species). This list includes long-lived organisms that are currently still alive as well as those that have already died. +Determining the length of an organism's natural lifespan is complicated by many problems of definition and interpretation, as well as by practical difficulties in reliably measuring age, particularly for extremely old organisms and for those that reproduce by asexual reproduction or cloning. In many cases the ages listed below are estimates based on observed present-day growth rates, which may differ significantly from the growth rates experienced thousands of years ago. Identifying the longest-living organisms also depends on defining what constitutes an "individual" organism, which can be problematic, since many asexual organisms and clonal colonies defy one or both of the traditional colloquial definitions of individuality (having a distinct genotype, and having an independent, physically separate body). Additionally, some organisms maintain the capability to reproduce through very long periods of metabolic dormancy, during which they may not be considered "alive" by certain definitions but nonetheless can resume normal metabolism afterward; it is unclear whether the dormant periods should be counted as part of the organism's lifespan. + +== Biological immortality == + +If the mortality rate of a species does not increase after maturity, the species does not age and is said to be biologically immortal. There are numerous plants and animals for which the mortality rate has been observed to actually decrease with age, for all or part of the life cycle. Specimens of the cnidarian genus Hydra were observed for four years without any increase in mortality rate. If the mortality rate remains constant, the rate determines the mean lifespan. The lifespan may be long or short, though the species technically does not "age" in the biological sense. +Individuals of other species have been observed to regress to a larval state and regrow into adults multiple times. The hydrozoan species Turritopsis dohrnii (formerly Turritopsis nutricula) is capable of cycling from a mature adult stage to an immature polyp stage and back again. This means no natural limit to its lifespan is known. No single specimen has been observed for any extended period, however, and estimating the age of a specimen is not possible by any known means. At least one other hydrozoan (Laodicea undulata), one scyphozoan (Aurelia sp. 1) and one tentaculata (Mnemiopsis leiydi) can also revert from a medusa stage into a polyp stage. +Similarly, the larvae of skin beetles undergo a degree of "reversed development" when starved, and later grow back to the previously attained level of maturity. This cycle can be repeated many times. However, repeated cycles result in physiological deterioration, suggesting that these beetle larvae still age. + +== Revival after dormancy == +If the definition of lifespan does not exclude time spent in metabolically inactive states, many organisms may be said to have lifespans that are millions of years in length. Various claims have been made about reviving bacterial spores to active metabolism after millions of years of dormancy. Spores preserved in amber have been revived after 40 million years, and spores from salt deposits in the Salado Formation of New Mexico have been revived after 250 million years, making these bacteria by far the longest-living organisms ever recorded. Similarly, in May 2022 prokaryotic and eukaryotic microorganisms were found in crystals of halite; these could be over 800 million years old but it remains uncertain if they are alive or if they could be revived. In a related find, a scientist was able to coax 34,000-year-old salt-captured bacteria to reproduce. These results were subsequently duplicated independently. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-1.md b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-1.md new file mode 100644 index 000000000..4ad24540b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-1.md @@ -0,0 +1,38 @@ +--- +title: "List of longest-living organisms" +chunk: 2/5 +source: "https://en.wikipedia.org/wiki/List_of_longest-living_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:08.624136+00:00" +instance: "kb-cron" +--- + +In July 2018, scientists from four Russian institutions collaborating with Princeton University reported that they had analyzed about 300 prehistoric nematode worms recovered from permafrost above the Arctic Circle in the Sakha Republic, and that after being thawed, two of the nematodes revived and began moving and eating. One found in a Pleistocene squirrel burrow in the Duvanny Yar outcrop on the Kolyma River was believed to be about 32,000 years old, while the other, recovered in 2015 near the Alazeya River, was dated at approximately 30,000–40,000 years old. These nematodes were believed to be the oldest living non-clonal multicellular organisms on Earth. In 2021, biologists reported the restoration of bdelloid rotifers frozen for 24,000 years in the Siberian permafrost. In 2023, it was reported that nematodes of the previously undescribed Panagrolaimus kolymaensis were revived after 46,000 years in cryptobiosis. +Like bacterial spores, plant seeds are often capable of germinating after very long periods of metabolic inactivity. A seed from the previously extinct Judean date palm was revived and managed to sprout after nearly 2,000 years. Named "Methuselah", it is currently growing at Kibbutz Ketura, Israel. Similarly, the flowering plant Silene stenophylla was grown from frozen fruit found in an ancient squirrel's cache. The germinated plants bore viable seeds. The fruit was dated at 31,800 ± 300 years old. In 1994, a seed from a sacred lotus (Nelumbo nucifera), dated at roughly 1,300 ± 270 years old, was successfully germinated. In 2024, a never-before-seen species of Commiphora was grown from a successfully germinated seed that is estimated to be 1,000 years old. +During the 1990s, Raul Cano, a microbiologist at California Polytechnic State University, San Luis Obispo, US, reported reviving yeast trapped in amber for 25 million years, although doubts were raised as to its antiquity. Cano founded a brewery and crafted an "amber ale" with a 45-million-year-old variant of Saccharomyces cerevisiae. + +== List of longest-living organisms == + +=== Microorganisms === + +Some endoliths have extremely long lives. In August 2013, researchers reported evidence of endoliths in the ocean floor, perhaps millions of years old, with a generation time of 10,000 years. These are slowly metabolizing and not in a dormant state. Some Actinomycetota found in Siberia are estimated to be half a million years old. +In July 2020, marine biologists reported that aerobic microorganisms (mainly), in "quasi-suspended animation", were found in organically poor sediments 68.9 metres (226 feet) below the seafloor in the South Pacific Gyre (SPG) ("the deadest spot in the ocean"). The sediments had been dated by previous research using cobalt-based techniques to 4.3 to 101.5 million years old, which would make them the longest-living life forms ever found, yet in October 2024, scientists reported aerobic microorganisms in a two billion-year-old rock drilled from 15 meters underground within a formation known as the Bushveld Igneous Complex in northeastern South Africa, though the age of the microorganisms is unknown. + +=== Clonal plant and fungal colonies === + +As with all long-lived plant and fungal species, no individual part of a clonal colony is alive (in the sense of active metabolism) for more than a very small fraction of the life of the entire colony. Some clonal colonies may be fully connected via their root systems, while most are not interconnected but are nonetheless genetically identical clones that populated an area through vegetative reproduction. Ages for clonal colonies are estimates, often based on current growth rates. + +A huge colony of the sea grass Posidonia oceanica in the Mediterranean Sea near Ibiza, Spain, is estimated to be between 12,000 and 200,000 years old. The maximum age is theoretical, as the region it now occupies was dry land at some point between 10,000 and 80,000 years ago. +The sole surviving clonal colony of the shrub Lomatia tasmanica in Tasmania is estimated to be at least 43,600 years old. +The Jurupa Oak colony in Riverside County, California, United States, is estimated to be at least 13,000 years old. Other estimates place it at 5,000 to 30,000 years old. +Eucalyptus recurva clones in Australia have been claimed to be 13,000 years old. +A box huckleberry bush in Perry County, Pennsylvania, United States, is thought to be around 13,000 years old. If true, it would predate human settlements in the area. +King Clone is an individual creosote bush (Larrea tridentata) in the Mojave Desert of southern California, United States, estimated at 11,700 years old. Another creosote bush has been said to be 12,150 years old, but this is as yet unconfirmed. +A Huon pine colony on Mount Read, Tasmania, is estimated at 10,000 years old, with individual specimens living over 3,000 years. +Old Tjikko, a Norway spruce tree in the county of Dalarna, Sweden, is living on top of roots that have been radiocarbon-dated to 9,550 years old. The tree is part of a clonal colony that was established at the end of the last ice age. Discovered by Professor Leif Kullman of Umeå University, Old Tjikko is small, only 5 m (16 ft) in height. +Pando is a clonal colony of Populus tremuloides (quaking aspen) trees in south-central Utah, United States, that is estimated to be several thousand years old, possibly as much as 14,000 years. Unlike many other clonal "colonies", Pando's above-ground tree trunks remain connected to each other by a single massive subterranean root system. +"Humongous Fungus", an individual of the clonal subterranean fungal species Armillaria solidipes in Oregon's Malheur National Forest, is thought to be between 2,000 and 8,500 years old. Apart from its extreme age, it is also thought to be the world's largest organism by area, at 2,384 acres (965 hectares). +A huge colony of the sea grass Posidonia australis in the Australian coast over Shark Bay is estimated to be over 4,500 years old and also the world's largest known plant. + +=== Individual plant specimens === \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-2.md b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-2.md new file mode 100644 index 000000000..095a1fc58 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-2.md @@ -0,0 +1,37 @@ +--- +title: "List of longest-living organisms" +chunk: 3/5 +source: "https://en.wikipedia.org/wiki/List_of_longest-living_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:08.624136+00:00" +instance: "kb-cron" +--- + +Methuselah, a Great Basin bristlecone pine (Pinus longaeva) in the White Mountains of California, has been measured by ring count to be 4,857 years old. It is therefore the oldest known living individual non-clonal tree in the world. +A specimen of Fitzroya cupressoides in Chile was measured by ring count as 3,655 years old, meaning this species has the second-oldest verified age of any non-clonal tree species. +The Cypress of Abarkuh, a Mediterranean cypress (Cupressus sempervirens) in Iran, is estimated to be between 4,000 and 5,000 years old. + +The Llangernyw Yew, an ancient yew (Taxus baccata) in the churchyard of the village of Llangernyw in North Wales, is believed to be between 4,000 and 5,000 years old. +The President, located in Sequoia National Park, California, is the oldest known living giant sequoia (Sequoiadendron giganteum) at approximately 3,200 years of age. +Yareta is a tiny flowering plant in the family Apiaceae native to South America, occurring in the Puna grasslands of the Andes in Peru, Bolivia, northern Chile, and western Argentina between 3,200 and 4,500 metres (10,500 and 14,800 ft) in altitude. Some yaretas may be up to 3,000 years old. +A Panke baobab (Adansonia digitata) in Zimbabwe was some 2,450 years old when it died in 2011, making it the oldest angiosperm ever documented, and two other trees of the same species – Dorslandboom in Namibia and Glencoe in South Africa – were estimated to be approximately 2,000 years old. +A sacred fig (Ficus religiosa), the Jaya Sri Maha Bodhi in Anuradhapura, Sri Lanka, is 2,313 years old, having been planted in 288 BC. It is the oldest known living human-planted tree in the world. +The Great sugi of Kayano, the cryptomeria deemed planted by humans in Kaga, Ishikawa, Japan, had an estimated age of 2,300 years in 1928. +Jōmon Sugi, the cryptomeria naturally grown in Yakushima Island, Kagoshima, Japan, is 2,170 to 7,200 years old. +A specimen of Lagarostrobos franklinii in Tasmania is thought to be about 2,000 years old. +The Fortingall Yew, an ancient yew (Taxus baccata) in the churchyard of the village of Fortingall in Perthshire, Scotland, is one of the oldest known individual trees in Europe. Various estimates have put its age between 2,000 and 5,000 years, although it is now believed to be at the lower end of this range. +Numerous olive trees are purported to be 2,000 years old or older. An olive tree in Ano Vouves, Crete, claiming such longevity, has been confirmed based on tree-ring analysis. Stara Maslina (Old Olive Tree) near Stari Bar in Montenegro, is estimated to be over 2,200 years old. +Tāne Mahuta, a kauri tree (Agathis australis) in New Zealand, is believed to be between 1,250 and 2,500 years old. It is the oldest and largest standing kauri tree at present. +Welwitschia is a monotypic genus of gymnosperm plant, composed solely of the distinct Welwitschia mirabilis. The plant is considered a living fossil. Radiocarbon dating has confirmed that many individuals have lived longer than 1,000 years, and some are suspected to be older than 2,000 years. +Old Tjikko, the world's oldest known Norway spruce in Sweden, continues via vegetative cloning. Although its trunk may be only a few centuries old, its root system is estimated to be 9,568 years old. + +=== Aquatic animals === +Glass sponges found in the East China Sea and Southern Ocean have been estimated to be more than 10,000 years old. Although this may be an overestimate, this is likely the longest lived animal on Earth. +Specimens of the black coral genus Leiopathes, such as Leiopathes glaberrima, are among the oldest continuously living organisms on the planet: around 4,265 years old. + +The giant barrel sponge Xestospongia muta is one of the longest-lived animals, with the largest specimens in the Caribbean estimated to be more than 2,300 years old. +The black coral Antipatharia in the Gulf of Mexico may live more than 2,000 years. +The Antarctic sponge Cinachyra antarctica has an extremely slow growth rate in the low temperatures of the Southern Ocean. One specimen has been estimated to be 1,550 years old. +A specimen, "Ming" of the Icelandic cyprine Arctica islandica (also known as an ocean quahog), a mollusk, was found to have lived 507 years. Another specimen had a recorded lifespan of 374 years. +The tubeworm Escarpia laminata that lives in deep sea cold seeps regularly reaches the age of between 100 and 200 years, with some individuals determined to be more than 300 years old. Some may live for over 1,000 years. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-3.md b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-3.md new file mode 100644 index 000000000..7d5ee1dca --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-3.md @@ -0,0 +1,40 @@ +--- +title: "List of longest-living organisms" +chunk: 4/5 +source: "https://en.wikipedia.org/wiki/List_of_longest-living_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:08.624136+00:00" +instance: "kb-cron" +--- + +The Greenland shark had been estimated to live to about 200 years, but a study published in 2016 found that a 5.02 m (16.5 ft) specimen was between 272 and 512 years old. That makes the Greenland shark the longest-lived vertebrate. +The maximum lifespan of the freshwater pearl mussel (Margaritifera margaritifera) may be 210–250 years. +Some confirmed sources estimate bowhead whales to have lived at least 211 years of age, making them the oldest mammals. +Rougheye rockfish can reach an age of 205 years. +Specimens of the Red Sea urchin Strongylocentrotus franciscanus have been found to be over 200 years old. +Many sub-families of the marine fish Oreosomatidae, including the Allocyttus, Neocyttus, and Pseudocyttus (collectively referred to as the Oreos) have been reported to live up to 170 years, based on otolith-increment estimates and radiometric dating. +The deepsea hydrocarbon seep tubeworm Lamellibrachia luymesi (Annelida, Polychaeta) lives for more than 170 years. +Geoduck, a species of saltwater clam native to the Puget Sound, have been known to live more than 160 years. +A Swedish man claimed that a European eel named Åle was 155 years old when it died in 2014. If correct, it would have been the world's oldest, having been hatched in 1859. +Orange roughy, also known as deep sea perch, can live up to 149 years. +George the lobster (an American lobster, Homarus americanus) was estimated to be about 140 years old by PETA in January 2009. +The bigmouth buffalo (Ictiobus cyprinellus), a freshwater fish in the family Catostomidae, has a maximum longevity of at least 127 years based on otolith annulus counts and bomb radiocarbon dating. +In 2012, a sturgeon estimated to be 125 years old was caught in a river in Wisconsin. +Tardigrades, capable of cryptobiosis, have been shown to survive nearly 120 years in a dry state. +The great white shark is estimated to live for 70+ years, making it one of the longest lived cartilaginous fishes currently known. +An orca of the Southern Resident population identified as J2 or Granny was estimated by some researchers to have been approximately 105 years old at her death in 2017; however, other dating methods estimated her age as 65–80. +A goldfish named Tish lived for 43 years after being won at a fairground in 1956. +A koi fish named Hanako reportedly died at 226 years old in 1977, making her the longest-lived koi fish ever recorded. However, there is uncertainty as to the veracity of her longevity, with Snopes reporting that no conclusive evidence of her age could be found. +A lungfish named Methuselah was determined to be between 92 and 101 years old in 2023, making her the oldest living fish in captivity at the time. + +=== Humans === + +Humans are among the longest living land mammals. + +Jeanne Calment, a French woman, lived to the age of 122 years and 164 days, making her the oldest fully documented human who has ever lived. She died on August 4, 1997. +Jiroemon Kimura, a Japanese man, died on 12 June 2013 at the age of 116 years and 54 days. He holds the record for the oldest ever male human. +The oldest known person alive today is Ethel Caterham, a British woman, at age 116 years, 256 days (born 21 August 1909). +These are single exceptional examples; for a broader view, see life expectancy. + +=== Other terrestrial and pagophilic animals === \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-4.md b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-4.md new file mode 100644 index 000000000..3f196d0e3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_longest-living_organisms-4.md @@ -0,0 +1,56 @@ +--- +title: "List of longest-living organisms" +chunk: 5/5 +source: "https://en.wikipedia.org/wiki/List_of_longest-living_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:08.624136+00:00" +instance: "kb-cron" +--- + +Adwaita, an Aldabra giant tortoise, died at an estimated age of 255 in March 2006 in Zoological Garden, Alipore, Kolkata, India. If confirmed, the tortoise would have been the oldest known terrestrial animal to have ever existed. +Jonathan, a Seychelles giant tortoise living on the island of Saint Helena, is reported to be at least 193 years old, hence the oldest currently living terrestrial animal. If Adwaita's claim is not true, Jonathan might be the oldest known terrestrial animal to have ever existed. +Tu'i Malila, a radiated tortoise, died at the age of 188 in May 1966, at the time the oldest verified vertebrate. This tortoise was hatched in 1777. +Harriet, a Galápagos tortoise, died at the age of 175 in June 2006. +Timothy, a Greek tortoise, born in Turkey died at the age of 165 on 3 April 2004 in the UK. +The oldest known bird in the world was an Australian sulphur-crested cockatoo called Cocky Bennett, who lived to 120. He could recall phrases such as "one feather more and I'll fly" and "one at a time, gentlemen, please". He lived from 1796 to 1916 and traveled the world with various owners. +The tuatara, a lizard-like reptile native to New Zealand, can live well over 100 years. Henry, a tuatara at the Southland Museum in New Zealand, mated for the first time at the estimated age of 111 years in 2009 with an 80-year-old female and fathered 11 baby tuatara. +Dakshayani, a female Asian elephant, initially owned by the Travancore royal family and later by the Travancore Devaswom Board, was 88 or 89 years old when she died on February 5, 2019. She is believed to be the oldest elephant in captivity in Asia and was nicknamed Gaja Muthassi (grandmother of elephants). +Lin Wang, an Asian elephant, was the oldest elephant in the Taipei Zoo. He was born on January 18, 1917, and died on February 26, 2003, at 86 years, surpassing the previous record of 84. Normally, elephants live up to 50 years, while their maximum lifespan is generally estimated at 70. +Hakuna, an African slender-snouted crocodile, was gifted to Blijdorp Zoo in Rotterdam, Netherlands, in 1929 by singer and dancer Josephine Baker, He lived there for 85 years until he died on 19 February 2015. +Henry, a Nile crocodile currently living in the Crocworld Conservation Centre of Scottburgh, South Africa is reported to be 123–124 years old, making him the oldest crocodile in captivity. He is also notable for fathering 10,000 offspring with 6 different mates and for meeting TV host, Robert Alleva. +A greater flamingo named Greater died at Adelaide Zoo in January 2014 at the age of at least 83. +Cookie (June 30, 1933 – August 27, 2016), an Australian-born Major Mitchell's cockatoo at Brookfield Zoo, Illinois, was the oldest member of his species in captivity, and died in August 2016 at a verified age of 83. +Muja, an American alligator at Belgrade Zoo, is considered the oldest alligator in the world. Muja is more than 80 years old. +Thaao, an Andean condor born c. 1930, died at the age of 79 or 80 in 2010. +Fatou, a gorilla at the Berlin Zoo is the oldest gorilla ever at the age of 68. +A female Laysan albatross named Wisdom successfully laid an egg at Midway Atoll in December 2024, at the age of 74. As of 2025, she is the oldest known wild bird in the world. +Bella, a Sumatran orangutan at Tierpark Hagenbeck, is the oldest orangutan ever at the age of 64. +The oldest living horse on record, Ol' Billy, was allegedly born in the year 1760 in London, England. Bill died in 1822 at the age of 62. Henry Harrison, a resident of London during the time, had also allegedly known Ol' Billy for 59 years until Bill's death. +Rod, an Egyptian vulture who lived at the Jurong Bird Park from 1971 to his death in 2022. Estimated to be 60 prior to his euthanasia, he may have been the oldest known individual of his species. +The oldest bear on record was Andreas, a European brown bear, living in the ARCTUROS bear sanctuary in northern Greece. He was at least 50 years old at the time of his death. +On May 27, 1983, a splendor beetle emerged from a staircase in Essex, UK, after at least 47 years as a larva. +A wild-born black rhino named Elly was the oldest in North America at an estimated 45 years of age, and resided in California's San Francisco Zoo from April 1974 until passing in May 2017. +The oldest living spider, named Number 16 by researchers, was a 43-year-old female Gaius villosus armored trapdoor spider, at the North Bungulla Reserve, Tammin, Western Australia. +Debby, the polar bear, an inhabitant of the Assiniboine Park Zoo in Winnipeg, Canada, was the oldest polar bear and third-oldest bear species on record when she died in 2008, at the age of 42. +The oldest recorded bat, a Siberian bat (previously identified as a Brandt's bat), was at least 41 years old at the time of capture. +Creme Puff, a cat owned by Jake Perry of Austin, Texas, was born on August 3, 1967, and died three days after her 38th birthday on August 6, 2005. +Bluey, an Australian Cattle Dog who was the longest-lived dog ever verified, reached 29 years and died in 1939. +The oldest goat was McGinty who lived to the age of 22 years and 5 months until her death in November 2003 on Hayling Island, UK. +A wild rabbit named Flopsy was caught on August 6, 1964, and died 18 years and 10 months later in Tasmania, Australia +A bearded dragon owned by Nik Vernon was 16 years 129 days old when he died on December 2, 2013. +A mouse named Patrick Stewart (in tribute to the actor) has been verified by Guinness World Records as the oldest living mouse in human care as well as the oldest mouse ever, aged 9 years 210 days as of 9 February 2023. +The oldest gerbil was a Mongolian gerbil named Sahara, she was born in May 1973 and died on 4 October 1981 aged 8 years and 4 months. +A hamster owned by Karen Smeaton in Tyne & Wear, UK, reached 4 years and 6 months. + +== See also == + +== References == + +== Further reading == +Rachel Sussman (2014). The Oldest Living Things in the World. Chicago: University of Chicago Press. ISBN 978-0-226-05750-7. + +== External links == +Rachel Sussman: World's oldest living things – TED Talk +Live Science: Longest living animals (August, 2021). +The latest version of AnAge database with longevity records and ageing information for >4,600 species (June, 2023) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_marine_ecoregions-0.md b/data/en.wikipedia.org/wiki/List_of_marine_ecoregions-0.md new file mode 100644 index 000000000..47d4017ff --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_marine_ecoregions-0.md @@ -0,0 +1,484 @@ +--- +title: "List of marine ecoregions" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_marine_ecoregions" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:19.837482+00:00" +instance: "kb-cron" +--- + +The following is a list of marine ecoregions, as defined by the WWF and The Nature Conservancy +The WWF/Nature Conservancy scheme groups the individual ecoregions into 12 marine realms, which represent the broad latitudinal divisions of polar, temperate, and tropical seas, with subdivisions based on ocean basins. The marine realms are subdivided into 62 marine provinces, which include one or more of the 232 marine ecoregions. +The WWF/Nature Conservancy scheme currently encompasses only coastal and continental shelf areas. + + +== Arctic realm == +(no provinces identified) + +North Greenland +North and East Iceland +East Greenland Shelf +West Greenland Shelf +Northern Grand Banks-Southern Labrador +Northern Labrador +Baffin Bay-Davis Strait +Hudson Complex +Lancaster Sound +High Arctic Archipelago +Beaufort-Admunsen-Viscount Melville-Queen Maud +Beaufort Sea-continental coast and shelf +Chukchi Sea +Eastern Bering Sea +East Siberian Sea +Laptev Sea +Kara Sea +North and East Barents Sea +White Sea + + +== Temperate Northern Atlantic == + + +=== Northern European Seas === +South and West Iceland +Faroe Plateau +Southern Norway +Northern Norway and Finnmark +Baltic Sea +North Sea +Celtic Seas + + +=== Lusitanian === +South European Atlantic Shelf +Saharan Upwelling +Azores Canaries Madeira + + +=== Mediterranean Sea === +Adriatic Sea +Aegean Sea +Levantine Sea +Tunisian Plateau/Gulf of Sidra +Ionian Sea +Western Mediterranean +Alboran Sea + + +=== Black Sea === +Black Sea + + +=== Cold Temperate Northwest Atlantic === +Gulf of St. Lawrence-Eastern Scotian Shelf +Southern Grand Banks-South Newfoundland +Scotian Shelf +Gulf of Maine-Bay of Fundy +Virginian + + +=== Warm Temperate Northwest Atlantic === +Carolinian +Northern Gulf of Mexico + + +== Temperate Northern Pacific == + + +=== Cold Temperate Northwest Pacific === +Sea of Okhotsk +Kamchatka Shelf and Coast +Oyashio Current +Northern Honshu +Sea of Japan +Yellow Sea + + +=== Warm Temperate Northwest Pacific === +Central Kuroshio Current +East China Sea + + +=== Cold Temperate Northeast Pacific === +Aleutian Islands +Gulf of Alaska +North American Pacific Fjordland +Puget Trough/Georgia Basin +Oregon, Washington, Vancouver Coast and Shelf +Northern California + + +=== Warm Temperate Northeast Pacific === +Southern California Bight +Cortezian +Magdalena Transition + + +== Tropical Atlantic == + + +=== Tropical Northwestern Atlantic === +Bermuda +Bahamian +Eastern Caribbean +Greater Antilles +Southwestern Caribbean +Western Caribbean +Southern Gulf of Mexico +Floridian + + +=== North Brazil Shelf === +Guianian +Amazonia + + +=== Tropical Southwestern Atlantic === +Sao Pedro and Sao Paulo Islands +Fernando de Noronha and Atol das Rocas +Northeastern Brazil +Eastern Brazil +Trindade and Martin Vaz Islands + + +=== St. Helena and Ascension Islands === +St. Helena and Ascension Islands + + +=== West African Transition === +Cape Verde +Sahelian Upwelling + + +=== Gulf of Guinea === +Gulf of Guinea West +Gulf of Guinea Upwelling +Gulf of Guinea Central +Gulf of Guinea Islands +Gulf of Guinea South +Angolan + + +== Western Indo-Pacific == + + +=== Red Sea and Gulf of Aden === +Northern and Central Red Sea +Southern Red Sea +Gulf of Aden + + +=== Somali/Arabian === +Persian Gulf +Gulf of Oman +Western Arabian Sea +Central Somali Coast + + +=== Western Indian Ocean === +Northern Monsoon Current Coast +East African Coral Coast +Seychelles +Cargados Carajos +Tromelin Island +Mascarene Islands +Southeast Madagascar +Western and Northern Madagascar +Bight of Sofala/Swamp Coast +Delagoa + + +=== West and South Indian Shelf === +Western India +South India and Sri Lanka + + +=== Central Indian Ocean Islands === +Maldives +Chagos + + +=== Bay of Bengal === +Eastern India +Northern Bay of Bengal + + +=== Andaman Sea === +Andaman and Nicobar Islands +Andaman Sea Coral Coast +Western Sumatra + + +== Central Indo-Pacific == + + +=== South China Sea === +Gulf of Tonkin +Southern China +South China Sea Oceanic Islands + + +=== Sunda Shelf === +Gulf of Thailand +Southern Vietnam +Sunda Shelf/Java Sea +Malacca Strait + + +=== Java Transitional === +Southern Java +Cocos-Keeling/Christmas Island + + +=== South Kuroshio === +South Kuroshio + + +=== Tropical Northwestern Pacific === +Ogasawara Islands +Mariana Islands +East Caroline Islands +West Caroline Islands + + +=== Western Coral Triangle === +Palawan/North Borneo +Eastern Philippines +Sulawesi Sea/Makassar Strait +Halmahera +Papua +Banda Sea +Lesser Sunda +Northeast Sulawesi + + +=== Eastern Coral Triangle === +Bismarck Sea +Solomon Archipelago +Solomon Sea +Southeast Papua New Guinea + + +=== Sahul Shelf === +Gulf of Papua +Arafura Sea +Arnhem Coast to Gulf of Carpentaria +Bonaparte Coast + + +=== Northeast Australian Shelf === +Torres Strait and Northern Great Barrier Reef +Central and Southern Great Barrier Reef + + +=== Northwest Australian Shelf === +Exmouth to Broome +Ningaloo + + +=== Tropical Southwestern Pacific === +Tonga Islands +Fiji Islands +Vanuatu +New Caledonia +Coral Sea + + +=== Lord Howe and Norfolk Islands === +Lord Howe and Norfolk Islands + + +== Eastern Indo-Pacific == + + +=== Hawaii === +Hawaii + + +=== Marshall, Gilbert, and Ellice Islands === +Marshall Islands +Gilbert and Ellice Islands + + +=== Central Polynesia === +Line Islands +Phoenix Islands/Tokelau/Northern Cook Islands +Samoa Islands + + +=== Southeast Polynesia === +Tuamotus +Rapa-Pitcairn +Southern Cook/Austral Islands +Society Islands + + +=== Marquesas === +Marquesas + + +=== Easter Island === +Easter Island + + +== Tropical Eastern Pacific == + + +=== Tropical East Pacific === +Revillagigedos +Clipperton +Mexican Tropical Pacific +Chiapas-Nicaragua +Nicoya +Cocos Islands +Panama Bight +Guayaquil + + +=== Galapagos === +Northern Galapagos Islands +Eastern Galapagos Islands +Western Galapagos Islands + + +== Temperate South America == + + +=== Warm Temperate Southeastern Pacific === +Central Peru +Humboldtian +Central Chile +Araucanian + + +=== Juan Fernandez and Desventuradas === +Juan Fernandez and Desventuradas + + +=== Warm Temperate Southwestern Atlantic === +Southeastern Brazil +Rio Grande +Rio de la Plata +Uruguay-Buenos Aires Shelf + + +=== Magellanic === +North Patagonian Gulfs +Patagonian Shelf +Falkland Islands +Channels and Fjords of Southern Chile +Chiloense + + +=== Tristan-Gough === +Tristan-Gough + + +== Temperate Southern Africa == + + +=== Benguela === +Namib +Namaqua + + +=== Agulhas === +Agulhas Bank +Natal + + +=== Amsterdam-St Paul === +Amsterdam-Saint-Paul + + +== Temperate Australasia == + + +=== Northern New Zealand === +Kermadec Islands (195) +Northeastern New Zealand (196) +Three Kings-North Cape (197) + + +=== Southern New Zealand === +Chatham Island (198) +Central New Zealand (199) +South New Zealand (200) +Snares Island (201) + + +=== East Central Australian Shelf === +Tweed-Moreton (202) +Manning-Hawkesbury (203) + + +=== Southeast Australian Shelf === +Cape Howe (204) +Bassian (205) +Western Bassian (206) + + +=== Southwest Australian Shelf === +South Australian Gulfs (207) +Great Australian Bight (208) +Leeuwin (209) + + +=== Western Central Australian Shelf === +Shark Bay (210) +Houtman (211) + + +== Southern Ocean == + + +=== Subantarctic Islands === +Macquarie Island +Heard Island and McDonald Islands +Kerguelen Islands +Crozet Islands +Prince Edward Islands +Bouvet Island +Peter the First Island + + +=== Scotia Sea === +South Sandwich Islands +South Georgia +South Orkney Islands +South Shetland Islands +Antarctic Peninsula + + +=== Continental High Antarctic === +East Antarctic Wilkes Land +East Antarctic Enderby Land +East Antarctic Dronning Maud Land +Weddell Sea +Amundsen/Bellingshausen Sea +Ross Sea + + +=== Subantarctic New Zealand === +Bounty and Antipodes Islands +Campbell Island +Auckland Island + + +== See also == + +List of terrestrial ecoregions (WWF) + + +== Notes == + + +== References == +Spalding, Mark D., Helen E. Fox, Gerald R. Allen, Nick Davidson et al. "Marine Ecoregions of the World: A Bioregionalization of Coastal and Shelf Areas". Bioscience Vol. 57 No. 7, July/August 2007, pp. 573–583. + + +== External links == + +World Wildlife Fund—WWF: Marine Ecoregions of the World (MEOW) +Queries listing ecoregions [1] and provinces [2] from Wikidata \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_marsupials_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_marsupials_by_population-0.md new file mode 100644 index 000000000..0b5c44be2 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_marsupials_by_population-0.md @@ -0,0 +1,42 @@ +--- +title: "List of marsupials by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_marsupials_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:14.141361+00:00" +instance: "kb-cron" +--- + +This is a list of estimated global populations of Marsupials (infraclass Marsupialia) species. This list is not comprehensive, as not all Marsupials have had their numbers quantified. +Some members of Marsupialia are extinct, and thus have population sizes of zero: + +Thylacine (Thylacinus cynocephalus) - last recorded wild individual captured in 1933, and died in captivity in 1936. +Liverpool Plains striped bandicoot (Perameles fasciata) - went extinct in 1840s. +Marl (Perameles myosuros) - last seen in 1907, extinct circa 1910. +South-eastern striped bandicoot (Perameles notina) - extinct sometime in late 19th century. +Nullarbor barred bandicoot (Perameles papillon) - formerly considered a subspecies of P. bougainville. Last record from 1920s, believed to have gone extinct circa 1928. +Desert bandicoot (Perameles eremiana) - last confirmed record from 1943. Unconfirmed reports persisted into the late 1960s. +Southern pig-footed bandicoot (Chaeropus ecaudatus) - last specimen collected in 1900, but likely persisted into the 1930s. +Northern pig-footed bandicoot, or Yirratji (Chaeropus yirratji) - likely went extinct in the 1950s. +Lake Mackay hare-wallaby, or Kuluwarri (Lagorchestes asomatus) - known from a single specimen taken in 1932. Likely went extinct by 1960. +Eastern hare-wallaby (Lagorchestes leporides) - last recorded in 1890. +Toolache wallaby (Notamacropus greyi) - last confirmed records from 1924; species persisted in captivity until 1939. Some unconfirmed reports were made as late as the 1970s, but could not be verified. +Crescent nail-tailed wallaby (Onychogalea lunata) - no confirmed records since 1940s. Estimated to have gone extinct circa 1963. +Desert bettong (Bettongia anhydra) - known from a single specimen collected in 1933. Likely went extinct circa 1960. +Nullarbor dwarf bettong (Bettongia pusilla) - first described in 1997, but is expected to have been extant at the time of European settlement in Oceania. +Desert rat-kangaroo (Caloprymnus campestris) - last confirmed record from 1935; unconfirmed reports have occurred as recently as 2013, but species has not been found despite extensive searches. +Broad-faced potoroo (Potorous platyops) - last recorded in 1875. + + +== Species without population estimates == + + +== See also == + +Lists of organisms by population +Lists of mammals by population +Lists of elephant species by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_microorganisms_tested_in_outer_space-0.md b/data/en.wikipedia.org/wiki/List_of_microorganisms_tested_in_outer_space-0.md index 95b6299c2..b758509e8 100644 --- a/data/en.wikipedia.org/wiki/List_of_microorganisms_tested_in_outer_space-0.md +++ b/data/en.wikipedia.org/wiki/List_of_microorganisms_tested_in_outer_space-0.md @@ -4,7 +4,7 @@ chunk: 1/1 source: "https://en.wikipedia.org/wiki/List_of_microorganisms_tested_in_outer_space" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T06:15:42.653813+00:00" +date_saved: "2026-05-05T07:57:21.198342+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/List_of_mitosporic_Ascomycota-0.md b/data/en.wikipedia.org/wiki/List_of_mitosporic_Ascomycota-0.md new file mode 100644 index 000000000..5ec0cd1f6 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_mitosporic_Ascomycota-0.md @@ -0,0 +1,16 @@ +--- +title: "List of mitosporic Ascomycota" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_mitosporic_Ascomycota" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:22.436296+00:00" +instance: "kb-cron" +--- + +The mitosporic Ascomycota are a heterogeneous group of ascomycotic fungi whose common characteristic is the absence of a sexual state (anamorph); many of the pathogenic fungi in humans belong to this group. + + +== References == + +https://www.uniprot.org/taxonomy/108599. Retrieved 29 November 2011 \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_model_organisms-0.md b/data/en.wikipedia.org/wiki/List_of_model_organisms-0.md new file mode 100644 index 000000000..31f968874 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_model_organisms-0.md @@ -0,0 +1,85 @@ +--- +title: "List of model organisms" +chunk: 1/4 +source: "https://en.wikipedia.org/wiki/List_of_model_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:23.660934+00:00" +instance: "kb-cron" +--- + +This is a list of model organisms used in scientific research. + +== Viruses == +Phages (infecting prokaryotes): + +Escherichia virus Lambda (Phage lambda) +Phi X 174, the first DNA genome ever to be sequenced (circular, 5386 base pairs in length), shortly after the RNA genome of bacteriophage MS2 (in 1976). +T4 phage +Animal viruses: + +SV40 +Human alphaherpesvirus (Herpes simplex virus) +Plant viruses: + +Tobacco mosaic virus + +== Bacteria == + +Escherichia coli (E. coli), common Gram-negative gut bacterium widely used in molecular genetics. Main lab strain is 'K-12'. +Bacillus subtilis, endospore forming Gram-positive bacterium. Main lab strain is '168'. +Caulobacter crescentus, bacterium that divides into two distinct cells used to study cellular differentiation. +Mycoplasma genitalium, minimal organism and human STD pathogen. +Aliivibrio fischeri, quorum sensing, bioluminescence and animal-bacterial symbiosis with Hawaiian bobtail squid. +Bacteroides thetaiotaomicron, polysaccharide-degrading member of the human gut microbiota, used to study functional aspects of the gut microbiota. +Synechocystis (specifically PCC 6803), photosynthetic cyanobacterium widely used in photosynthesis research. +Pseudomonas fluorescens, soil bacterium that readily diversifies into different strains in the lab. +Azotobacter vinelandii, obligate aerobe diazotroph used in nitrogen fixation research. +Streptomyces coelicolor, soil-dwelling filamentous bacterium used to produce many clinically useful antibiotics. + +=== Bacteria with minimal synthetic genomes === +Bacteria with synthetic, minimized genomes provide a near-"blank slate" for study. Foreign genes, natural or artificial, can be introduced into these minimal bacteria to study their function as well as what is needed for their function. + +"Mycoplasma laboratorium", a series of minimized Mycoplasma mycoides strains. Syn3B has been used to research the interaction between Mycoplasma and mammal cells, specifically what genes are needed for intracellular parasitism. +Escherichia coli Syn61, a minimized version of E. coli with three unused codons. Has been used to research expanded genetic code. +Escherichia coli Syn57, a further minimization with seven unused codons. + +== Archaea == +Methanococcus and Methanosarcina, model methanogens, representing the two metabolic types of hydrogenotrophism and methylotrophism. Methanogenesis remains a key area of metabolic research. +Halobacterium salinarum and Haloferax volcanii, model Haloarchaea. The former has a reputation in the study of DNA repair. The latter is more suited to more traditional genetics due to a shorter generation time and more stable genome. This order is known for its easy updake of genetic tools as well as resistance to culture contamination. +Thermococcus kodakarensis, Pyrococcus abyssi, and Pyrococcus furiosus are the Thermococcales models. This order is known for its unique metabolic pathways. +Three members of Sulfolobus, S. solfataricus PBL2025, S. islandicus E322S, and S. acidocaldarius are the current Sulfolobales models. Proteins from these thermophilic bacteria are easy to crystalize, simplifying structural work. + +== Eukaryotes == + +=== Protists === +Stentor coeruleus, used in molecular biology (its genome has been sequenced), and is studied as a model of single-cell regeneration. +Dictyostelium discoideum, used in molecular biology and genetics (its genome has been sequenced), and is studied as an example of cell communication, differentiation, and programmed cell death. +Tetrahymena thermophila, free living freshwater ciliate protozoan. +Naegleria gruberi, freshwater non-pathogenic amoeboflagellate sometimes used in eukaryotic cell biology experiments. +Emiliania huxleyi, unicellular marine coccolithophore alga, extensively studied as a model phytoplankton species. +Thalassiosira pseudonana, unicellular marine diatom alga, extensively studied as a model marine diatom since its genome was published in 2004. + +=== Fungi === +Ashbya gossypii, cotton pathogen, subject of genetics studies (polarity, cell cycle). +Aspergillus nidulans, mold subject of genetics studies. +Coprinus cinereus, mushroom (genetic studies of mushroom development, genetic studies of meiosis). +Cryptococcus neoformans, opportunistic human pathogen +Neurospora crassa, orange bread mold (genetic studies of meiosis, metabolic regulation, and circadian rhythm). +Pichia pastoris (Komagataella phaffii), widely used in biochemical research and industry as an expression system for protein production, as well as genetic study +Rhizophagus irregularis, used for studying arbuscular mycorrhizal symbiosis. +Saccharomyces cerevisiae (baker's yeast or budding yeast), used in brewing and baking. +Schizophyllum commune, model for mushroom formation. +Schizosaccharomyces pombe, fission yeast, (cell cycle, cell polarity, RNAi, centromere structure and function, transcription). +Ustilago maydis, dimorphic yeast and plant pathogen of maize (dimorphism, plant pathogen, transcription). + +=== Plants === + +==== Vascular plants ==== + +Arabidopsis thaliana, currently the most popular model plant. This herbaceous dicot of the family Brassicaceae is closely related to the mustard plant. Its small stature and short generation time facilitates rapid genetic studies, and many phenotypic and biochemical mutants have been mapped. Arabidopsis was the first plant to have its genome sequenced. Its genome sequence, along with a wide range of information concerning Arabidopsis, is maintained by the TAIR database.(Plant physiology, Developmental biology, Molecular genetics, Population genetics, Cytology, Molecular biology) +Boechera genus, combines some of the experimental tractability and genetic tools developed for its close relative Arabidopsis with a largely undisturbed natural history, making it a promising model system for research at the intersection of genetics, genomics, ecology, and evolution. The genus includes species with the rare trait of apomixis at the diploid level.(Evolutionary ecology, Population genetics, Molecular ecology, Evolutionary biology, Ecological genetics) +Selaginella moellendorffii, remnant of an ancient lineage of vascular plants that is key to understanding the evolution of land plants. It has a small genome size (~110Mb) and its sequence was released by the Joint Genome Institute in early 2008. (Evolutionary biology, Molecular biology) +Brachypodium distachyon, emerging experimental model grass that has many attributes that make it an excellent model for temperate cereals. (Agronomy, Molecular biology, Genetics) +Setaria viridis, emerging model grass for C4 photosynthesis and related bioenergy grasses. +Lotus japonicus, model legume used to study the symbiosis responsible for nitrogen fixation. (Agronomy, Molecular biology) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_model_organisms-1.md b/data/en.wikipedia.org/wiki/List_of_model_organisms-1.md new file mode 100644 index 000000000..78933e9ed --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_model_organisms-1.md @@ -0,0 +1,28 @@ +--- +title: "List of model organisms" +chunk: 2/4 +source: "https://en.wikipedia.org/wiki/List_of_model_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:23.660934+00:00" +instance: "kb-cron" +--- + +Lemna gibba, rapidly growing aquatic monocot, one of the smallest flowering plants. Lemna growth assays are used to evaluate the toxicity of chemicals to plants in ecotoxicology. Because it can be grown in pure culture, microbial action can be excluded. Lemna is being used as a recombinant expression system for economical production of complex biopharmaceuticals. It is also used in education to demonstrate population growth curves. +Zea mays L. (Maize/corn), cereal grain. It is a diploid monocot with 10 large chromosome pairs, easily studied with the microscope. Its genetic features, including many known and mapped phenotypic mutants and a large number of progeny per cross (typically 100–200) facilitated the discovery of transposons ("jumping genes"). Many DNA markers have been mapped and the genome has been sequenced. (Genetics, Molecular biology, Agronomy) +Medicago truncatula, model legume, closely related to the common alfalfa. Its rather small genome is currently being sequenced. It is used to study the symbiosis responsible for nitrogen fixation. (Agronomy, Molecular biology) +Mimulus guttatus, model organism used in evolutionary and functional genomes studies. The genus Mimulus contains c. 120 species and is in the family Phrymaceae. Several genetic resources have been designed for the study of this genus and some are free access (http://www.mimulusevolution.org) +Nicotiana benthamiana, model organism for plant-pathogen studies. +Nicotiana tabacum cv. BY-2 (Tobacco BY-2 cells), suspension cell line from tobacco (Nicotiana tabacum) that is useful for general plant physiology studies at the cell level. The genome of this particular cultivar will not be sequenced in the near future, but sequencing of its wild species Nicotiana tabacum is presently in progress. (Cytology, Plant physiology, Biotechnology) +Oryza sativa (Rice) is used as a model for cereal biology. It has one of the smallest genomes of any cereal species, and sequencing of its genome is finished. (Agronomy, Molecular biology) + +Populus, genus used as a model in forest genetics and woody plant studies. It has a small genome size, grows very rapidly, and is easily transformed. The genome sequence of black cottonwood (Populus trichocarpa) is publicly available. + +==== Other Archaeplastida ==== +Chlamydomonas reinhardtii, unicellular green alga used to study photosynthesis, flagella and motility, regulation of metabolism, cell–cell recognition and adhesion, response to nutrient deprivation and many other topics. Chlamydomonas reinhardtii has well-studied genetics, with many known and mapped mutants and expressed sequence tags, and there are advanced methods for genetic transformation and selection of genes. Sequencing of the Chlamydomonas reinhardtii genome was reported in October 2007. A Chlamydomonas genetic stock center exists at Duke University, and an international Chlamydomonas research interest group meets on a regular basis to discuss research results. Chlamydomonas is easy to grow on an inexpensive defined medium. +Physcomitrella patens, moss increasingly used for studies on development and molecular evolution of plants. It is so far the only non-vascular plant(and so the only "primitive" plant) with its genome completely sequenced. Moreover, it is currently the only land plant with efficient gene targeting that enables gene knockout. The resulting knockout mosses are stored and distributed by the International Moss Stock Center. (Plant physiology, Evolutionary biology, Molecular genetics, Molecular biology) +Marchantia polymorpha, liverwort that is also emerging as a model for plant biology and development. + +=== Animals === + +==== Invertebrates ==== \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_model_organisms-2.md b/data/en.wikipedia.org/wiki/List_of_model_organisms-2.md new file mode 100644 index 000000000..8836901d5 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_model_organisms-2.md @@ -0,0 +1,51 @@ +--- +title: "List of model organisms" +chunk: 3/4 +source: "https://en.wikipedia.org/wiki/List_of_model_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:23.660934+00:00" +instance: "kb-cron" +--- + +Amphimedon queenslandica, a demosponge from the phylum Porifera used as a model for evolutionary developmental biology and comparative genomics +Arbacia punctulata, the purple-spined sea urchin, classical subject of embryological studies +Aplysia, a sea slug, whose ink release response serves as a model in neurobiology and whose growth cones serve as a model of cytoskeletal rearrangements +Branchiostoma floridae, a species commonly known as amphioxus or lancelet from the subphylum Cephalochordata of the phylum Chordata used as a model for understanding the evolution of nonchordate deuterostomes, invertebrate chordates, and vertebrates +Caenorhabditis elegans, a nematode, usually called C. elegans - an excellent model for understanding the genetic control of development and physiology. C.elegans has a fixed number of 1031 cells. C. elegans was the first multicellular organism whose genome was completely sequenced +Callosobruchus maculatus, the bruchid beetle, used to study sexual selection and sexual conflict +Chorthippus parallelus (the meadow grasshopper), used to study sexual selection and sexual conflict +Ciona intestinalis, a sea squirt +Daphnia spp., small planktonic crustaceans, highly sensitive to pollution, used for evaluating environmental toxicity of chemicals on aquatic invertebrates. +Coelopidae, seaweed flies, used to study sexual selection and sexual conflict +Diopsidae, stalk-eyed flies, used to study sexual selection and sexual conflict +Drosophila, usually the species Drosophila melanogaster – a kind of fruit fly, famous as the subject of genetics experiments by Thomas Hunt Morgan and others. Easily raised in lab, rapid generations, mutations easily induced, many observable mutations. Recently, Drosophila has been used for neuropharmacological research. (Molecular genetics, Population genetics, Developmental biology). +Euprymna scolopes (the Hawaiian bobtail squid), model for animal-bacterial symbiosis, bioluminescent vibrios +Galleria mellonella (the greater wax moth), the larvae of which are an excellent model organism for in vivo toxicology and pathogenicity testing, replacing the use of small mammals in such experiments. +Gryllus bimaculatus (the field cricket), used to study sexual selection and sexual conflict +Hydra, a Cnidarian is the model organism to understand the processes of regeneration and morphogenesis, as well as the evolution of bilaterian body plans +Loligo pealei, a squid is the subject of studies of nerve function because of its giant axon (nearly 1 mm diameter, roughly a thousand times larger than typical mammalian axons) +Lymnaea stagnalis (great pond snail), a widely used model mollusc, for the study of biomineralization, neurobiology, eco-toxicology, sexual selection and body asymmetry +Macrostomum lignano, a free-living, marine flatworm, a model organism for the study of stem cells, regeneration, ageing, gene function, and the evolution of sex. Easily raised in the lab, short generation time, indetermined growth, complex behaviour +Manduca sexta (Tobacco hornworm), the large caterpillars are an excellent model organism for immunity and in vivo imaging, replacing mice and rats in such experiments. +Mnemiopsis leidyi, from the phylum Ctenophora (comb jelly) used as a model for evolutionary developmental biology and comparative genomics +Nematostella vectensis, a sea anemone from the phylum Cnidaria used as a model for evolutionary developmental biology and comparative genomics +Oikopleura dioica, an appendicularian, a free-swimming tunicate (or urochordate) +Ormia ochracea, a tachinid fly used to study sound localization. +Oscarella carmela, a homoscleromorph sponge (phylum Porifera) used as a model in evolutionary developmental biology +Parhyale hawaiensis an amphipod crustacean, used in evolutionary developmental (evo-devo) studies, with an extensive toolbox for genetic manipulation. +Platynereis dumerilii a marine polychaetous annelid, which evolved very slowly and therefore retained many ancestral features. +Podisma spp., in the Alps, used to study sexual selection and sexual conflict +Pristionchus pacificus, a roundworm used in evolutionary developmental biology in comparative analyses with C. elegans +Scaptomyza flava, herbivorous leaf miner fly nested in the Drosophila, and a close relative of D. melanogaster. +Scathophaga stercoraria (the yellow dung fly), used to study sexual selection and sexual conflict +Schmidtea mediterranea (freshwater planarian), a model for regeneration and development of tissues such as the brain and germline +Solenopsis invicta (the red imported fire ant), the most-studied species of ant, used as a model organism for evolution of polyphenism and caste +Stomatogastric ganglion, various arthropod species, and a model for motor pattern generation seen in all repetitive motions +Strongylocentrotus purpuratus (the purple sea urchin), widely used in developmental biology +Symsagittifera roscoffensis, a flatworm, subject of studies of bilaterian body plan development +Tribolium castaneum (the flour beetle), small and easily kept darkling beetle used especially in behavioural ecology experiments +Trichoplax adhaerens, simple free-living animal from the phylum Placozoa used as a model in evolutionary developmental biology and comparative genomics +Tubifex tubifex, an oligochaeta used for evaluating environmental toxicity of chemicals on aquatic and terrestrial worms. + +==== Vertebrates ==== \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_model_organisms-3.md b/data/en.wikipedia.org/wiki/List_of_model_organisms-3.md new file mode 100644 index 000000000..aa4c67f46 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_model_organisms-3.md @@ -0,0 +1,40 @@ +--- +title: "List of model organisms" +chunk: 4/4 +source: "https://en.wikipedia.org/wiki/List_of_model_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:23.660934+00:00" +instance: "kb-cron" +--- + +Canis lupus familiaris (Dog), important respiratory and cardiovascular model, also contributed to the discovery of classical conditioning. +Felis sylvestris catus (Cat), used in neurophysiological research. +Mustela furo (Ferret), used as a model organism to study influenza A virus infection. +Ambystoma mexicanum (Axolotl), used to study regeneration and developmental processes +Bombina bombina and Bombina variegata, used to study sexual selection and sexual conflict +Anolis carolinensis (Carolina anole), used to study reptile genomics +Gallus gallus domesticus (Chicken), used for developmental studies, as it is an amniote and excellent for micromanipulation (e.g. tissue grafting) and over-expression of gene products. +Sigmodon hispidus (Cotton rat), formerly used in polio research. +Mesocricetus auratus (Golden hamster), first used to study kala-azar (leishmaniasis). +Cavia porcellus (Guinea pig), used by Robert Koch and other early bacteriologists as a host for bacterial infections, hence a byword for "laboratory animal" even though less commonly used today. +Myotis lucifugus (Little brown bat), used to prove echolocation exists in bats in 1930s and also used in experiments predicting microbat behavior as it is a reliable species that has typical features of a temperate bat species. +Oryzias latipes (Medaka, or Japanese ricefish), important model in developmental biology, and has the advantage of being much sturdier than the traditional zebrafish. +Mus musculus (Mouse), the classic model vertebrate. Many inbred strains exist, as well as lines selected for particular traits, often of ethological or medical interest, e.g. body size, obesity, muscularity, voluntary wheel-running behavior. (Quantitative genetics, Molecular evolution, Genomics) +Heterocephalus glaber (Naked mole-rat), studied for their characteristic pain insensitivity, thermoregulation, cancer resistance, eusociality, and longevity. +Nothobranchius furzeri, is studied because of their extreme short-lifespan in research on aging, disease and evolution. +Astyanax mexicanus (Mexican tetra or blind cave fish), studied for their rapid convergent evolution of multiple traits across multiple populations, including troglomorphism, circadian rhythms, and sleep +Columba livia domestica (Pigeon), studied extensively for cognitive science and animal intelligence +Poecilia reticulata (Guppy), used to study sexual selection and sexual conflict +Rattus norvegicus (Rat), particularly useful as a toxicology model; also particularly useful as a neurological model and source of primary cell cultures, owing to the larger size of organs and suborganellar structures relative to the mouse. (Molecular evolution, Genomics) +Oryctolagus cuniculus domesticus (Domestic rabbit), used as immunology model for production of antibodies and toxicology model for eye irritation tests. +Macaca mulatta (Rhesus macaque or rhesus monkey), used for studies on infectious disease and cognition. +Macaca fascicularis (variously crab-eating macaque, long-tailed macaque, or cynomolgus macaque) used for studies on neuroscience and disease. +Petromyzon marinus (Sea lamprey), spinal cord research +Takifugu rubripes (Takifugu, a pufferfish), has a small genome with little junk DNA. +Gasterosteus aculeatus (Three-spined stickleback), fish used to study ethology and behavioral ecology. +Xenopus tropicalis and Xenopus laevis (African clawed frog), the eggs and embryos from these frogs are used in developmental biology, cell biology, toxicology, and neuroscience +Taeniopygia guttata (Zebra finch), used in the study of the song system of songbirds and the study of non-mammalian auditory systems. +Danio rerio (Zebrafish), freshwater fish with a transparent body during early development, which provides unique visual access to the animal's internal anatomy. Zebrafish are used to study development, toxicology and toxicopathology, specific gene function and roles of signaling pathways. + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_neuroscience_databases-0.md b/data/en.wikipedia.org/wiki/List_of_neuroscience_databases-0.md new file mode 100644 index 000000000..cb83d7c2b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_neuroscience_databases-0.md @@ -0,0 +1,26 @@ +--- +title: "List of neuroscience databases" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_neuroscience_databases" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:30.180215+00:00" +instance: "kb-cron" +--- + +A number of online neuroscience databases are available which provide information regarding gene expression, neurons, macroscopic brain structure, and neurological or psychiatric disorders. Some databases contain descriptive and numerical data, some to brain function, others offer access to 'raw' imaging data, such as postmortem brain sections or 3D MRI and fMRI images. Some focus on the human brain, others on non-human. +As the number of databases that seek to disseminate information about the structure, development and function of the brain has grown, so has the need to collate these resources themselves. As a result, there now exist databases of neuroscience databases, some of which reach over 3000 entries. + + +== Neuroscience databases == + + +== Databases of neuroscience databases == + + +== See also == +Neuroinformatics +Budapest Reference Connectome + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_obsolete_taxa-0.md b/data/en.wikipedia.org/wiki/List_of_obsolete_taxa-0.md new file mode 100644 index 000000000..a6fcfe24d --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_obsolete_taxa-0.md @@ -0,0 +1,23 @@ +--- +title: "List of obsolete taxa" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_obsolete_taxa" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:32.709983+00:00" +instance: "kb-cron" +--- + +In the history of the Linnaean classification system, many taxa (e.g. species, genera, families, and higher taxonomic ranks) have become defunct or obsolete, and are no longer used. + + +== Kingdoms == + + +== Animals == + + +== Protists == + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_odd-toed_ungulates_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_odd-toed_ungulates_by_population-0.md new file mode 100644 index 000000000..88e1e8b06 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_odd-toed_ungulates_by_population-0.md @@ -0,0 +1,21 @@ +--- +title: "List of odd-toed ungulates by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_odd-toed_ungulates_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:16.058484+00:00" +instance: "kb-cron" +--- + +This is a list of odd-toed ungulate species (order Perissodactyla) by estimated global population. +Unless otherwise noted, primary populations given are for number of mature individuals. + + +== See also == + +Lists of mammals by population +Lists of organisms by population + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_parasitic_organisms-0.md b/data/en.wikipedia.org/wiki/List_of_parasitic_organisms-0.md new file mode 100644 index 000000000..c7e262086 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_parasitic_organisms-0.md @@ -0,0 +1,157 @@ +--- +title: "List of parasitic organisms" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_parasitic_organisms" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:36.434419+00:00" +instance: "kb-cron" +--- + +This is an incomplete list of organisms that are true parasites upon other organisms. + + +== Endoparasites == +(endo = within; parasites that live inside their hosts) + + +=== Plants === +Rafflesia +Cuscuta +Mistletoe + + +=== Parasitic worms === +These can be categorized into three groups; cestodes, nematodes and trematodes. Examples include: + +Acanthocephala +Ascariasis (roundworms) +Cestoda (tapeworms) including: Taenia saginata (human beef tapeworm), Taenia solium (human pork tapeworm), Diphyllobothrium latum (fish tapeworm) and Echinococcosis (hydatid tapeworm) +Clonorchis sinensis (the Chinese liver fluke) +Dracunculus medinensis (Guinea worm) +Enterobius vermicularis (pinworm) +Filariasis +Hookworm +Loa loa +Onchocerciasis (river blindness) +Schistosomiasis +Strongyloides stercoralis +Tapeworm +Toxocara canis (dog roundworm) +Trichinella +Whipworm + + +=== Protozoans === +Entamoeba histolytica and Entamoeba coli - can cause Amoebiasis +Acanthamoeba +Balamuthia mandrillaris +Giardia +Cyclospora cayetanensis +Cryptosporidium +Toxoplasma gondii +Leishmania - L. tropica, L. donovani, and L. mexicana are known to cause Leishmaniasis. +Plasmodium - causes the fatal disease, Malaria. P. falciparum, P. vivax, and P. malariae are pathogenic to humans. +Babesia + + +=== Fungi === +Gymnosporangium and other rusts +Pyrenophora teres +Cordyceps + + +=== Arthropods === +Pentastomida + + +== Ectoparasites == +(ecto = outside; parasites that live on but not within their hosts, for example, attached to their skin) + + +=== Arthropoda === +Acari +Varroa destructor +Cymothoa exigua +Amblyoponinae (Dracula ants) +Bed bugs +Culicidae (mosquitoes) +Calyptra (moth) (vampire moths) +Hippoboscoidea +Tsetse fly +Lipoptena +Melophagus ovinus, (sheep keds) and relatives +Oestridae (bot flies) +Human botfly +Cuterebra fontinella (mouse botfly) +Phlebotominae (sand flies) +Phthiraptera (Lice) +Body louse +Crab louse +Head louse +Siphonaptera (fleas) +Tabanidae (horse flies) +Tantulocarida +Triatominae +Pea crab +Sacculina + + +=== Annelids === +Hirudinea (some leeches) + + +=== Monogeneans === +Monogeneans are flatworms, generally ectoparasites on fish. + +Calydiscoides euzeti +Lethacotyle vera +Protocotyle euzetmaillardi +Pseudorhabdosynochus spp. + + +=== Mollusks === +Cancellaria cooperii +Glochidium +Pyramidellidae +†Platyceratidae + + +=== Chordates === +Cookiecutter shark +Candiru (vampire fish of Brazil, a facultative parasite) +Lampreys +Male Deep sea anglers +False cleanerfish +Pearlfish +Hood mockingbird +Oxpeckers (cleaning symbiosis) +Snubnosed eel +Vampire bat +Vampire finch +Cuckoo (brood parasite) +Cowbird (brood parasite) +Whydah (brood parasite) + + +=== Plants === +Mistletoe +Monotropa uniflora +Certain orchids +Nuytsia +Orobanche (broomrape) +Santalum album +Certain plants with albinism + + +=== Fungi === +Corn smut +Certain mushrooms +Asterotremella albida + + +== References == + + +== See also == +List of fictional parasites \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_participants_in_the_Evolving_Genes_and_Proteins_symposium-0.md b/data/en.wikipedia.org/wiki/List_of_participants_in_the_Evolving_Genes_and_Proteins_symposium-0.md index 7f71e8c51..ee15ec5d9 100644 --- a/data/en.wikipedia.org/wiki/List_of_participants_in_the_Evolving_Genes_and_Proteins_symposium-0.md +++ b/data/en.wikipedia.org/wiki/List_of_participants_in_the_Evolving_Genes_and_Proteins_symposium-0.md @@ -4,7 +4,7 @@ chunk: 1/1 source: "https://en.wikipedia.org/wiki/List_of_participants_in_the_Evolving_Genes_and_Proteins_symposium" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T06:41:40.554772+00:00" +date_saved: "2026-05-05T07:57:37.680304+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/List_of_plant_orders-0.md b/data/en.wikipedia.org/wiki/List_of_plant_orders-0.md new file mode 100644 index 000000000..9738fab65 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_plant_orders-0.md @@ -0,0 +1,553 @@ +--- +title: "List of plant orders" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_plant_orders" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:38.983809+00:00" +instance: "kb-cron" +--- + +This article lists the living orders of the Viridiplantae, based primarily on the work of Ruggiero et al. 2015. Living order of Lycophytes and ferns are taken from Christenhusz et al. 2011b and Pteridophyte Phylogeny Group. Living orders of Gymnosperms are added from Christenhusz et al. 2011a while extinct orders are from Anderson, Anderson & Cleal 2007. + + +== Division Prasinodermophyta == + + +=== Class Prasinodermophyceae === +Order Prasinodermatales + + +=== Class Palmophyllophyceae === +Order Prasinococcales +Order Palmophyllales + + +== Division Chlorophyta == + + +=== Subdivision Prasinophytina === + + +==== Class Mamiellophyceae ==== +Order Monomastigales +Order Dolichomastigales +Order Mamiellales + + +==== Class Pyramimonadophyceae ==== +Order Pyramimonadales + + +=== Subdivision Chlorophytina === + + +==== Class Nephroselmidophyceae ==== +Order Nephroselmidales + + +==== Class Picocystophyceae ==== +Order Picocystales +Order ?Pseudoscourfieldiales + + +==== Class Chloropicophyceae ==== +Order Chloropicales + + +==== Class Pedinophyceae ==== +Order ?Scourfieldiales +Order Marsupiomonadales +Order Pedinomonadales + + +==== Class Chlorodendrophyceae ==== +Order Chlorodendrales + + +==== Class Trebouxiophyceae ==== +Order ?Phyllosiphonales +Order Chlorellales +Order Prasiolales +Order Microthamniales +Order Trebouxiales + + +==== Class Ulvophyceae ==== +Order Ignatiales +Order Oltmannsiellopsidales +Order Scotinosphaerales +Order Ulotrichales +Order Ulvales +Order Trentepohliales +Order Cladophorales +Order Dasycladales +Order Bryopsidales + + +==== Class Chlorophyceae ==== +Order Chaetopeltidales +Order Chaetophorales +Order Chlamydomonadales +Order Chlorococcales +Order Microsporales +Order Oedogoniales +Order Sphaeropleales +Order Tetrasporales + + +== Division Streptophyta == + + +=== Subdivision Chlorokybophytina === + + +==== Class Mesostigmatophyceae ==== +Order Mesostigmatales + + +==== Class Chlorokybophyceae ==== +Order Chlorokybales + + +=== Subdivision Klebsormidiophyinta === + + +==== Class Klebsormidiophyceae ==== +Order Klebsormidiales + + +=== Subdivision Charophytina === + + +==== Class Charophyceae ==== +Order †Sycidiales +Order †Chovanellales +Order †Moellerinales +Order Charales (Stoenworts & musk grasses) + + +=== Subdivision Coleochaetophytina === + + +==== Class Coleochaetophyceae ==== +Order Coleochaetales + + +=== Subdivision Zygnematophytina === + + +==== Class Zygnematophyceae ==== +Order Spirogloeales +Order Zygnematales +Order Mesotaeniales +Order Desmidiales + + +=== Subdivision Anthocerotophytina === +Source: + + +==== Class Leiosporocerotopsida ==== +Order Leiosporocerotales + + +==== Class Anthocerotopsida ==== +Order Anthocerotales +Order Notothyladales +Order Phymatocerotales +Order Dendrocerotales + + +=== Subdivision Marchantiophytina === +Source: + + +==== Class Haplomitriopsida ==== +Order Treubiales +Order Calobryales + + +==== Class Marchantiopsida ==== +Subclass Blasiidae +Order Blasiales +Subclass Marchantiidae (Complex thalloid liverworts) +Order Neohodgsoniales +Order Sphaerocarpales +Order Lunulariales (crescent-cup liverwort) +Order Marchantiales + + +==== Class Jungermanniopsida ==== +Subclass Pelliidae +Order Pelliales +Order Pallaviciniales +Order Fossombroniales +Subclass Metzgeriidae +Order Pleuroziales +Order Metzgeriales +Subclass Jungermanniidae (leafy liverworts) +Order Porellales +Order Ptilidiales +Order Jungermanniales + + +=== Subdivision Bryophytina === +Source: + + +==== Class Takakiopsida ==== +Order Takakiales + + +==== Class Sphagnopsida ==== +Order †Protosphagnales +Order Ambuchananiales +Order Sphagnales (Peat/bog mosses) + + +==== Class Andreaeobryopsida ==== +Order Andreaeobryales + + +==== Class Andreaeopsida ==== +Order Andreaeales (Granite/lantern mosses) + + +==== Class Oedipodiopsida ==== +Order Oedipodiales + + +==== Class Tetraphidopsida ==== +Order Tetraphidales + + +==== Class Polytrichopsida ==== +Order Polytrichales (Hair-cap mosses) + + +==== Class Bryopsida ==== +Subclass Buxbaumiidae +Order Buxbaumiales +Subclass Diphysciidae +Order Diphysciales +Subclass Gigaspermidae +Order Gigaspermales +Subclass Funariidae +Order Disceliales +Order Encalyptales +Order Funariales +Subclass Timmiidae +Order Timmiales +Subclass Dicranidae (Haplolepideous mosses) +Order Archidiales +Order Pseudoditrichales +Order Catoscopiales +Order Scouleriales +Order Bryoxiphiales +Order Grimmiales +Order Pottiales +Order Dicranales +Subclass Bryidae (Diplolepideous-alternate mosses) +Superorder Bryanae +Order Splachnales +Order Hedwigiales +Order Bartramiales +Order Bryales +Order Rhizogoniales +Order Orthotrichales +Order Orthodontiales +Order Aulacomniales +Superorder Hypnanae +Order Hypnodendrales +Order Ptychomniales +Order Hypopterygiales +Order Hookeriales +Order Hypnales + + +=== Clade †Horneophytina === + + +==== Class †Horneophytopsida ==== +Order †Horneophytales + + +=== Subdivision Tracheophytina === +Source: + + +==== Class †Cooksoniopsida ==== +Order †Cooksoniales + + +==== Class †Rhyniopsida ==== +Order ?†Yarraviales +Order ?†Taeniocradales +Order †Rhyniales + + +==== Clade †Zosterophyllophyta ==== +Class †Barinophytopsida +Order †Barinophytales +Class †Zosterophyllopsida +Order †Sawdoniales +Order †Zosterophyllales + + +==== Class Lycopodiopsida ==== +Order †Drepanophycales +Subclass †Asteroxylidae +Order ?†Thursophytales +Order †Asteroxylales +Subclass Lycopodiidae +Order Lycopodiales (Clubmosses, groundpines, groundcedars) +Subclass †Prolepidodendridae +Order †Protolepidodendrales +Subclass Selaginellidae (Spikemosses; rose of Jericho; resurrection plant; Engels moss) +Order Selaginellales +Order †Lepidodendrales +Order †Pleuromeiales +Order Isoetales (Quillworts) + + +==== Class †Eophyllophytopsida ==== +Order †Eophyllophytales + + +==== Class †Trimerophytopsida ==== +Order †Trimerophytales + + +==== Clade Pteridophyta ==== +Order †Ibykales +Class †Cladoxylopsida +Order †Hyeniales +Order †Iridopteridales +Order †Steloxylales +Order †Pseudosporochnales +Order †Cladoxylales +Class Polypodiopsida (Ferns) +Order †Stauropteridales +Subclass †Zygopterididae +Order †Rhacophytales +Order †Zygopteridales +Subclass Equisetidae +Order †Pseudoborniales +Order †Sphenophyllales +Order Equisetales (Horsetails; scouring-rushes) +Subclass Ophioglossidae +Order Psilotales (Whisk ferns) +Order Ophioglossales (Adder's tongues, moonworts) +Subclass Marattiopsida +Order Marattiales +Subclass Polypodiidae +Order †Urnatopteridales +Order †Senftenbergiales +Order †Botryopteridiales +Order †Anachoropteridales +Order Osmundales (Royal ferns) +Order Hymenophyllales (Filmy ferns) +Order Gleicheniales +Order Schizaeales +Order Salviniales +Order Cyatheales +Order Polypodiales (Cathetogyrates) + + +==== Class †Noeggerathiopsida ==== +Order †Discinitiales +Order †Noeggerathiales +Order †Tingiales + + +==== Class †Aneurophytopsida ==== +Order †Scougonophytales +Order †Aneurophytales + + +==== Class †Archaeopteridopsida ==== +Order †Cecropsidales +Order †Archaeopteridales + + +==== Incertae sedis ==== +Order †Protopityales +Order †Stenokoleales + + +==== Clade Spermatophyta ==== +Order †Calamopityales +Order †Callistophytales +Order †Erdtmanithecales +Order †Hlatimbiales +Order †Umkomasiales +Class †Arberiopsida +Order †Aberiales +Order †Dicranophyllales +Class †Moresnetiopsida +Order †Moresnetiales +Order †Pullarithecales +Order †Tetrastichiales +Class †Lyginopteridopsida +Order †Hexapterospermales +Order †Lyginopteridales +Class †Pachytestopsida +Order †Codonospermales +Order †Pachytestales +Class †Peltaspermopsida +Order †Peltaspermales +Order †Sporophyllitales +Order †Trichopityales +Class †Phasmatocycadopsida +Order †Gigantopteridales +Order †Phasmatocycadales +Class †Pentoxylopsida +Order †Pentoxylales +Class †Dictyopteridiopsida +Order †Dictyopteridiales +Order †Lidgettoniales +Order †Rigbyales +Class †Cycadeoideopsida +Order †Fredlindiales +Order †Cycadeoideales +Class †Caytoniopsida +Order †Caytoniales +Class †Axelrodiopsida +Order †Axelrodiales +Class Pinopsida +†Subclass Pityidae +†Order Pityales +Subclass Cycadidae +Order ?†Noeggerathiopsidales +Order †Podozamitales +Order Cycadales (Cycads) +Subclass Ginkgoidae +Order †Hamshawviales +Order †Vladimariales +Order †Matatiellales +Order †Petriellales +Order †Czekanowskiales +Order Ginkgoales +Subclass Pinidae +Order †Cordaitales +Order †Dordrechtitales +Order †Vojnovskyales +Order †Buriadiales +Order †Ferugliocladales +Order †Ullmanniales +Order †Walchiales +Order †Voltziales +Order †Bernettiales +Order †Eoanthales +Order †Fraxinopsiales +Order Gnetales (incl. Ephedrales & Welwitschiales) +Order Pinales (Pines and allies) +Order Araucariales +Order Cupressales (Cypresses and allies) +Class Magnoliopsida +Subclass †Archaemagnoliidae +Order †Archaefructales +Superorder Amborellanae +Order Amborellales +Subclass Nymphaeidae +Order Nymphaeales +Subclass Illiciidae +Order Austrobaileyales +Subclass Chloranthidae +Order Chloranthales +Subclass Magnoliidae +Order Canellales +Order Piperales +Order Laurales +Order Magnoliales +Subclass Liliidae +Superorder Acoranae +Order Acorales +Superorder Alismatanae +Order Alismatales +Superorder Petrosavianae +Order Petrosaviales +Superorder Pandananae +Order Dioscoreales +Order Pandanales +Superorder Lilianae +Order Liliales +Superorder Orchidanae +Order Asparagales +Superorder Commelinids +Order Arecales +Order Commelinales +Order Zingiberales +Order Poales +Subclass Ceratophyllidae +Order Ceratophyllales +Clade Eudicots +Order ?†Sarbaicarpales +Subclass Ranunculidae +Order Ranunculales +Subclass Nelumbonidae +Order Proteales +Subclass Trochodendridae +Order Trochodendrales +Superorder Buxanae +Order Buxales +Superorder Myrothamnanae +Order Gunnerales +Clade Pentapetalae +Subclass Dilleniidae +Order Dilleniales +'Subclass Asteridae +Superorder Berberidopsidanae +Order Berberidopsidales +Superorder Santalanae +Order Santalales +Superorder Caryophyllanae +Order Caryophyllales +Superorder Cornanae +Order Cornales +Superorder Ericanae +Order Ericales +Superorder Asteranae +Order Apiales +Order Aquifoliales +Order Asterales +Order Bruniales +Order Dipsacales +Order Escalloniales +Order Paracryphiales +Superorder Lamianae +Order Boraginales +Order Garryales +Order Gentianales +Order Icacinales +Order Lamiales +Order Metteniusales +Order Solanales +Order Vahliales +Subclass Rosidae +Superorder Saxifraganae +Order Saxifragales +Superorder Vitanae +Order Vitales +Superorder Rosanae +Order Zygophyllales +Order Celastrales +Order Malpighiales +Order Oxalidales +Order Fabales +Order Cucurbitales +Order Fagales +Order Rosales +Superorder Myrtanae +Order Geraniales +Order Myrtales +Order Crossosomatales +Order Picramniales +Order Sapindales +Order Huerteales +Order Malvales +Order Brassicales + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-0.md b/data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-0.md new file mode 100644 index 000000000..4bfe58b1f --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-0.md @@ -0,0 +1,833 @@ +--- +title: "List of prehistoric bryozoan genera" +chunk: 1/2 +source: "https://en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:40.298558+00:00" +instance: "kb-cron" +--- + +This list of prehistoric bryozoans is an attempt to create a comprehensive listing of all genera that have ever been included in the bryozoa which are known from the fossil record. This list excludes purely vernacular terms. It includes all commonly accepted genera, but also genera that are now considered invalid, doubtful (nomina dubia), or were not formally published (nomina nuda), as well as junior synonyms of more established names, and genera that are no longer considered bryozoans. Naming conventions and terminology follow the International Code of Zoological Nomenclature, as indicated. + +== A == +Acanthocella +Acanthoceramoporella +Acanthocladia +Acanthoclema +Acanthodesia +Acantholaminatus +Acanthopora +Acanthoporella +Acanthoporidea +Acanthotrypa +Acanthotrypina +Acoscinopleura +Acrogenia +Actinopora +Actinotaxia +Actinotrypa +Actinotrypella +Actisecos +Adenifera +Adeona +Adeonella +Adeonellopsis +Admiratella +Aechmella +Aegyptopora +Aeolopora +Aetea +Aetomacladia +Aggregopora +Aimulosia +Aisenvergia +Akatopora +Alderina +Allantopora +Allonema +Alternifenestella +Altshedata +Aluverina +Alveolaria +Alwynopora +Alysidota +Amalgamoporous +Amalgamoprus +Amathia +Ammatophora +Amphiblestrella +Amphiblestrum +Amphimorsoniella +Amphiporella +Amplexopora +Amsassipora +Amurodictya +Anaphragma +Anaptopora +Anarthropora +Anastomopora +Andriopora +Angelopora +Anguisia +Anisotrypa +Anisotrypella +Annectocyma +Annunziopora +Anolotichia +Anomalotoechus +Anornithopora +Anotopora +Antropora +Aostipora +Apatotervia +Apertostella +Aplousina +Apsendesia +Arachnidid +Arachnidium +Arachnoidella +Arachnopusia +Araxopora +Arborocladia +Archaeofenestella +Archaeomeson +Archimedes +Arcticopora +Arctipoora +Argopora +Armillopora +Artchedella +Arthroclema +Arthropoma +Arthrostyloecia +Arthrostylus +Arthrotrypa +Ascodictyon +Ascopora +Ascoporella +Asperopora +Aspidopora +Aspidostoma +Assatkinella +Astralochoma +Astrovidictya +Astroviella +Astroviellina +Atacama (see Plesiothoa) +Atactopora +Atactoporella +Atactoporidra +Atactotoechus +Atagma +Atelesopora +Athrophragma +Atractosoecia +Attinopora +Auchenopora +Australofenestella +Australopolypora + +== B == +Bactrellaria +Bactridium +Bactropora +Baculopora +Bajolla +Balantiostoma +Balticopora +Balticoporella +Balticoporellina +Banastella +Baptopora +Bascomella +Bashkiriella +Basslederella +Bathosella +Bathystomella +Batopora +Batostoma +Batostomella +Batostomellina +Batrachopora +Beania +Beisselina +Beisselinopsis +Belorussipora +Berenicea +Biavicularium +Bicavea +Bicorbis +Bicornifera +Bicoronipora +Bicrisia +Bicrisina +Bidiastopora +Bifaxaria +Bifissurinella +Biflabellaria +Biflustra +Bimuropora +Biovicella +Biselenaria +Bisidmonea +Bitectipora +Bitubigera +Bivestis +Bobiesipora +Boreas +Boreasina +Botryllopora +Bracebridgia +Brachysoecia +Braiesopora +Brestopora +Brydonella +Bryocryptella +Bubnoffiella +Buffonella +Buffonellodes +Buria +Buskia +Buskopora +Bythopora +Bythotrypa + +== C == +Caberea +Caberoides +Calacanthopora +Calamotrypa +Callocladia +Callopora +Calloporella +Calloporina +Callotrypa +Calopora +Calpensia +Calpidopora +Calvetina +Calvina +Canalipora +Canda +Canupora +Canutrypa +Capillapora +Cardiarachnidium +Cardioecia +Carinifer +Carinodictya +Carinophylloporina +Carydiopora +Cassianopora +Castanopora +Casteropora +Catenariopsis +Catenicella +Cava +Cavaria +Cavarinella +Cavernella +Ceata +Ceidmonea +Cellaria +Cellarinella +Cellarinidra +Cellepora +Celleporaria +Celleporella +Celleporina +Cellulipora +Centronea +Ceramella +Ceramophylla +Ceramopora +Ceramoporella +Ceriocava +Ceriopora +Cerioporella +Cervella +Chainodictyon +Championodictya +Champlainopora +Chaperia +Characodoma +Charixa +Chartecytis +Chasmatopora +Chasmatoporina +Chasmazoon +Chazydictya +Cheethamia +Cheilohorneropsis +Cheilonella +Cheilopora +Cheiloporina +Cheilotrypa +Chelidozoum +Chilopora +Chisma +Chlidoniopsis +Chondraulus +Choristopetalum +Chorizopora +Christinella +Cianotremella +Cillia +Cinctipora +Circibiopora +Cladodictya +Clathropora +Clausa +Clausotrypa +Clavicava +Claviporella +Clavisparsa +Clavitubigera +Cleidochasma +Clinopora +Cliocystiramus +Cliotrypa +Clithriellum +Clonopora +Clypeina +Codonellina +Coelocaulis +Coeloclemis +Coelocochlea +Coelopora +Coelospiropora +Coleopora +Collapora +Collarina +Colletosia +Collura +Columnotheca +Condranema +Conescharellina +Conopeum +Conotubigera +Constellaria +Cookobryozoon +Copidozoum +Corbulipora +Cornuticella +Coronidmonea +Corymbopora +Corymboporella +Corynostylus +Corynotrypa +Coscinella +Cosciniopsis +Coscinium +Coscinoecia +Coscinopleura +Coscinotrypa +Costazia +Costula +Cothurnicella +Cranosina +Craspedopora +Craspedoporina +Crassalina +Crassicellepora +Crassimarginatella +Crassodiscopora +Crassohornera +Crateropora +Crepidacantha +Crepipora +Crepis +Crescis +Cribella +Cribellopora +Cribrendoecium +Cribrilaria +Cribrilina +Cricodictyum +Crisia +Crisidia +Crisidmonea +Crisiella +Crisina +Crisinella +Crisiona +Crisisina +Crisulipora +Crownopora +Crustopora +Cryptoglena +Cryptostomella +Cryptosula +Ctenopora +Cubifenestella +Cucullipora +Cuneatopora +Cupuladria +Cuvilliera +Cyclicopora +Cyclocites +Cyclocolposa +Cyclopelta +Cycloperiella +Cyclophaenopora +Cyclopora +Cycloporella +Cyclotrypa +Cylindropora +Cyphonella +Cyphotrypa +Cyrtopora +Cystiramus +Cystisella +Cystitrypa +Cystodictya +Cystomeson +Cystoporella +Cystostictoporus +Cytis + +== D == +Dacryonella +Dacryopora +Dacryoporella +Dakaria +Decurella +Decurtaria +Defrancia +Defranciopora +Dekayella +Dekayia +Dendroecia +Dentalitrya +Dentiporella +Desmatelesia +Desmediaperoecia +Desmeplatioecia +Desmepora +Diacanthopora +Diamesopora +Diancopora +Dianulites +Diastoporina +Diazipora +Dibunostoma +Diceratopora +Dichospiropora +Dichotrypa +Dicranopora +Dictuonia +Dictyoretmon +Didymosella +Dightonia +Dimorphocella +Dimorphocellaria +Dimorphostylus +Dionella +Diplobeisselina +Diplocava +Diploclema +Diplodesmepora +Diplopetalopora +Diplopholeous +Diploporaria +Diplorula +Diplosolen +Diplostenopora +Diplotresis +Diplotrypa +Discocytis +Discofascigera +Discoflustrellaria +Discoporella +Discosella +Discosparsa +Discotruncatulipora +Discotrypa +Discotrypina +Discotubigera +Discovibracella +Dishelopora +Disporella +Distansescharella +Distefanella +Disteginopora +Ditaxia +Ditaxipora +Ditaxiporina +Dittopora +Dittosaria +Diversipora +Duncanoclema +Duvergiera +Dybowskiella +Dybowskites +Dyoidophragma +Dyscritella +Dyscritellina +Dysnoetocella +Dysnoetopora + +== E == +Echinocava +Eichwaldictya +Elaphopora +Elea +Electra +Eliasopora +Ellisina +Ellisinidra +Emballotheca +Enallopora +Encicellaria +Enoplostomella +Ensiphragma +Ensipora +Entalophora +Entalophoroecia +Entomaria +Eodyscritella +Eofistulipora +Eoheteropora +Eohippotha +Eohornera +Eopachydictya +Eoscrupocellaria +Eosemicoscinium +Eostenopora +Eostenoporella +Epiactinotrypa +Eridocamplyus +Eridopora +Eridotrypa +Eridotrypella +Eridotrypellina +Erinella +Erkosonea +Escharella +Escharicellaria +Escharifora +Escharina +Escharipora +Escharoides +Escharopora +Esthoniopora +Esthonioporina +Esthoniporella +Etherella +Eucheilopora +Eucratea +Eulyra +Euritina +Europora +Eurydictya +Eurystomella +Eurystrotos +Eurythyrhombopora +Euspilopora +Evactinopora +Evactinostella +Exechonella +Exfenestella +Exidomonea +Exochella +Exochoecia + +== F == +Fabifenestella +Fasciculinopora +Fasciculipora +Fascigera +Fascipora +Favicella +Favositella +Fenestella +Fenestellata +Fenestepora +Fenesteverta +Fenestralia +Fenestrapora +Fenestrellina +Fenestrulina +Figularia +Filicava +Filicea +Filicrisia +Filicrisina +Filifascigera +Filiramoporina +Filisparsa +Filites +Fischerella +Fissuricella +Fistulamina +Fistulicanta +Fistuliphragma +Fistulipora +Fistuliporella +Fistuliporidra +Fistuliramus +Fistulocladia +Fistulotrypa +Flabellopora +Flabellotrypa +Flexifenestella +Floridina +Floridinella +Flustra +Flustrella +Flustrellaria +Foraripora +Foricula +Francopora +Frondipora +Frurionella +Fungella +Fusicellaria + +== G == +Galeopsis +Ganiella +Gargantua +Gastropella +Gaudryanella +Geinitzella +Geisopora +Gemellaria +Gemellipora +Gemelliporella +Gemelliporidra +Gemelliporina +Geminella +Gephyrophora +Gephyrotes +Gigantopora +Gilmouropora +Girtyopora +Girtyoporina +Glauconomella +Globulipora +Glossotrypa +Glyptopora +Goldfussitrypa +Goniocladia +Goniocladiella +Goniotrypa +Gortanipora +Goryunovia +Grammanotosoecia +Grammascosoecia +Grammella +Grammothoa +Graptodictya +Graptopora +Graptoporella + +== H == +Hagenowinella +Haimeina +Hallopora +Halloporina +Haplocephalopora +Haplooecia +Haplopoma +Haplopomella +Haplotrypa +Hapsidopora +Harmeriella +Haswellia +Hayasakapora +Helenopora +Helicopora +Heliotrypa +Helixotionella +Heloclema +Helopora +Hemeschara +Hemibashkirella +Hemicellaria +Hemicosciniopsis +Hemicyclopora +Hemieridotrypa +Heminematopora +Hemiphlactella +Hemiphragma +Hemiseptella +Hemismittina +Hemistylus +Hemitrypa +Hemitrypella +Hemiulrichostylus +Hennigopora +Herentia +Hernodia +Herpetopora +Hesperopora +Heteractis +Heterocella +Heteroconopeum +Heterocrisina +Heterohaplooecia +Heteropora +Heteroporella +Heterotrypa +Hexacanthopora +Hexagonella +Hexaporites +Hexites +Hiantopora +Hinaclema +Hincksina +Hincksipora +Hinganella +Hinganotrypa +Hippadenella +Hippaliosina +Hipperechonella +Hippiopora +Hippodiplosia +Hippoexechonella +Hippolyrula +Hippomenella +Hippomonavella +Hippophylactella +Hippopleurifera +Hippopodina +Hippopodinella +Hippoporella +Hippoporidra +Hippoporina +Hippopozoon +Hipposera +Hippothoa +Hippozeugosella +Hoeverella +Holoporella +Holostegopora +Homalostega +Homoeosolen +Homotrypa +Homotrypella +Hoplitaechmella +Hoplocheilina +Hopora +Hormerella +Hornera +Houzeauina +Hubeipora +Hunanopora +Hyalotoechus +Hyphasmopora +Hyporosopora +Hystricopora + +== I == +Iberostomata +Ichnopora +Ichthyorachis +Idioclema +Idiotrypa +Idmidronea +Idmonea +Idmonella +Idmoneoides +Ignotifenestella +Ignotrypa +Ikelarchimedes +Immergentia +Inconobotopora +Infundibulipora +Insignia +Intrapora +Inversiula +Ipmorella +Iraidina +Isotrypa +Isphairamella + +== J == +Jaculina +Jordanopora + +== K == +Kalevipora +Kallodictyon +Kalvariella +Kankopora +Kasakhstanella +Kazarchimedes +Kelestoma +Kenella +Kielanopora +Kielcepora +Kingopora +Kionidella +Klaucena +Kleidionella +Koldophos +Kronothoa +Kuarnbyella +Kukersella +Kunradina +Kyarnbyella +Kylonisa +Kysylschinopora + +== L == +Labioporella +Lacerna +Lacrimula +Lagarozoum +Lagenipora +Lagenosypho +Lagonoecia +Lagynopora +Laminopora +Lamottopora +Lamtshinopora +Lanarkopora +Lanceopora +Lanopora +Latereschara +Laterocavea +Laterocea +Lateroflustrellaria +Laterotecatia +Laterotubigera +Laxifenestella +Leeporina +Leioclema +Leiosella +Leiosoecia +Lekythionia +Lekythoglena +Lekythopora +Lepralia +Lepralina +Leptocheilopora +Leptopora +Leptotrypa +Leptotrypella +Levifenestella +Lichenalia +Lichenopora +Lichenotrypa +Liguloclema +Linotaxis +Lioclemella +Lioporida +Liripora +Lobopora +Lobosoecia +Locularia +Loculipora +Lophoclema +Lopholepsis +Loxophragma +Lunaferamita +Lunularia +Lunulites +Lyrocladia +Lyropora +Lyroporella +Lyroporidra \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-1.md b/data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-1.md new file mode 100644 index 000000000..9ecae6ff6 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera-1.md @@ -0,0 +1,783 @@ +--- +title: "List of prehistoric bryozoan genera" +chunk: 2/2 +source: "https://en.wikipedia.org/wiki/List_of_prehistoric_bryozoan_genera" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:40.298558+00:00" +instance: "kb-cron" +--- + +== M == +Macropora +Macroporina +Magnea +Magnederella +Mamillopora +Manzonella +Marcusodictyon +Marcusopora +Margaretta +Marginaria +Marquetta +Marssoniella +Marssonopora +Mastigophora (see Herentia) +Mastigophorella +Matherocladia +Matheropora +Matsutrypa +Maychella +Maychellina +Meandropora +Mecynoecia +Mediapora +Medisemicoscinium +Meekopora +Meekoporella +Megacanthopora +Megacanthoporina +Melicerita +Melicerita +Meliceritella +Meliceritites +Meliceritites +Membranipora +Membraniporella +Membraniporidra +Membraniporina +Membrendoecium +Meniscopora +Mesenteripora +Mesonea +Mesonopora +Mesostomaria +Mesotrypa +Mesotrypina +Metadictya +Metastenodiscus +Metelipora +Metracolposa +Metradolium +Metrarabdotos +Metrocrypta +Metroperiella +Microcampylus +Microecia +Micropora +Microporella +Microporina +Minilya +Minussina +Mirifenestella +Mitoclema +Mitoclemella +Mojczatrypa +Mollia +Mongoloclema +Mongolodictya +Monoceratopora +Monocerina +Monodesmopora +Monoporella +Monotrypa +Monotrypella +Monsella +Monticellaria +Monticulipora +Moorephylloporina +Morozovapora +Morozoviella +Morphasmopora +Mosathoa +Moyanopora +Moyerella +Mucronella +Multicavea +Multicrescis +Multifascigera +Multigalea +Multiphragma +Multisparsa +Multitubigera +Multizonopora +Mumiella +Murengoloclema +Murinopsia +Myagropora +Myriapora +Myriozoum +Mystriopora + +== N == +Nannopora +Nekhoroshoviella +Neliella +Nellia +Nemacanthclema +Nemacanthopora +Nemataxidra +Nemataxis +Nematifera +Nematopora +Nematoporella +Nematotrypa +Neoeridocampilus +Neoeridotrypella +Neoretenoa +Neoreteporina +Neorhombopora +Neotrematopora +Nephropora +Neuropora +Neuroporella +Nevianopora +Newportopora +Nicholsonella +Nicklesopora +Niigaella +Nikiforopora +Nikiforovella +Nipponstenopora +Notamia +Notoplagioecia +Nudonychocella +Nudymiella + +== O == +Oanduella +Oanduellina +Obliquostoma +Ochetosella +Ochetosellina +Odonotrypa +Odontionella +Oeciophylloporina +Ogbinopora +Ogiva +Ogivalia +Ogivalina +Oligotopora +Omalosecosa +Oncousoecia +Onychocella +Onychocellaria +Opisthornithopora +Orbignyella +Orbignyopora +Orbipora +Orbitulipora +Orectodictya +Orthopora +Osburnostylus +Osculipora +Osthimosia +Otionella +Otopora +Ottoseetaxis + +== P == + +Pachycraspedon +Pachydera +Pachydictya +Pachystomaria +Pachyteichopora +Pachythecella +Pakridictya +Palaeocoryne +Palaeocrisidia +Paleoatactoechus +Paleschara +Palmicellaria +Pamirella +Pancheilopora +Papillalunaria +Parachasmatopora +Paracrescis +Parafenestalia +Parafenestella +Paralhederella +Paralioclema +Parametelipora +Paranicklespora +Paraseptopora +Parasmittina +Parastenodiscus +Paratrachytoechus +Paratretocycloecia +Paravinella +Parellisina +Parleiosoecia +Parmularia (see Lanceopora) +Parobeisselina +Partretocycloecia +Parvohallopora +Pasythea +Patellipora +Patenaria +Patsyella +Paucipora +Pavobeisselina +Pavolunuites +Pedrogopora +Pelmatopora +Penetrantia +Pennipora +Penniretepora +Perfodiastopora +Pergensella +Perigastrella +Peripora +Periporosella +Peristomella +Permofenestella +Permoheloclema +Permoleioclema +Permopora +Peronopora +Persiopora +Pesnastylus +Petalopora +Petaloporella +Petalostegas +Petalotrypa +Petigopora +Petraliella +Phacelopora +Phaenophragma +Phaenopora +Phaenoporella +Pharopora +Phidolopora +Phoceana +Pholidopora +Phonicosia +Phormopora +Phractopora +Phractoporella +Phragmophera +Phragmopora +Phragmotrypa +Phrynopora +Phylactella +Phylactellipora +Phyllodictya +Phylloporina +Pictatella +Pileotrypa +Pinacotrypa +Pinegopora +Pinnatopora +Pinnctoporella +Pithodella +Plagioecia +Plagiosmittia +Planicellaria +Platonea +Platyglena +Plethopora +Plethoporella +Pleurolyrula +Pleuronea +Pleuroschizella +Pliophloea +Pnictopora +Pnictoporopsis +Podljassopra +Polyascosoecia +Polyascosoeciella +Polycephalopora +Polyceratopora +Polycylindricus +Polyfenestella +Polypora +Polyporella +Polyspinopora +Polyteichus +Porella +Poriceata +Poricella +Poricellaria +Porina +Porismittina +Porometra +Poropeltarion +Poroplagioecia +Praesemicoscinium +Prasopora +Prasoporina +Prattia +Prenantia +Primarella +Primorella +Prismopora +Proavella +Proboscina +Proboscinopora +Prodromopora +Profistulipora +Promediapora +Prophyllodictya +Prosotopora +Prosthenoecia +Prostomaria +Protocrisina +Protoretepora +Proutella +Pseudoascopora +Pseudobatostomella +Pseudobeisselma +Pseudofrondipora +Pseudohornera +Pseudoisotrypa +Pseudolunulites +Pseudonematopora +Pseudopachydictya +Pseudoseptopora +Pseudoseriopora +Pseudostege +Pseudostictoporella +Pseudotervia +Pseudothyracella +Pseudounitrypa +Psilosecos +Psilosolen +Pterocella +Pteropora +Ptilocella +Ptilodictya +Ptilofenestella +Ptilofenestella +Ptiloporella +Ptiloporina +Ptilotrypa +Ptilotrypina +Ptylopora +Puellina +Puncturiella +Pushkinella +Pustulopora +Pycnobasis +Pycnopora +Pyricavea +Pyripora +Pyriporella +Pyriporopsis +Pyrulella +Pywackia + +== Q == +Qilianopora +Quadricellaria +Quadriscutella +Quadrisemicoscinium +Quasitrilaminopora + +== R == +Radicipora +Radiocavaria +Radiofascigera +Radiopora +Radiotrypa +Radulopora +Ralfina +Ralfinella +Ramia +Ramipora +Ramiporalia +Ramiporella +Ramiporidra +Ramofilisparsa +Ramphonotus +Rarifenestella +Realeksella +Rectifenestella +Rectonychocella +Reginella +Reptadeonella +Reptaria +Reptescharipora +Reptoceritites +Reptoclausa +Reptofascigera +Reptolunites +Reptomultelea +Reptomulticava +Reptomulticlausa +Reptomultisparsa +Reptonodicava +Retecava +Retelea +Retenoa +Retepora +Reteporellina +Reteporidra +Reteporina +Reticrisina +Reticulipora +Reussia +Revalopora +Revalotrypa +Revssirella +Rhabdomeson +Rhabdopora +Rhabdotometra +Rhacheopora +Rhagasostoma +Rhammatopora +Rhamphostomella +Rhebasia +Rhenanerella +Rhiniopora +Rhinopora +Rhinoporella +Rhipidiopora +Rhombocladia +Rhombopora +Rhomboporella +Rhombotrypa +Rhombotrypella +Rimulostoma +Ripisoecia +Romancheina +Ropalonaria +Rosacilla +Rosseliana +Rotoporina +Rozonovia +Ruzhencevia +Ryhopora + +== S == +Saevitella +Saffordotaxis +Sagenella +Salairia +Salicornaria +Samaria +Sandalopora +Sardesonina +Savignyella +Scalaripora +Scenellopora +Sceptropora +Schischatella +Schiscjkatella +Schismopora +Schismoporella +Schistacanthopora +Schizaropsis +Schizemiella +Schizemiellopsis +Schizobathysella +Schizobrachiella +Schizomavella +Schizoporella +Schizoporellopsis +Schizoretepora +Schizorthosecos +Schizosmittina +Schizostomella +Schizotheca +Schizotrema +Schizotremopora +Schulgina +Scorpiodina +Scruparia +Scrupocellaria +Scuticella +Seelandia +Seguenziella +Selenaria +Selenopora +Semicea +Semicinctipora +Semiclausa +Semicoscinium +Semicytella +Semicytis +Semielea +Semieschara +Semiescharinella +Semifascipora +Semifenestella +Semifungella +Semihaswellia +Semilaterotubigera +Semimulticavea +Seminodicrescis +Semiopora +Semitubigera +Septatopora +Septopora +Serietubigera +Seriopora +Serpentipora +Sertella +Setosella +Setosellina +Setosinella +Shishoviclema +Shylgapora +Sibiredictya +Silenella +Silenopora +Silvaseptopora +Sinoatactoechus +Sinupetraliella +Siphodictyum +Siphoniotyphlus +Siphonoporella +Skylonia +Smittina +Smittinella +Smittipora +Smittistoma +Smittoidea +Solenonychocella +Solenophragma +Sonninopora +Sparsicavea +Sparsicytis +Sparsiporina +Spathipora +Spatiopora +Speotrypa +Sphaerogypina +Sphaeropora +Sphaerulobryozoon +Sphenella +Sphragiopora +Spinicharixa +Spinofenestella +Spinopora +Spira +Spirentolophora +Spirillopora +Spiropora +Spiroporina +Spridmonea +Staffordotaxis +Stamenocella +Stathmepora +Staurosteginopora +Steginopora +Steginoporella +Stellahevaformis +Stellatodictya +Stellipora +Stellocavea +Stenocladia +Stenodiscus +Stenophragmidium +Stenopora +Stenoporella +Stenopsella +Stenopsis +Stenosipora +Stephanodesma +Stephanollona +Stephanosella +Stephanotrema +Steraechmella +Stereotoechus +Stichocados +Stichomicropora +Stichopora +Stichoporina +Stichtostega +Stictocella +Stictopora +Stictoporella +Stictoporellina +Stictoporina +Stictotrypa +Stigmatella +Stigmatoechos +Stolonicella +Stomachetosella +Stomatopora +Stomatoporina +Stomatoporopsis +Stomhypselosaria +Streblascopora +Streblocladia +Streblopax +Streblotrypa +Streblotrypella +Stromatotrypa +Strongylopora +Strophipora +Strotopora +Stylopoma +Subretepora +Sulcocava +Sulcoretepora +Supercytis +Sylonika +Synaptacella +Synnotum +Synocladia +Synocladiopsis +Syringoclemis +Systenostoma + +== T == +Tabulipora +Tabuliporella +Taeniocellana +Taeniodictya +Taeniopora +Taenioporella +Taenioporina +Talmontipora +Tamaroclema +Taphrostoma +Taractopora +Tarphophragma +Tavayzopora +Tebitopora +Tegella +Teichopora +Telopora +Terebellaria +Terebripora +Tervia +Tessaradoma +Tetragonoecia +Tetraplaria +Tetrapora +Tetratoechus +Teuchopora +Thalamoporella +Thamniscus +Thamnotrypa +Thecatia +Theonoa +Tholopora +Thoracopora +Thornipora +Thyracella +Timanodictya +Timanotrypa +Trachytoechus +Trataucladia +Trematella +Trematooecia +Trematopora +Trematoporina +Tremocoscinopleura +Tremogasterina +Tremolyrula +Tremopora +Tremoschizodina +Tremotoichos +Trepocryptopora +Trepostomina +Treptopora +Tretocycloecia +Tretonea +Tretosina +Tricephalopora +Tricolpopora +Tricornicella +Trigonodictya +Trigonopora +Trilophopora +Triplopora +Triplozooecia +Triporula +Triznella +Trochiliopora +Trochopora +Trochosodon +Tropidopora +Truncatula +Truncatulipora +Trypematella +Trypocella +Trypostega +Tshokrakopora +Tubescharina +Tubigera +Tubigerina +Tubiporella +Tubitrabecularia +Tubucella +Tubucellaria +Tubulipora +Tubulitrypa +Turbicellopora +Tylopora + +== U == +Ubaghsia +Uldzapora +Ulrichostylus +Ulrichotrypa +Ulrichotrypella +Umbonula +Umbrellina +Uniavicularia +Unicrisia +Unicytis +Unitrypa +Unitubigera +Uralotrypa +Utgaardostylus +Utropora + +== V == +Vasalemmapora +Velumella +Verella +Verminaria +Veroclema +Vesicularia +Vibracella +Vibracellina +Vibraculina +Vincularia +Vinella +Virgatella +Virgocella +Vittaticella +Voigtella +Voigtia +Voigtiella +Voigtopora +Volgia +Volnovachia +Volviflustrellaria +Voorthuyseniella + +== W == +Wassypora +Watersipora +Wawalia +Wilbertopora +Wjatkella +Wolinella +Woodipora +Worthenopora +Wyseotrypa + +== X == +Xaveropora +Xenotrypa + +== Y == +Yangotrypa +Ybseloscoecia +Yichangopora +Yunnanopora + +== Z == +Zagorsekia +Zigzagopora +Zlambachia +Zonopora +Zozariella + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_primates_by_population-0.md b/data/en.wikipedia.org/wiki/List_of_primates_by_population-0.md new file mode 100644 index 000000000..a5ca9b796 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_primates_by_population-0.md @@ -0,0 +1,26 @@ +--- +title: "List of primates by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_primates_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:17.360838+00:00" +instance: "kb-cron" +--- + +This is a list of primate species by estimated global population. This list is not comprehensive as not all primates have had their numbers quantified. +Unless specified in the Notes section, primary population values given are for number of mature individuals. + + +== Species without population estimates == + + +== See also == + +Lists of organisms by population +Lists of mammals by population +Human population +The World's 25 Most Endangered Primates + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_proteins-0.md b/data/en.wikipedia.org/wiki/List_of_proteins-0.md new file mode 100644 index 000000000..1b5218437 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_proteins-0.md @@ -0,0 +1,135 @@ +--- +title: "List of proteins" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_proteins" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:41.469510+00:00" +instance: "kb-cron" +--- + +Proteins are a class of macromolecular organic compounds that are essential to life. They consist of a long polypeptide chain that usually adopts a single stable three-dimensional structure. They fulfill a wide variety of functions including providing structural stability to cells, catalyzing chemical reactions that produce or store energy or synthesize other biomolecules including nucleic acids and proteins, transporting essential nutrients, or serving other roles such as signal transduction. They are selectively transported to various compartments of the cell or in some cases, secreted from the cell. +This list aims to organize information on how proteins are most often classified: by structure, by function, or by location. + + +== Structure == +Proteins may be classified as to their three-dimensional structure (also known a protein fold). The two most widely used classification schemes are: + +CATH database +Structural Classification of Proteins database (SCOP) +Both classification schemes are based on a hierarchy of fold types. At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. +While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. Finally other proteins appear not to adopt any stable conformation and are referred to as intrinsically disordered. +Proteins frequently contain two or more domains, each have a different fold separated by intrinsically disordered regions. These are referred to as multi-domain proteins. + + +== Function == + +Proteins may also be classified based on their cellular function. A widely used classification is PANTHER (protein analysis through evolutionary relationships) classification system. + + +=== Structural === +Protein#Structural proteins + + +=== Catalytic === +Enzymes classified according to their Enzyme Commission number (EC). Note that strictly speaking, an EC number corresponds to the reaction the enzyme catalyzes, not the protein per se. However each EC number has been mapped to one or more specific proteins. + +List of enzymes +EC 1: Oxidoreductases +EC 2: Transferases +EC 3: Hydrolases +EC 4: Lyases +EC 5: Isomerases +EC 6: Ligases +EC 7: Translocases + + +=== Transport === +Transport protein + +Ion channel +Solute carrier family + + +=== Immune === +Acute phase protein +Antibody +Chemokines and their receptors +Cytokines and their receptors +MHC Class I +MHC Class II +Pattern recognition receptors +Complement System + + +=== Genetic === +DNA/RNA synthesis +DNA repair +replication +transcription (Transcription factor, transcriptional coregulator) + + +=== Signal transduction === +Signal transduction + + +== Sub-cellular distribution == + +Proteins may also be classified by which subcellular compartment they are found. + + +=== Nuclear === +Nuclear proteins + + +=== Cytosolic === +Cytosolic proteins + + +=== Cytoskeletal === +Cytoskeletal proteins + + +=== Organelle === + + +==== Endoplasmic reticulum ==== +Endoplasmic reticulum resident protein + + +==== Lysosomal ==== + + +==== Mitochondrial ==== +Mitochondrial DNA that encode mitochondrial proteins (note that some mitochondrial proteins are encoded by nuclear DNA) + + +==== Chloroplast ==== +Chloroplast DNA that encode chloroplast proteins + + +=== Cell membrane === +Membrane protein + +Integral membrane protein +Peripheral membrane protein + + +=== Extracellular matrix === +Extracellular matrix proteins + + +=== Plasma === +Blood protein + + +== Species distribution == +Mammalian proteins +Vertebrate proteins +Plant proteins +Bacterial proteins +Archaeal proteins +Viral proteins + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md new file mode 100644 index 000000000..9397ea9f6 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-0.md @@ -0,0 +1,83 @@ +--- +title: "List of red seaweeds of the Cape Peninsula and False Bay" +chunk: 1/6 +source: "https://en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:48.020280+00:00" +instance: "kb-cron" +--- + +This is a list of red seaweeds recorded from the oceans bordering The Cape Peninsula in South Africa from Melkbosstrand on the West Coast to Cape Hangklip on the South Coast. +This list comprises locally used common names, scientific names with author citation and recorded ranges. Ranges specified may not be the entire known range for the species, but should include the known range within the waters surrounding the Republic of South Africa. +Red seaweed refers to thousands of species of macroscopic, multicellular, marine algae in the taxon Rhodophyta +The marine ecology is unusually varied for an area of this size, as a result of the meeting of two major oceanic water masses near Cape Point, and the park extends into two coastal marine bioregions. The ecology of the west or "Atlantic Seaboard" side of the Cape Peninsula is noticeably different in character and biodiversity to that of the east, or "False Bay" side. Both sides are classified as temperate waters, but there is a significant difference in average temperature, with the Atlantic side being noticeably colder on average. +List ordering and taxonomy complies where possible with the current usage in Algaebase, and may differ from the cited source, as listed citations are primarily for range or existence of records for the region. +Sub-taxa within any given taxon are arranged alphabetically as a general rule. +Details of each species may be available through the relevant internal links. Synonyms may be listed where useful. + +== Class: Bangiophyceae == + +=== Order: Bangiales === + +==== Family Bangiaceae ==== +Bangia atropurpurea (Mertens ex Roth) C.Agardh 1824, syn. Conferva atropurpurea Mertens ex Roth 1806, Oscillatoria atropurpurea (Roth) C.Agardh 1817, Bangia fuscopurpurea var. atropurpurea (Roth) Lyngbye 1819, Bangia atropurpurea (Mertens ex Roth) C.Agardh 1824, Bangiella atropurpurea (Roth) Gaillon 1833, Bangiadulcis atropurpurea (Roth) W.A.Nelson 2007, (Cosmopolitan) +Purple laver, Porphyra capensis Kützing 1843, (Abundant on whole of west coast extending into Namibia and along south coast of Western and Eastern Cape. Endemic) +Pyropia gardneri (G.M.Smith & Hollenberg) S.C.Lindstrom in Sutherland et al. 2011, syn. Porphyrella gardneri G.M.Smith & Hollenberg 1943, Porphyra gardneri (G.M.Smith & Hollenberg) M.W.Hawkes 1977, (Cape of Good Hope to Brandfontein) +Pyropia saldanhae (Stegenga, J.J.Bolton & R.J.Anderson) J.E.Sutherland in Sutherland et al. 2011, syn. Porphyra saldanhae Stegenga, Bolton & R.J.Anderson 1997, (Hondeklip Bay and Olifantsbos, endemic) + +=== Order: Porphyridiales === + +==== Family Phragmonemataceae ==== +Neevea cf. repens Batters 1900, (Hout Bay) + +== Class: Compsopogonophyceae == + +=== Order: Erythropeltidales === + +==== Family Erythrotrichiaceae ==== +Erythrocladia cf. polystromatica P.J.L.Dangeard 1932, (St James, False Bay and Cape Hangklip) +Erythrotrichia carnea (Dillwyn) J.Agardh 1883, syn. Erythrocladia carnea, Conferva carnea Dillwyn 1807, Bangia ciliaris subsp. pulchella (Harvey) De Toni 1897, (Probably fairly common, but South African distribution uncertain) +Erythrotrichia welwitschii (Ruprecht) Batters 1902, syn. Cruoria welwitschii Ruprecht 1850, (Cape of Good Hope and False Bay extending eastwards at least as far as Port Elizabeth) +Membranella africana Stegenga, Bolton & Anderson 1997, (Cape of Good Hope at least as far as Port Alfred) +Porphyrostromium boryanum (Montagne) P.C.Silva in Silva, Basson & Moe 1996, Porphyra boryana Montagne 1846, Erythrotrichia boryana (Montagne) Berthold 1882, Phyllona boryana (Montagne) Kuntze 1891, Erythrotrichopeltis boryana (Montagne) Kornmann 1984, Porphyrostromium boryanum (Montagne) M.J.Wynne 1986, (Yzerfontein to Oatlands Point, False Bay) +Sahlingia subintegra (Rosenvinge, 1909) Kornmann 1989, syn. Erythrocladia subintegra Rosenvinge 1909, Erythrocladia irregularis f. subintegra (Rosenvinge) Garbary, Hansen & Scagel 1981. Erythropeltis subintegra (Rosenvinge) Kornmann & Sahling 1985, Erythrotrichopeltis subintegra (Rosenvinge) Kornmann & Sahling 1985, (Worldwide – probably widely distributed in SA ) + +== Class: Florideophyceae == + +=== Order: Acrochaetiales === + +==== Family Acrochaetiaceae ==== +Acrochaetium brebneri (Batters) G.Hamel 1928, syn. Rhodochorton brebneri Batters 1897, Chantransia brebneri (Batters) Rosenvinge 1909, Audouinella brebneri (Batters) P.S.Dixon 1976, (False Bay side of the Cape Peninsula) +Acrochaetium balliae (Stegenga), nom. illeg. syn. Audouinella balliae Stegenga 1985, (Port Nolloth to Hout Bay) +Acrochaetium catenulatum M.A.Howe 1914, (Namibia to Eastern Cape) +Acrochaetium endozoicum (Darbishire) Batters 1902, syn. Chantransia endozoica Darbishire 1899, Rhodochorton endozoicum (Darbishire) Drew 1928, Audouinella endozoica (Darbishire) P.S.Dixon 1976, (Cape Peninsula) +Acrochaetium moniliforme (Rosenvinge) Børgesen 1915, Chantransia moniliformis Rosenvinge 1909, Rhodochorton moniliforme (Rosenvinge) Drew 1928, Kylinia moniliformis (Rosenvinge) Kylin 1944, Chromastrum moniliforme (Rosenvinge) Papenfuss 1945, Audouinella moniliformis (Rosenvinge) Garbary 1979, (False Bay eastward at least as far as Transkei) +Acrochaetium plumosum (K.M.Drew) G.M.Smith 1944, syn. Colaconema plumosum (Drew) Woelkerling 1971, Rhodochorton Plumosum Drew 1928, (Hondeklip Bay to Betty's Bay) +Acrochaetium reductum (Rosenvinge) G.Hamel 1927, syn. Chantransia reducta Rosenvinge 1909, (Between False Bay and Plettenberg Bay) +Acrochaetium secundatum (Lyngbye) Nägeli 1858, syn. Callithamnion daviesii var. secundatum Lyngbye 1819, (Namibia to False Bay) +Audouinella occulta H.Stegenga 1985, (Hout Bay) +Audouinella monorhiza (Stegenga) Garbary 1987, syn. Colaconema monorhiza Stegenga 1985, (Noordhoek and Olifantsbos, Cape Peninsula) +Audouinella pectinata (Kylin) Papenfuss 1945, syn. Chantransia pectinata Kylin, 1906, (Doring Bay to Olifantsbos) +Audouinella spongicola (Weber-van Bosse) Stegenga 1985, syn. Acrochaetium spongicola Weber-van Bosse 1921, (Hout Bay to Bird Island, Eastern Province) + +=== Order Balliales === + +==== Family Balliaceae ==== +Ballia callitricha (C.Agardh) Kützing 1843, syn. Sphacelaria callitricha C.Agardh 1824, (West side of Cape Peninsula to Cape Agulhas) +Ballia sertularioides (Suhr) Papenfuss 1940, syn. Callithamnion sertularioides Suhr 1840, (Lüderitz in Namibia to Hout Bay, Southern African endemic) + +=== Order Bonnemaisoniales === + +==== Family Bonnemaisoniaceae ==== +Asparagopsis armata Harvey 1855syn. Falkenbergia rufolanosa (Harvey) F.Schmitz in Engler & Prantl 1897, (Platbank, Cape Peninsula eastwards) +Bonnemaisonia hamifera Hariot 1891, (Known from one collection at Strandfontein, False Bay) +Delisea flaccida (Suhr) Papenfuss 1940, syn. Sphaerococcus flaccidus Suhr 1834, (Olifantsbos on the Cape Peninsula eastwards) + +=== Order Ceramiales === + +==== Family Callithamniaceae ==== +Aglaothamnion hookeri (Dillwyn) Maggs & Hommersand 1993, syn. Conferva hookeri Dillwyn 1809, Callithamnion hookeri (Dillwyn) S.F.Gray 1821, (Namibia to East London) +Callithamnion stuposum Suhr 1840, syn. Phlebothamnion stuposum (Suhr) Kützing 1843, Spongoclonium stuposum (Suhr) De Toni 1903, (Swartklip to KwaZulu-Natal) +Callithamnion sp. indet. (Cape Peninsula to East London) +Heteroptilon pappeanum (Kützing) Hommersand in Hommersand, D.W. Freshwater, J. López-Bautista, & S. Fredericq 2006, syn. Euptilota pappeana Kützing 1849, (Hondeklipbaai to Cape Agulhas, endemic) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md new file mode 100644 index 000000000..5c2737bd9 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-1.md @@ -0,0 +1,77 @@ +--- +title: "List of red seaweeds of the Cape Peninsula and False Bay" +chunk: 2/6 +source: "https://en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:48.020280+00:00" +instance: "kb-cron" +--- + +==== Family Ceramiaceae ==== +Antithamnion diminuatum var. polyglandulum Stegenga 1986, (Olifantsbos in the southern Cape Peninsula eastward to KwaZulu-Natal) +Antithamnion pseudoarmatum Stegenga 1986, (Olifantsbos and Brandfontein, endemic) +Antithamnionella tasmanica Wollaston 1968, (Kalk Bay to Kowie River) +Antithamnionella tormentosa Stegenga 1986, (Cape Peninsula from Three Anchor Bay to Muizenberg, endemic) +Antithamnionella verticillata (Suhr) Lyle 1922, syn. Callithamnion vertillatum Suhr 1840, Antithamnion verticillatum (Suhr) De Toni 1903, (Swartklip in False Bay to Transkei) +Bornetia repens Stegenga 1985, (Swartklip in False Bay to Transkei, possibly KwaZulu-Natal) +Callithamniella capensis Simons 1970, (Muizenberg to East London, endemic) +Callithamnion stuposum Suhr 1840, syn. Phlebothamnion stuposum (Suhr) Kützing 1843, Spongoclonium stuposum (Suhr) De Toni 1903, (Rare on weat coast, common on south coast and KwaZulu-Natal at least as far north as Mabibi) +Flaccid kelp-weed, Carpoblepharis flaccida (J.V.Lamouroux) Kützing 1849, syn. Ptilota flaccida (J.V.Lamouroux) C.Agardh 1822, Delesseria flaccida J.V.Lamouroux 1813, (Namibia to the Kei river, Southern African endemic) +Carpoblepharis minima E.S.Barton 1893, (Möwe Bay in Namibia to Buffels Bay on the Cape Peninsula) +Centroceras clavulatum (C.Agardh) Montagne 1846, syn. Ceramium clavulatum C.Agardh 1822, Spyridia clavulata (C.Agardh) J.Agardh 1842, (Whole southern African coast) +Centroceras distichum Okamura 1934, (Cape Hangklip) +Curl-claw, Centroceras spp. +Beaded ceramium, Ceramium arenarium Simons 1966, (Swakopmund in Namibia to East London, Southern African endemic) +Black-red ceramium, Ceramium atrorubescens Kylin, 1938. +Ceramium aff. callipterum Mazoyer 1938, (West side of southern Cape Peninsula) +Ceramium camouii E.Y.Dawson 1944, (Cape Point eastwards along south coast) +Cape ceramium, Ceramium capense Kützing 1841, (Lüderitz to Kommetjie, endemic) +Ceramium centroceratiforme Simons 1966, (Cape Hangklip to Kei River, endemic) +Ceramium dawsonii A.B.Joly 1957, (False Bay eastward along entire Cape south coast) +Ceramium glanduliferum Kylin 1938, (Sea Point on Cape Peninsula eastward into KwaZulu-Natal, Southern African endemic) +Coarse ceramium, Ceramium obsoletum C.Agardh 1828, (From Namibia south and eastwards along the whole Cape South coast, Southern African endemic) +Ceramium papenfussianum Simons 1966, (Primarily a West Coast species, endemic) +Flat-fern ceramium, Ceramium planum Kützing 1849, (Swakopmund in Namibia to False Bay. Southern African endemic) +Ceramium tenerrimum (G.Martens) Okamura 1921, syn. Hormoceras tenerrimum G.Martens 1866, (Whole of Cape west coast and east to Knysna) +Compsothamnionella sciadophila Stegenga 1990, (Found once at Muizenberg, endemic) +Crouania attenuata (C.Agardh) J.Agardh 1842, syn. Mesogloia attenuata C.Agardh 1824, (Kalk Bay eastward into tropical East Africa) +Crouania francescoi Cormaci, G.Furnari & Scammacca 1978, (False Bay eastwards to northern KwaZulu-Natal) +Laurenciophila minima Stegenga 1986, (Clovelly in False Bay to Kowie river, endemic) +Microcladia gloria-spei Stegenga 1986, (Port Nolloth to Southern Cape Peninsula), +Platythamnion capense Stegenga 1986, (Only known from Platboombaai, endemic) +Pterothamnion recurvatum (Wollaston) Athanasiadis & Kraft 1994, syn. Platythamnion recurvatum E.M.Wollaston 1972, (Paternoster to Olifantsbos, Port Alfred) + +==== Family Callithamniaceae ==== +Aristocratic plume-weed, Callithamnion collabens (Rudolphi) L.McIvor & Maggs 2002, syn. Asperocaulon collabens Rudolphi 1831, Aristothamnion collabens (Rudolphi) Papenfuss 1968, (Namibia to Port Alfred, Southern African endemic) +Iridescent plume-weed, Callithamnion stuposum Suhr, 1840 + +==== Family Dasyaceae ==== +Dasya echinata Stegenga, Bolton & R.J.Anderson 1997, (Brandfontein, Strandfontein in False Bay, and Waterloo Bay in Eastern Cape, endemic) +Bottlebrush, Dasya scoparia Harvey in J. Agardh 1841, (Lambert's Bay to East London), (Lamberts Bay to Mabibi in northern KwaZulu-Natal) +Heterosiphonia arenaria Kylin 1938, (Swartklip. Brandfontein, and Port Elizabeth to East London, endemic) +Heterosiphonia crispa (Suhr) Falkenberg 1901, syn. Dasya crispa Suhr 1840, (Lamberts Bay to KwaZulu-Natal, endemic) +Heterosiphonia dubia (Suhr) Falkenberg 1901, syn. Dasya dubia Suhr 1840, (Paternoster to KwaZulu-Natal, Southern African endemic) +Heterosiphonia pellucida (Harvey) Falkenberg 1901, syn. Dasya pellucida Harvey 1849, (Lamberts Bay to Brandfontein, endemic) + +==== Family Delesseriaceae ==== +Acrosorium acrospermum (J.Agardh) Kylin 1938, Plain acrosorium, syn. Nitophyllum ascospermum J.Agardh 1852, (False Bay to Eastern Cape, endemic) +Acrosorium maculatum (Sonder ex Kützing) Papenfuss 1940, syn. Aglaophyllum maculatum Sonder ex Kützing 1866, Nitophyllum uncinatum var. maculatum (Sonder ex Kützing) De Toni 1900, (Southern Cape Peninsula to KwaZulu-Natal) +Acrosorium ciliolatum (Harvey) Kylin 1924, crled acrosorium, syn. Nitophyllum ciliolatum Harvey 1855, Aglaophyllum ciliolatum (Harvey) Kützing 1869, Nitophyllum venulosum Zanardini 1866, Acrosorium venulosum (Zanardini) Kylin 1924, (as A. venulosum, Kommetjie to KwaZulu-Natal) (as A. ciliatum, Kommetjie eastward extending into KwaZulu-Natal at least as far as Sodwana Bay) +Apoglossum ruscifolium (Turner) J.Agardh 1898, syn. Fucus ruscifolius Turner 1802, Delesseria ruscifolia (Turner) J.V.Lamouroux 1813, (Oudekraal to Brandfontein) +Bartoniella crenata (J.Agardh ex Mazza) Kylin 1924, syn. Phitymophora crenata J.Agardh ex Mazza 1908, (Muizenberg and Cape Hangklip at least as far as Mission Rocks, endemic) +Black spot, Botryocarpa prolifera Greville 1830, (Namibia to southern Cape Peninsula) +Botryoglossum, Botryoglossum platycarpum (Turner) Kützing 1843, syn. Fucus platycarpus Turner 1809, Delesseria platycarpa (Turner) J.V.Lamouroux 1813, Phyllophora platycarpa (Turner) Greville ex Krauss 1846, Nitophyllum platycarpum (Turner) J.Agardh 1876, (Namibia to Cape of Good Hope. Southern African endemic) +Erythroglossum sp. indet. (Glencairn to Hluleka, endemic) +Gonimophyllum africanum M.T.Martin & M.A.Pocock 1953, (Table Bay to Kei River) +Haraldiophyllum bonnemaisonii (Kylin) A.D.Zinova 1981, syn. Myriogramme bonnemaisonii Kylin 1924, Nitophyllum bonnemaisonii (Kylin) Kylin 1934, (Kommetjie to Muizenberg on the Cape Peninsula) +Veined oil-weed, Hymenena venosa (Linnaeus) Krauss 1846, syn. Fucus venosus Linnaeus 1771, Delesseria venosa (Turner) J.V.Lamouroux 1813, (Namibia to southern Cape Peninsula) +Martensia elegans Hering 1841, syn. Capraella elegans (Harvey) J.De Toni 1936, Mesotrema elegans (Hering) Papenfuss 1942, (Common south coast species, extending into KwaZulu-Natal at least as far as Sodwana Bay) +Myriogramme eckloniae Stegenga, Bolton & R.J.Anderson 1997, (Drift material at Muizenberg, endemic) +Myriogramme livida (J.D.Hooker & Harvey) Kylin 1924, syn. Nitophyllum lividum J.D.Hooker & Harvey 1845, Cryptopleura livida (J.D.Hooker & Harvey) Kützing 1868, (Swakopmund to Kommetjie) +Veined tongues, Neuroglossum binderianum Kützing 1843, (Namibia to southern Cape Peninsula) +Papenfussia laciniata (Harvey) M.D. Guiry 2005?, syn. Pollexfenia laciniata Harvey 1844, (Both sides of the Cape Peninsula, endemic) +Frilly broekies, Paraglossum papenfussii (M.J.Wynne) S.-M.Lin, Fredericq & Hommersand, 2012, also recorded as syn. Delesseria papenfussii M.J.Wynne 1984, (Port Nolloth to Brandfontein. Southern African endemic) +Platyclinia sp. (Olifantsbos) +Platysiphonia intermedia (Grunow) M.J.Wynne 1983, syn. Sarcomenia intermedia Grunow 1867, (Port Nolloth to Cape Agulhas) +Delesseriaceae vel. aff. (Oudekraal, endemic) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-2.md b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-2.md new file mode 100644 index 000000000..701fc2055 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-2.md @@ -0,0 +1,70 @@ +--- +title: "List of red seaweeds of the Cape Peninsula and False Bay" +chunk: 3/6 +source: "https://en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:48.020280+00:00" +instance: "kb-cron" +--- + +==== Family Rhodomelaceae ==== +Aiolocolax pulchellus M.A.Pocock 1956, (Blaauwberg eastwards) +Bostrychia intricata (Bory de Saint-Vincent) Montagne 1852, syn. Scytonema intricatum Bory de Saint-Vincent 1828, Stictosiphonia intricata (Bory de Saint-Vincent) P.C.Silva 1996, (Saldanha Bay, Kommetjie on Cape Peninsula eastward along whole of south coast) +Kelp fern, Carradoriella virgata (C.Agardh) P.C.Silva, 1996, recorded as syn. Polysiphonia virgata (C.Agardh) Sprengel 1827, syn. Hutchinsia virgata C.Agardh 1824, Carradoria virgata (C.Agardh) Kylin 1956, (Namibia to Brandfontein) +Cape chondria, Chondria capensis (Harvey) Askenasy 1888, syn. Laurencia capensis Harvey 1849, Chondriopsis capensis (Harvey) J.Agardh 1863, (Namibia to just east of Cape Agulhas. Southern African endemic.) +Falkenbergiella capensis Kylin 1938, (St James, Muizenberg and Swartklip in False Bay. Cape south coast. Endemic) +Herposiphonia didymosporangia Stegenga & Kemperman 1987, (St James, Brandfontein and coast of De Hoop nature reserve, Southern African endemic) +Herposiphonia heringii (Harvey) Falkenberg 1901, syn. Polysiphonia heringii Harvey 1847, (Between Hondeklipbaai and St James, endemic) +Herposiphonia secunda (C.Agardh) Ambronn 1880, syn. Hutchinsia secunda C.Agardh 1824, Polysiphonia secunda (C.Agardh) Zanardini 1840, Herposiphonia tenella f. secunda (C.Agardh) Hollenberg 1968, (Muizenberg, Cape Agulhas eastward to the tropics) +Flexuose laurencia, Laurencia flexuosa Kützing 1849, (False Bay to KwaZulu-Natal at least as far north as Mabibi, endemic)) +Grape laurencia, Laurencia glomerata (Kützing) Kützing 1849, syn. Chondria glomerata Kützing 1847, (Port Nolloth?, Melbosstrand?, Cape Peninsula eastward) +Laurencia peninsularis Stegenga, Bolton & R.J.Anderson 1987, (False Bay to East London, endemic) +Ophidocladus simpliciusculus (P.L.Crouan & H.M.Crouan) Falkenberg in Schmitz & Falkenberg 1897, syn. Polysiphonia simpliciuscula P.L.Crouan & H.M.Crouan 1852, (Hondeklipbaai?, Platboombaai on Cape Peninsula to Mozambique) +Pachychaeta cryptoclada Falkenberg 1901, (Swartklip, Brandfontein, more common in Eastern Cape, endemic) +Placophora binderi (J.Agardh) J.Agardh 1863, syn. Amansia binderi J.Agardh 1841, Micramansia binderi (J.Agardh) Kützing 1865, (Kalk Bay on the Cape Peninsula extending along south and east coast to southern Mozambique) +Placophora monocarpa (Montagne) Papenfuss 1956, syn. Polysiphonia monocarpa Montagne 1842, (Melkbosstrand to Strandfontein in False Bay, possibly further east, endemic) +Polysiphonia incompta Harvey 1847, (Namibia, the entire South African coast into Mozambique) +Polysiphonia namibiensis Stegenga & Engeldow in Stegenga, Bolton & Anderson 1997, (Olifantsbos, Cape Agulhas, Eastern Cape. Southern African endemic) +Polysiphonia scopulorum Harvey 1855, syn. Vertebrata scopulorum (Harvey) Kuntze 1891, Lophosiphonia scopulorum (Harvey) Womersley 1950, (Muizenberg and Clovelly in False Bay) +Polysiphonia urbana Harvey 1847, (Port Nolloth to Cape Agulhas. Southern African endemic) +Polysiphonia sp.1 (Muizenberg, endemic) +Red feather-weed, Pterosiphonia cloiophylla (C.Agardh) Falkenberg in Schmitz & Falkenberg 1897, syn. Rytiphlaea cloiophylla (C.Agardh) J.Agardh, Rhodomela cloiophylla C.Agardh 1822, Polysiphonia cloiophylla (C.Agardh) J.Agardh 1863, (Namibia, Cape west coast and Cape south coast) +Pterosiphonia stangeri (J.Agardh) Falkenberg 1901, syn. Polysiphonia stangeri J.Agardh 1863, Vertebrata stangeri (J.Agardh) Kuntze 1891, (Swartklip in False Bay, Cape south coast and KwaZulu-Natal. Southern African endemic) +Streblocladia camptoclada (Montagne) Falkenberg 1901, syn. Polysiphonia camptoclada Montagne 1837, (Yzerfontein to Clovelly in False Bay) +Streblocladia corymbifera (C.Agardh) Kylin 1938, syn. Hutchinsia corymbifera C.Agardh 1828, Polysiphonia corymbifera (C.Agardh) Endlicher 1843, (Saldanha to St. James in False Bay) +Stromatocarpus parasiticus Falkenberg in Schmitz & Falkenberg 1897, (Blaauwberg to Cape Hangklip, endemic) +Tayloriella tenebrosa (Harvey) Kylin 1938, Polysiphonia tenebrosa Harvey 1847, (Doring Bay, Muizenberg and Glencairn in False Bay eastward, Southern African endemic) + +==== Family Spyridiaceae ==== +Spyridia filamentosa (Wulfen) Harvey in Hooker 1833, syn. Fucus filamentosus Wulfen 1803, Hutchinsia filamentosa (Wulfen) C.Agardh 1824, Polysiphonia filamentosa (Wulfen) Sprengel 1827, Ceramium filamentosum (Wulfen) C.Agardh 1828, (Rare in Western Cape. False Bay, Eastern Cape to tropical East Africa) +Spyridia plumosa F.Schmitz ex J.Agardh 1897, (Camps Bay, Kowie area, extending into KwaZulu-Natal as far as Shelly Beach, endemic) + +==== Family Wrangeliaceae ==== +Anotrichium furcellatum (J.Agardh) Baldock 1976, syn. Griffithsia furcellata J.Agardh 1842, Neomonospora furcellata (J.Agardh) Feldmann-Mazoyer & Meslin 1939, Corynospora furcellata (J.Agardh) Levring 1974, (False Bay, Kowie) +Anotrichium tenue (C.Agardh) Nägeli 1862, syn. Griffithsia tenuis C.Agardh 1828, (Doring Bay to Cape Agulhas and further east to KwaZulu-Natal) +Griffithsia confervoides Suhr 1840, (Namibia to KwaZulu-Natal, Southern African endemic) +Gymnothamnion elegans (Schousboe ex C.Agardh) J.Agardh 1892, syn. Callithamnion elegans Schousboe ex C.Agardh 1828, (Bakoven on Cape Peninsula to KwaZulu-Natal) +Gymnothamnion elegans var. bisporum Stegenga 1986, (Hout Bay to East London, endemic) +Hommersandiella humilis (Kützing) Alongi, Cormaci & G.Furnari 2007, syn. Callithamnion humile Kützing 1849, Lomathamnion humile (Kützing) Stegenga 1989, (Namibia to Cape Hangklip, Southern African endemic) +Lomathamnion capense Stegenga 1984, (Cape Point to Arniston, endemic) +Pleonosporium filicinum (Harvey ex J.Agardh) De Toni 1903, syn. Halothamnion filicinum Harvey ex J.Agardh 1876, (Swartklip in False Bay to Natal, Southern African endemic) +Pleonosporium harveyanum (J.Agardh) De Toni 1903, syn. Halothamnion harveyanum J.Agardh 1876, (Namibia to East London, Southern African endemic) +Pleonosporium paternoster Stegenga 1986, (Paternoster and Oudekraal, endemic) +Pleonosporium ramulosum (J.Agardh) De Toni 1903, Corynospora ramulosa J.Agardh 1851, (Port Nolloth to southern Cape Peninsula, endemic) +Ptilothamnion polysporum Gordon-Mills & Wollaston in Wollaston 1984; (Swartklip in False Bay to Mozambique) +Spongoclonium caribaeum (Børgesen) M.J.Wynne 2005, syn. Mesothamnion caribaeum Børgesen 1917, Pleonosporium caribaeum (Børgesen) R.E.Norris 1985, (Clovelly in False Bay to KwaZulu-Natal, Widespread in tropical regions.) +Tiffaniella cymodoceae (Børgesen) E.M.Gordon 1972, syn. Spermothamnion cymodoceae Børgesen 1952, (Platbank on Cape Peninsula to Mozambique) +Tiffaniella schmitziana (E.S.Barton) Bolton & Stegenga 1987, syn. Spermothamnion schmitzianum E.S.Barton 1893, (Kraalbaai, Strandfontein, Port Elizabeth to Hluleka, endemic) +Wrangelia purpurifera J.Agardh 1863, (Paternoster to Kowie River, endemic) + +=== Order Colaconematales === + +==== Family Colaconemataceae ==== +Colaconema caespitosum (J.Agardh) Jackelman, Stegenga & J.J.Bolton 1991, (Kommetjie eastward entire south coast and Eastern Cape) +Colaconema daviesii (Dillwyn) Stegenga 1985, (Hondeklipbaai to Transkei) +Colaconema interpositum (Heydrich) H.Stegenga, J.J.Bolton & R.J.Anderson 1997, (Platbank, Cape Peninsula) +Colaconema nemalionis (De Notaris ex L.Dufour) Stegenga 1985, (Hondeklip Bay to East London) +Colaconema panduripodium H.Stegenga, J.J.Bolton & R.J.Anderson 1997, (Hondeklip Bay and Oudekraal, endemic) + +=== Order Corallinales === \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-3.md b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-3.md new file mode 100644 index 000000000..60d8ed69e --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-3.md @@ -0,0 +1,58 @@ +--- +title: "List of red seaweeds of the Cape Peninsula and False Bay" +chunk: 4/6 +source: "https://en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:48.020280+00:00" +instance: "kb-cron" +--- + +==== Family Corallinaceae ==== +Amphiroa capensis Areschoug 1852, (Llandudno on Cape Peninsula to Kowie River, endemic) +Amphiroa epheddraea horsetail coralline, +Arthrocardia corymbosa (Lamarck) Decaisne 1842, syn. Corallina corymbosa Lamarck 1815, Amphiroa corymbosa (Lamarck) Decaisne 1842, Cheilosporum corymbosum (Lamarck) Decaisne 1842, (Southern Cape Peninsula eastward) +Arthrocardia flabellata (Kützing) Manza 1940, syn. Corallina flabellata Kützing 1858, (Probably along most of the southern African coast) (Probably along the entire South African coast extending into Mozambique) +Arthrocardia filicula (Lamarck) Johansen 1984, syn. Corallina filicula Lamarck 1815, Cheilosporum palmatum var. filicula (Lamarck) Yendo 1902, (Namibia and west coast) +Feather coralline, Corallina officinalis Linnaeus 1758, (Oudekraal to Kowie river) (Oudekraal eastward to Mission Rocks) +Hydrolithon samoënse (Foslie) Keats & Y.M.Chamberlain 1994, syn. Lithophyllum samoënse Foslie 1906, Pseudolithophyllum samoënse (Foslie) Adey 1970, (Yzerfontein, Western Cape to Sodwana Bay, KwaZulu-Natal.) +Finely forked coralline, Jania adhaerens J.V.Lamouroux, 1816 (TMNPMPA) +Jania crassa J.V.Lamouroux 1821, (St. James in False Bay, Eastern Cape and KwaZulu-Natal) +Arrowhead coralline, Jania cultrata (Harvey) J.H.Kim, Guiry & H.-G.Choi 2007, syn. Amphiroa cultrata Harvey 1849, Cheilosporum cultratum (Harvey) Areschoug 1852, (as Cheilosporum cultratum, Platboombaai on Cape Peninsula to Mozambique) +Jania sagittata (J.V.Lamouroux) Blainville 1834, syn. Corallina sagittata J.V.Lamouroux 1824, Amphiroa sagittata (J.V.Lamouroux) Decaisne 1842, Arthrocardia sagittata (J.V.Lamouroux) Decaisne 1842, Cheilosporum sagittatum (J.V.Lamouroux) Areschoug 1852, (as Cheilosporum sagittatum, Melkbosstrand to northern Mabibi in KwaZulu-Natal.) +Jania verrucosa J.V.Lamouroux 1816, syn. Corallina verrucosa (Lamouroux) Kützing 1858, (False Bay eastward) +Lithophyllum corallinae (P.L.Crouan & H.M.Crouan) Heydrich 1897, syn. Melobesia corallinae P.L.Crouan & H.M.Crouan 1867, Dermatolithon corallinae (P.L.Crouan & H.M.Crouan) Foslie 1902, Lithophyllum pustulatum var. corallinae (P.L.Crouan & H.M.Crouan) Foslie 1905, Lithophyllum macrocarpum f. corallinae (P.L.Crouan & H.M.Crouan) Foslie 1909, Tenarea corallinae (P.L.Crouan & H.M.Crouan) Notoya 1974, Titanoderma corallinae (P.L.Crouan & H.M.Crouan) Woelkerling, Y.M.Chamberlain & P.C.Silva 1985, (Kommetjie (Western Cape) to KwaZulu-Natal) +Lithophyllum neoatalayense Masaki 1968, (as Titanoderma neoatalayense, Groenriviermond (Northern Cape) to Cape Agulhas (Western Cape)) +Lithophyllum polycephalum Foslie, syn. Titanoderma polycephalum (Foslie) Woelkerling, Y.M.Chamberlain & P.C.Silva 1985, (as Titanoderma polycephalum, False Bay to Cape Agulhas (Western Cape)) +Lithophyllum pustulatum (J.V.Lamouroux) Foslie 1904, syn. Melobesia pustulata J.V.Lamouroux 1816, Titanoderma pustulatum (J.V.Lamouroux) Nägeli 1858, Dermatolithon pustulatum (J.V.Lamouroux) Foslie 1898, Epilithon pustulatum (J.V.Lamouroux) M.Lemoine 1921, Tenarea pustulata (J.V.Lamouroux) Shameel 1983, (as Titanoderma pustulatum, Occasional throughout the west coast and increasing in abundance toward KwaZulu-Natal where it is particularly abundant.) +Pneophyllum coronatum (Rosanoff) Penrose in Chamberlain 1994, syn. Melobesia coronata Rosanoff 1866, (Oudekraal, western Cape Peninsula, Western Cape.) +Pneophyllum fragile Kützing 1843, (Widespread along the west coast.) +Pneophyllum keatsii Y.M.Chamberlain 1994, (Oudekraal, western Cape Peninsula, Western Cape, to Cape Agulhas, Western Cape.) +Spongites discoidea (Foslie) D.Penrose & Woelkerling 1988, syn. Lithophyllum discoideum Foslie 1900, Hydrolithon discoideum (Foslie) M.L.Mendoza & J.Cabioch 1985, (Port Nolloth, Northern Cape, to Cape Agulhas, Western Cape.) +Scrolled coralline crust, Spongites impar (Foslie) Y.M.Chamberlain 1994, syn. Lithophyllum impar Foslie 1909, (Cape St. Martin just south of St. Helena Bay, Western Cape, to Oudekraal, western Cape Peninsula, Western Cape.) +Cochlear coralline crust, Spongites yendoi (Foslie) Y.M.Chamberlain 1993, syn. Lithophyllum yendoi (Foslie) Foslie 1900, Goniolithon yendoi Foslie 1900, Lithothamnion yendoi (Foslie) Lemoine 1965, Pseudolithophyllum yendoi (Foslie) Adey 1970, (Throughout South Africa (Namibia to the Mozambican border). Most abundant along the southern west and south coasts, becoming less common toward the east.) + +=== Order Gelidiales === + +==== Family Gelidiaceae ==== +Gelidium abbottiorum R.E.Norris, 1990 (TMNPMPA) +Gelidium applanatum Stegenga, Bolton & R.J.Anderson 1997, (Vulcan Rock off Hout Bay and Muizenberg) +Cape jelly-weed, Gelidium capense (S.G.Gmelin) P.C.Silva in P.C.Silva, E.G.Meñez, & Moe 1987, (Melkbosstrand to Kenton on Sea Eastern Cape. Endemic?) +Gelidium micropterum Kützing 1868, (Cape Peninsula to Knysna) +Saw-edged jelly-weed, Gelidium pristoides (Turner) Kützing 1843, (Sea Point and False Bay eastwards) +Fern-leafed jelly-weed, Gelidium pteridifolium R.E.Norris, Hommersand & Fredericq 1987, (Glencairn, Cape Hangklip, Eastern Cape and southern KwaZulu-Natal up to Tinley Manor just north of Durban) +Turf jelly-weed, Gelidium reptans (Suhr) Kylin 1938, syn. Phyllophora reptans Suhr 1841, (Cape Peninsula and False Bay to KwaZulu-Natal and Mozambique) +Red ribbons, Gelidium vittatum (Linnaeus) Kützing 1843, syn. Fucus vittatus Linnaeus 1767, Suhria vittata (Linnaeus) Endlicher 1843, Chaetangium vittatum (Linnaeus) P.G.Parkinson 1981, (Möwe Bay, Nabibia to Brandfontein, drift specimens to Port Elizabeth) + +=== Order Gigartinales === + +==== Family Caulacanthaceae ==== +Spiky turf-weed, Caulacanthus ustulatus (Mertens ex Turner) Kützing 1843, syn. Fucus acicularis var. ustulatus Mertens ex Turner 1808, Sphaerococcus ustulatus (Mertens ex Turner) C.Agardh 1828, Gigartina ustulata (Mertens ex Turner) Greville 1830, Hypnea ustulata (Mertens ex Turner) Montagne 1840, Gelidium ustulatum (Mertens ex Turner) J.Agardh 1842, Olivia ustulata (Mertens ex Turner) Montagne 1846, (Whole South African coast) +Heringia mirabilis (C.Agardh) J.Agardh 1846, syn. Sphaerococcus mirabilis C.Agardh 1820, (Namibia to East london, Southern African endemic) + +==== Family Cystocloniaceae ==== +Straight-tipped hypnea, Hypnea ecklonii Suhr 1836, (Pearly Beach to Namibia, Southern African endemic) +Hypnea rosea Papenfuss 1947, (Strand in False Bay and Die Walle, just west of Cape Agulhas, and south and east coasts, endemic) +Green tips, Hypnea spicifera (Suhr) Harvey in J. Agardh 1847, syn. Gracilaria spicifera Suhr 1834, Hypnophycus spicifera (Suhr) Kützing 1843, (virtually the entire South African coast, Southern African endemic) +Fine hypnea, Hypnea tenuis Kylin 1938, (Mainly south and east coast, as far west as Swartklip in False Bay) +Roseleaf, Rhodophyllis reptans (Suhr) Papenfuss 1956, syn. Halymenia reptans Suhr 1834, Euhymenia reptans (Suhr) Kützing 1849, Kallymenia reptans (Suhr) E.S.Barton 1893, (Hondeklipbaai to KwaZulu-Natal, Southern African endemic) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-4.md b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-4.md new file mode 100644 index 000000000..9a7a5f42e --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-4.md @@ -0,0 +1,73 @@ +--- +title: "List of red seaweeds of the Cape Peninsula and False Bay" +chunk: 5/6 +source: "https://en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:48.020280+00:00" +instance: "kb-cron" +--- + +==== Family Gigartinaceae ==== +Red tongue-weed, Gigartina bracteata (S.G.Gmelin) Setchell & N.L.Gardner 1933, syn. Fucus bracteatus S.G.Gmelin 1768, (Namibia to Cape of Good Hope, drift material from Muizenberg, Southern African endemic) +Gigartina insignis (Endlicher & Diesing) F.Schmitz in E.S.Barton 1896, syn. Iridaea insignis Endlicher & Diesing 1845, (Muizenberg, Cape Hangklip to Kowie River, Southern African endemic) +Gigartina pistillata (S.G.Gmelin) Stackhouse 1809, syn. Fucus pistillatus S.G.Gmelin 1768, (Smitswinkel Bay and Swartklip east to the Kowie area) +Tongue-weed, Gigartina polycarpa (Kützing) Setchell & N.L.Gardner, 1933 (TMNPMPA) +Gigartina tysonii Reinbold in Tyson 1912, (Three Anchor Bay to Camps Bay, drift specimens from Platboombaai and Olifantsbos, endemic) +Gigartina scabiosa (Kützing) Papenfuss (date not specified) (TMNPMPA) +Iridaea convoluta (Areschoug ex J Agardh) Hewitt 1960, syn. Gigartina convoluta Areschoug ex J.Agardh 1899, (Table Bay to Cape of Good Hope, endemic) +Spotted mazzaella, Mazzaella capensis (J.Agardh) Fredericq in Hommersand et al. 1993, Iridaea capensis J.Agardh 1848, Iridophycus capensis (J.Agardh) Setchell & N.L.Gardner 1936, Gigartina capensis (J.Agardh) D.H.Kim 1976, (Port Nolloth to Cape Agulhas, extending into Namibia, Southern African endemic) +Convoluted mazzaella Mazzaella convoluta (Areschoug ex J.Agardh) Hommersand, 1994, (TMNPMPA) +Rhodoglossum alcicorne Stegenga, Bolton & R.J.Anderson 1997, (Hout Bay, endemic) +Sarcothalia radula (Esper) Edyvane & Womersley 1994, syn. Fucus radula Esper 1802, Sphaerococcus radula (Esper) C.Agardh 1822, Iridaea radula (Esper) Bory de Saint-Vincent 1828, Gigartina radula (Esper) J.Agardh 1851, (Port Nolloth to Cape Agulhas, rare at De Hoop, extending into Namibia) +Forked gigartina, Sarcothalia scutellata (Hering) Leister 1993, syn. Sphaerococcus scutellatus Hering 1841, Dicurella scutellata (Hering) Papenfuss 1940, Gigartina scutellata (Hering) Simons 1983, (Namibia to Cape Hangklip) +Twisted togue-weed, Sarcothalia stiriata (Turner) Leister in Hommersand, Guiry, Fredericq & Leister 1993, syn. Fucus stiriata Turner 1807, Sphaerococcus stiriatus (Turner) C.Agardh 1817, Sphaerococcus radula var. stiriatus (Turner) Rudolphi 1831, Mastocarpus stiriatus (Turner) Kützing 1843, Gigartina stiriata (Turner) J.Agardh 1851, (Namibia and Port Nolloth to Cape Agulhas) as Gigartina stiriata in TMNPMPA. + +==== Family Kallymeniaceae ==== +Kallymenia agardhii R.E.Norris 1964, (Namibia to Cape Agulhas, Southern African endemic) +Kallymenia schizophylla J.Agardh 1848, (Namibia to southern Cape Peninsula and Cape Hangklip. Southern African endemic) +Pugetia harveyana (J.Agardh) R.E.Norris 1964, syn. Kallymenia harveyana J.Agardh 1844, (Namibia to southern Cape Peninsula, Drift material from Muizenberg) +Split disc-weed, Thamnophyllis discigera (J.Agardh) R.E.Norris 1964, syn. Rhodymenia discigera J.Agardh 1841, Callophyllis discigera (J.Agardh) J.Agardh 1847, (Port Nolloth to Cape Agulhas) +Thamnophyllis pocockiae R.E.Norris 1964, (St Helena bay to East London) + +==== Family Phyllophoraceae ==== +Ahnfeltiopsis complicata (Kützing) P.C.Silva & DeCew 1992, complicated gymnogongrus, syn. Chondrus complicatus Kützing 1849, Gymnogongrus complicatus (Kützing) Papenfuss 1943, (Namibia to False Bay, Southern African endemic) +Ahnfeltiopsis glomerata (J.Agardh) P.C.Silva & DeCew 1992, clustered gymnogongrus, syn. Gymnogongrus glomeratus J.Agardh 1849, (Namibia to Cape Agulhas, Southern African endemic) +Ahnfeltiopsis intermedia (Kylin) Stegenga, Bolton & R.J.Anderson 1997, gymnogongrus, syn. Gymnogongrus intermedius Kylin 1938, (Kalk Bay, Sea Point and possibly Keurboomstrand in Plettenberg Bay) +Ahnfeltiopsis polyclada (Kützing) P.C.Silva & DeCew 1992, fine gymnogongrus, syn. Chondrus polycladus Kützing 1849, Gymnogongrus polycladus (Kützing) J.Agardh 1851, (False Bay to Brandfontein, possibly Melkbosstrand and Postberg) +Ahnfeltiopsis vermicularis (C.Agardh) P.C.Silva & DeCew 1992, fine gymnogongrus,syn. Sphaerococcus vermicularis C.Agardh 1817, Gymnogongrus vermicularis (C.Agardh) J.Agardh 1851, (Hondeklipbaai to False Bay, South African endemic) +Dilated gymnogongrus, Gymnogongrus dilatatus (Turner) J.Agardh 1851, syn. Fucus dilatatus Turner 1811, Sphaerococcus dilatatus (Turner) C.Agardh 1817, Pachycarpus dilatatus (Turner) Kützing 1843, (Namibia to southern Cape Peninsula, drift material from Muizenberg) + +==== Family Rhizophyllidaceae ==== +Portieria hornemannii (Lyngbye) P.C.Silva in P.C. Silva, Meñez & Moe 1987, syn. Desmia hornemannii Lyngbye 1819, Chondrococcus hornemannii (Lyngbye) F.Schmitz 1895, (Table Bay, False Bay, south and east coast, extending into Mozambique) + +=== Order Gracilariales === + +==== Family Gracilariaceae ==== +Agar-weed, Gracilaria gracilis (Stackhouse) Steentoft, L.M.Irvine & Farnham, 1995 (TMNPMPA) +Gracilaria verrucosa (Hudson) Papenfuss 1950, syn. Fucus verrucosus Hudson 1762, (recorded from: St Helena Bay, Velddrif, Saldanha Bay, Langebaan Lagoon, Table Bay, False bay, Swartkops River) +Gracilariopsis lemaneiformis(Bory de Saint-Vincent) E.Y.Dawson, Acleto & Foldvik 1964, syn. Gigartina lemaneiformis Bory de Saint-Vincent 1828, Gracilaria lemaneiformis (Bory de Saint-Vincent) Greville 1830, Cordylecladia lemanaeformis (Bory de Saint-Vincent) M.A.Howe 1914, (Simon's Town in False Bay) + +==== Family Pterocladiophilaceae ==== +Gelidiocolax suhriae (M.T.Martin & M.A.Pocock) K.-C.Fan & Papenfuss 1959, syn. Choreocolax suhriae M.T.Martin & M.A.Pocock 1953, (Blaauwberg to Strandfontein, endemic) + +=== Order Halymeniales === + +==== Family Grateloupiaceae ==== +Grateloupia doryphora (Montagne) M.A.Howe 1914, syn. Halymenia doryphora Montagne 1839, (Port Nolloth to Cape Agulhas) +Grateloupia filicina (J.V.Lamouroux) C.Agardh 1822, syn. Delesseria filicina J.V.Lamouroux 1813, (Whole west coast and south coast to Eastern Cape as far as the Kowie area) +Grateloupia longifolia Kylin, 1938, (TMNPMPA), + +==== Family Halymeniaceae ==== +Red rubber-weed, Pachymenia carnosa (J.Agardh) J.Agardh 1876, syn. Platymenia carnosa J.Agardh 1848. Iridaea carnosa (J.Agardh) Kützing 1849, Schizymenia carnosa (J.Agardh) J.Agardh 1851, (Whole west coast into Namibia, eastward to Brandtfontein) +Pachymenia cornea (Kützing) Chiang 1970, syn. Iridaea cornea Kützing 1867, Cyrtymenia cornea (Kützing) F.Schmitz 1897, Phyllymenia cornea (Kützing) Setchell & Gardner 1936, (Doring Bay to East London) +Pachymenia orbitosa (Suhr) L.K.Russell in L.K. Russell et al. 2009, slippery orbits, syn. Iridaea orbitosa Suhr 1840, Aeodes orbitosa (Suhr) F.Schmitz 1894, (Whole Cape west coast, extending into Namibia, and eastward at least as far as Cape Agulhas, endemic) +Corrugated red algae, Phyllymenia belangeri (Bory de Saint-Vincent) Setchell & N.L.Gardner, 1936 recorded as syn. Grateloupia belangeri (Bory de Saint-Vincent) De Clerck, Gavio, Fredericq, Cocquyt & Coppejans, 2005, syn. Iridaea belangeri Bory de Saint-Vincent 1834, (Whole west coast extending into Namibia. Southernmost record from Platboombaai, endemic) (TMNPMPA) +Tattered rag-weed, Phyllymenia capensis (O.De Clerck) Gargiulo, M.Morabito & Manghisi, 2013, (TMNPMPA) recorded as syn. Grateloupia capensis O.De Clerck, 2005. +Constricted polyopes, Polyopes constrictus (Turner) J.Agardh 1851, syn. Fucus constrictus Turner 1809, Sphaerococcus constrictus (Turner) C.Agardh 1822, Gelidium constrictum (Turner) Kützing 1849, (Doring Bay to Kei River mouth) + +==== Family Tsengiaceae ==== +Lance-weed, Tsengia lanceolata (J.Agardh) Saunders & Kraft 2002, syn. Nemastoma lanceolatum J.Agardh 1847, (Hondeklipbaai to Cape Hangklip) +Tsengia pulchra (Baardseth) Masuda & Guiry 1994, syn. Nemastoma pulchrum Baardseth 1941, (found only once at the Cape of Good Hope) + +=== Order Hapalidiales === \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-5.md b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-5.md new file mode 100644 index 000000000..fc0ce3dd6 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay-5.md @@ -0,0 +1,118 @@ +--- +title: "List of red seaweeds of the Cape Peninsula and False Bay" +chunk: 6/6 +source: "https://en.wikipedia.org/wiki/List_of_red_seaweeds_of_the_Cape_Peninsula_and_False_Bay" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:48.020280+00:00" +instance: "kb-cron" +--- + +==== Family Hapalidiaceae ==== +Thin coralline crust, Phymatolithon foveatum (Y.M.Chamberlain & Keats) Maneveldt & E.Van der Merwe 2014, (TMNPMPA), syn. Leptophytum foveatum Y.M.Chamberlain & D.W.Keats, 1994. + +=== Order Hildenbrandiales === + +==== Family Hildenbrandiaceae ==== +Tar crust, Hildenbrandia lecannellieri Hariot 1887, (Entire west coast and east coast as far as Port Elizabeth) +Hildenbrandia rubra (Sommerfelt) Meneghini 1841, (Probably the whole of the west coast) + +=== Order Nemaliales === + +==== Family Liagoraceae ==== +Helminthocladia papenfussii Kylin 1938, (Oudekraal eastward at least as far as Cape Morgan) +Helminthora furcellata (Reinbold ex Tyson) M.T.Martin 1947, (Endemic, Three Anchor Bay to Cape Hangklip) + +==== Family Scinaiaceae ==== +Hedgehog seaweed, Nothogenia erinacea (Turner) P.G.Parkinson 1983, (Cape Fria, Namibia to East London) +Balloon weed, Nothogenia ovalis (Suhr) P.G.Parkinson 1983, syn. Dumontia ovalis Suhr 1840, (Endemic, Möwe Bay, Namibia to Cape Agulhas) +Scinaia capensis (Setchell) Huisman 1985, syn. Gloiophloea capensis Setchell 1914, (Endemic, Melkbosstrand to Kowie area of Eastern Cape) +Ramrod weed, Scinaia salicornioides (Kützing) J.Agardh 1851, syn. Ginnania salicornioides Kützing, (Endemic, Muizenberg to east coast) + +=== Order Nemastomatales === + +==== Family Schizymeniaceae ==== +Schizymenia apoda (J.Agardh) J.Agardh 1851, syn. Platymenia apoda J.Agardh 1848, Platymenia undulata var. obovata J.Agardh 1848, Schizymenia obovata (J.Agardh) J.Agardh 1851, (Port Nolloth to Cape Agulhas) + +=== Order Palmariales === + +==== Family Meiodiscaceae ==== +Meiodiscus concrescens (K.M.Drew) P.W.Gabrielson in Gabrielsen et al. 2000, syn. Audouinella concrescens (K.M.Drew) P.S.Dixon 1976, Rhodochorton concrescens, K.M. Drew 1928, (Hout Bay) + +==== Family Rhodophysemataceae ==== +Rhodophysema feldmannii Cabioch 1975, (Hout Bay to Platbank on Cape Peninsula) + +==== Family Rhodothamniellaceae ==== +Rhodothamniella floridula (Dillwyn) Feldmann in T.Christensen 1978, (Lambert's Bay to Hluleka, Transkei) + +=== Order Peyssonneliales === + +==== Family Peyssonneliaceae ==== +Peyssonnelia atropurpurea P.L.Crouan & H.M.Crouan 1867, (Yzerfontein to Brandfontein) +Red Fan-weed, Sonderophycus capensis (Montagne) M.J.Wynne 2011, Peyssonnelia capensis Montagne 1847, Pterigospermum capense (Montagne) Kuntze 1891, Sonderopelta capensis (Montagne) A.D.Krayesky 2009, (as Peyssonnelia capensis, Hout Bay on Cape Peninsula eastwards extending into Mozambique) + +=== Order Plocamiales === + +==== Family Plocamiaceae ==== +Plocamiocolax papenfussianus M.F.Martin & M.A.Pocock 1953, (Melkbosstrand to East London, endemic) (Arniston north to Rabbit Rock in KwaZulu-Natal) +Plocamium beckeri F.Schmitz ex Simons 1964, (Collected at Muizenberg, Eastern Cape and KwaZulu-Natal) +Coral plocamium Plocamium corallorhiza (Turner) J.D.Hooker & Harvey 1845, syn. Fucus corallorhiza Turner 1808, Thamnophora corallorhiza (Turner) C.Agardh 1822, (Yzerfontein to KwaZulu-Natal extending into southern Mozambique) +Horny plocamium, Plocamium cornutum (Turner) Harvey 1849, syn. Fucus cornutus Turner 1819, Thamnophora cornuta (Turner) Greville 1830, Thamnocarpus cornutus (Turner) Kützing 1843, (entire coastline of the Western Cape to Namibia, rarer in the Eastern Cape, Southern African endemic) +Plocamium glomeratum J.Agardh 1851, (Namibia to Still Bay, Southern African endemic) +Plocamium maxillosum (Poiret) J.V.Lamouroux 1813, syn. Fucus maxillosus Poiret 1808, (Hondeklipbaai to Cape Agulhas, endemic) +Rigid plocamium, Plocamium rigidum Bory de Saint-Vincent in Bélanger & Bory de Saint-Vincent 1834, syn. Nereidea rigida (Bory de Saint-Vincent) Kuntze 1891, (Namibia to Eastern Cape, Southern African endemic) +Plocamium sp. indet. (False Bay coast, endemic?) + +==== Family Sarcodiaceae ==== +Comb-fan weed, Trematocarpus flabellatus (J.Agardh) De Toni 1900, syn. Phyllotylus flabellatus J.Agardh 1847, Dicurella flabellata (J.Agardh) J.Agardh 1852, (Lüderitz to Port Elizabeth, Southern African endemic) +Trematocarpus fragilis (C.Agardh) De Toni 1900, syn. Sphaerococcus fragilis C.Agardh 1822, Chondrus fragilis (C.Agardh) Greville 1830, Dicurella fragilis (C.Agardh) J.Agardh 1852, (Port Nolloth to Brandfontein, Southern African endemic) + +=== Order Rhodymeniales === + +==== Family Champiaceae ==== +Compressed champia. Champia compressa Harvey 1838, (False Bay eastward to northern KwaZulu-Natal and extending into Mozambique. Rarer on west side of Cape Peninsula and also found at Kraalbaai and Paternoster) +Earthworm champia, Champia lumbricalis (Linnaeus) Desvaux, 1809. + +==== Family Lomentariaceae ==== +Lomentaria diffusa Stegenga, Bolton & R.J.Anderson 1997, (Saldanha Bay and Kraalbaai to Brandfontein, endemic) + +==== Family Rhodymeniaceae ==== +Botryocladia paucivesicaria Stegenga, Bolton & R.J.Anderson 1997, (Known from drift specimens collected on the west side of Cape peninsula at Noordhoek Beach and Olifantsbos, endemic) +Cape wine-weed, Rhodymenia capensis J.Agardh 1894, syn. Epymenia capensis (J.Agardh) Papenfuss 1940, +Rhodymenia holmesii Ardissone 1893, (drift material from Olifantsbos) (Southern half of the Cape Peninsula, endemic) +Stalked roseweed, Rhodymenia natalensis Kylin 1938, (From Namibia along the whole of the South African coast extending into southern Mozambique) +Broad wine weed, Rhodymenia obtusa (Greville) Womersley 1996, syn. Phyllophora obtusa Greville 1831, Epymenia obtusa (Greville) Kützing 1849, (Muizenberg and the southern Cape Peninsula to Namibia) +Palmate roseweed, Rhodymenia pseudopalmata (J.V.Lamouroux) P.C.Silva 1952, syn. Fucus pseudopalmatus J.V.Lamouroux 1805, Delesseria pseudopalmata (J.V.Lamouroux) J.V.Lamouroux 1813, (From drift at Strandfontein) + +=== Order Sporolithales === + +==== Family Sporolithaceae ==== +Velvety coralline crust, Heydrichia woelkerlingii R.A.Townsend, Y.M.Chamberlain & Keats, 1994 (TMNPMPA) + +== Class Rhodophyta incertae sedis == + +=== Order Rhodophycophyta incertae sedis === + +==== Family Rhodophycophyta incertae sedis ==== +Callophycus densus (Sonder) Kraft 1984, syn. Thysanocladia densa Sonder 1871, (Olifantsbos to southern KwaZulu-Natal) + +== Class: Stylonematophyceae == + +=== Order: Stylonematales === + +==== Family Stylonemataceae ==== +Stylonema alsidii (Zanardini, 1840) K.M.Drew 1956, (Saldanha Bay southward, and south coast of Western Cape, Eastern Cape to Kwa-Zulu Natal) +Neevea cf repens Batters 1900, (Hout Bay) + +== Geographical position of places mentioned in species ranges == + +== See also == +Helderberg Marine Protected Area – Marine conservation area in the Western Cape in South Africa +List of marine animals of the Cape Peninsula and False Bay +List of red seaweeds of South Africa +Geology of Cape Town +Table Mountain National Park – Nature conservation area on the Cape Peninsula in Cape Town, South Africa +Table Mountain National Park Marine Protected Area – Marine conservation area around the Cape Peninsula in South Africa +False Bay – Bay of the Atlantic Ocean at South Africa + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_research_methods_in_biology-0.md b/data/en.wikipedia.org/wiki/List_of_research_methods_in_biology-0.md new file mode 100644 index 000000000..46dc7fefe --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_research_methods_in_biology-0.md @@ -0,0 +1,44 @@ +--- +title: "List of research methods in biology" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_research_methods_in_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:54:58.182285+00:00" +instance: "kb-cron" +--- + +This list of research methods in biology is an index to articles about research methodologies used in various branches of biology. + + +== Research design and analysis == + + +=== Research designs === + + +=== Charts and diagrams === + + +=== Statistical analyses === + + +== Laboratory techniques == + + +== Field techniques == + + +== Computational tools == + + +=== Mathematical models === + + +=== Algorithms === + + +== References == + + +== External links == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_scattering_experiments-0.md b/data/en.wikipedia.org/wiki/List_of_scattering_experiments-0.md new file mode 100644 index 000000000..beb80bf8b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_scattering_experiments-0.md @@ -0,0 +1,50 @@ +--- +title: "List of scattering experiments" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_scattering_experiments" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:43.874208+00:00" +instance: "kb-cron" +--- + +This is a list of scattering experiments. + + +== Specific experiments of historical significance == + +Davisson–Germer experiment +Gold foil experiments, performed by Geiger and Marsden for Rutherford which discovered the atomic nucleus +Elucidation of the structure of DNA by X-ray crystallography +Discovery of the antiproton at the Bevatron +Discovery of W and Z bosons at CERN +Discovery of the Higgs boson at the Large Hadron Collider +MINERνA + + +== Types of experiment == + + +=== Optical methods === +Compton scattering +Raman scattering +X-ray crystallography +Biological small-angle scattering with X-rays, or Small-angle X-ray scattering +Static light scattering +Dynamic light scattering +Polymer scattering with X-rays + + +=== Neutron-based methods === +Neutron scattering +Biological small-angle scattering with neutrons, or Small-angle neutron scattering +Polymer scattering with neutrons + + +=== Particle accelerators === +Electrostatic nuclear accelerator +Linear induction accelerator +Betatron +Linear particle accelerator +Cyclotron +Synchrotron \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_selective_estrogen_receptor_modulators-0.md b/data/en.wikipedia.org/wiki/List_of_selective_estrogen_receptor_modulators-0.md new file mode 100644 index 000000000..35611e4e1 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_selective_estrogen_receptor_modulators-0.md @@ -0,0 +1,31 @@ +--- +title: "List of selective estrogen receptor modulators" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_selective_estrogen_receptor_modulators" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:49.247802+00:00" +instance: "kb-cron" +--- + +This is a list of selective estrogen receptor modulators (SERMs). + + +== Approved == +SERMs that have been approved for medical use include anordrin (+mifepristone (Zi Yun)), bazedoxifene (+conjugated estrogens (Duavee)), broparestrol (Acnestrol), clomifene (Clomid), cyclofenil (Sexovid), lasofoxifene (Fablyn), ormeloxifene (Centron, Novex, Novex-DS, Sevista), ospemifene (Osphena; deaminohydroxytoremifene), raloxifene (Evista), tamoxifen (Nolvadex), and toremifene (Fareston; 4-chlorotamoxifen). + + +== Clinical trials == +SERMs that are currently under development and in clinical trials include acolbifene, afimoxifene (4-hydroxytamoxifen; metabolite of tamoxifen), elacestrant, enclomifene ((E)-clomifene), endoxifen (4-hydroxy-N-desmethyltamoxifen; metabolite of tamoxifen), and zuclomifene ((Z)-clomifene). + + +== Non-approved == +SERMs that have not been approved for medical use include arzoxifene, brilanestrant, clomifenoxide (clomiphene N-oxide; metabolite of clomifene), droloxifene (3-hydroxytamoxifen), etacstil, fispemifene, GW-7604 (4-hydroxyetacstil; metabolite of etacstil), idoxifene (pyrrolidino-4-iodotamoxifen), levormeloxifene ((L)-ormeloxifene), miproxifene, nafoxidine, nitromifene (CI-628), NNC 45-0095, panomifene, pipendoxifene (ERA-923), trioxifene, and zindoxifene (D-16726). +Sivifene (A-007) was initially thought to be a SERM due to its structural similarity to tamoxifen but it was subsequently found not to bind to the estrogen receptor (ER). Tesmilifene (DPPE; YMB-1002, BMS-217380-01) is also structurally related to tamoxifen but similarly does not bind to the ER and is not a SERM. + + +== Structure == +SERMs can be variously classified structurally as triphenylethylenes (tamoxifen, clomifene, toremifene, droloxifene, idoxifene, ospemifene, fispemifene, afimoxifene, others), benzothiophenes (raloxifene, arzoxifene), indoles (bazedoxifene, zindoxifene, pipendoxifene), tetrahydronaphthalenes (lasofoxifene, nafoxidine), and benzopyrans (acolbifene, ormeloxifene, levormeloxifene). + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-0.md new file mode 100644 index 000000000..1893a321c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-0.md @@ -0,0 +1,165 @@ +--- +title: "List of sequenced animal genomes" +chunk: 1/6 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_animal_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:50.483884+00:00" +instance: "kb-cron" +--- + +This list of sequenced animal genomes contains animal species for which complete genome sequences have been assembled, annotated and published. Substantially complete draft genomes are included, but not partial genome sequences or organelle-only sequences. For all kingdoms, see the list of sequenced genomes. +For the far more abundant mitochondrial genomes, see list of sequenced animal mitochondrial genomes. + +== Porifera (Sponges) == + +Amphimedon queenslandica, a sponge (2009) +Stylissa carteri (2016) +Ephydatia muelleri (2020) +Xestospongia testudinaria (2016) + +== Ctenophora == + +Mnemiopsis leidyi (Ctenophora), (order Lobata) (2012/2013) +Hormiphora californensis (Ctenophora) (2021) +Pleurobrachia bachei (Ctenophora) (2014) +Bolinopsis microptera(Ctenophora) (2022) + +== Placozoa == + +== Cnidaria == + +Hydra vulgaris, (previously Hydra magnipapillata), a model hydrozoan (2010) +Nematostella vectensis, a model sea anemone (starlet sea anemone) (2007) +Aiptasia pallida, a sea anemone (2015) +Renilla muelleri, an octocoral (2017, 2019) +Stylophora pistillata, a coral (2017) +Aurelia aurita, moon jellyfish (2019) +Clytia hemisphaerica, Hydrozoan jellyfish (2019) +Myxobolus honghuensis (2022) +Nemopilema nomurai, Nomura jellyfish (2019) +Rhopilema esculentum, Flame jellyfish (2020) +Cassiopea xamachana (Scyphozoa) (2019) +Alatina alata (Cubozoa) (2019) +Calvadosia cruxmelitensis (Staurozoa) (2019) +Dendronephthya gigantea, an octocoral (2019) +Acropora acuminata (2020) +Acropora awi (2020) +Acropora cytherea, Table coral (2020) +Acropora digitifera, a coral (2011) +Acropora echinata (2020) +Acropora florida, branching staghorn coral(2020) +Acropora gemmifera (2021) +Acropora hyacinthus, Brush coral (2020) +Acropora intermedia, Noble Staghorn Coral (2020) +Acropora microphthalma (2020) +Acropora muricata, Staghorn coral (2020) +Acropora nasta, branching staghorn coral (2020) +Acropora pulchra (2025) +Acropora selago, Green Selago Acropora (2020) +Acropora tenuis, Purple Tipped Acropora (2020) +Acropora yongei ,Yonge's staghorn coral (2020) +Corallium rubrum, Precious coral (2024) +Astreopora myriophthalma, Porous star coral (2020) +Lophelia pertusa, Deepwater White Coral (2023) +Montipora cactus (2020) +Montipora capitata, Rice coral (2022) +Montipora efflorescens, Velvet coral (2020) +Orbicella faveolata, mountainous star coral (2016) +Paragorgia papillata, Bubble-gum coral (2025) +Pocillopora acuta, Hosoeda Hanayasai coral (2022) +Pocillopora damicornis, cauliflower coral (2018) +Pocillopora meandrina, Cauliflower coral (2022) +Porites astreoides, Mustard hill coral (2022) +Porites compressa, Finger coral (2022) + +== Hemichordata == + +=== Order Enteropneusta (Acorn Worms) === + +== Echinodermata == + +Acanthaster planci, starfish (2014) +Apostichopus japonicus, sea cucumber (2017) +Arbacia lixula, black sea urchin (2024) +Astropecten irregularis, sand sea star (2024) +Australostichopus mollis, Australian sea cucumber (2016) +Chiridota hydrothermica, deep sea cucumber (2024) +Diadema setosum, Long-spined sea urchin (2024) +Echinometra lucunter, rock boring urchin (2023) +Ophionereis fasciata, mottled brittlestar (2016) +Patiriella regularis, the New Zealand common cushion star (2016) +Plazaster borealis, Octopus starfish (2022) +Strongylocentrotus purpuratus, a sea urchin and model deuterostome (2006) + +== Cephalocordata (Lancelets) == + +== Tunicates == + +=== Appendicularia === + +==== Order Copelata (Larvaceans) ==== + +Oikopleura dioica, a larvacean (2001). + +=== Acopa === + +==== Order Stolidobranchia ==== + +==== Thaliacea ==== + +===== Order Pyrosomida (Pyrosomes) ===== + +===== Order Salpida (Salps) ===== + +===== Order Doliolida ===== + +==== Enterogona ==== + +===== Order Phlebobranchia ===== +Ciona intestinalis, a tunicate (2002) +Ciona savignyi, a tunicate (2007) + +===== Order Aplousobranchia ===== + +== Vertebrates == + +=== Cartilaginous fish === + +==== Holocephali ==== + +===== Order Chimaeriformes (Chimeras) ===== + +==== Selachimorpha (True Sharks) ==== +Superorder Galeomorphi +Order Carcharhiniformes (Ground Sharks) +Scyliorhinus torazame, Cloudy catshark (2018) +Order Lamniformes (Mackerel Sharks) +Carcharodon carcharias, Great white shark (2018) +Order Orectolobiformes (Carpet Sharks) +Chiloscyllium plagiosum, Whitespotted bamboo shark (2020) +Chiloscyllium punctatum, Brownbanded bamboo shark (2018) +Rhincodon typus, Whale shark (2017) + +==== Batomorphi (Rays) ==== +Order Myliobatiformes +Potamotrygon leopoldi, Xingu river ray (2023 draft) +Order Rajiformes +Leucoraja erinacea, Little skate (2023) + +=== Ray-Finned Fish === + +==== Cladistia ==== +Order Polypteriformes +Polypterus senegalus, Senegal bichir, (2021) + +==== Chondrostei ==== +Order Acipenseriformes +Polyodon spathula, American paddlefish, (2021 draft) + +==== Holostei ==== +Order Amiiformes +Amia calva, Bowfin, (2021 draft) +Order Lepisosteiformes +Atractosteus spatula, Alligator gar, (2024) +Lepisosteus oculatus, Spotted gar \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-1.md b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-1.md new file mode 100644 index 000000000..87b55ad9f --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-1.md @@ -0,0 +1,249 @@ +--- +title: "List of sequenced animal genomes" +chunk: 2/6 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_animal_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:50.483884+00:00" +instance: "kb-cron" +--- + +==== Teleostei ==== +Order Anabantiformes +Betta splendens, Siamese fighting fish (2018) +Helostoma temminkii, Kissing gourami (2020) +Order Anguilliformes +Anguilla anguilla, European Eel (2012) +Anguilla japonica, Japanese Eel (2022) +Order Atheriniformes +Atherinopsis californiensis, Jack silverside (2023) +Order Beloniformes +Oryzias latipes, medaka (2007) +Order Callionymiformes +Callionymus lyra, common dragonet (2020) +Order Carangiformes +Caranx ignobilis, Giant trevally (2022) +Caranx melampygus, Bluefin trevally (2021) +Pseudocaranx georgianus, New Zealand trevally (2021) +Order Centrarchiformes +Oplegnathus fasciatus, barred knifejaw (2019) +Siniperca roulei (Slender Mandarinfish) (2025) +Order Characiformes +Astyanax jordani, Mexican cavefish (2014) +Astyanax mexicanus, Mexican tetra (2021) +Colossoma macropomum, Tambaqui (2021) +Hasemania nana, Silvertip tetra (2013) +Hyphessobrycon heterorhabdus, Flag tetra (2023) +Petitella bleheri, Firehead tetra (2015) +Psalidodon paranae, (2016) +Order Cichliformes +Oreochromis niloticus, Nile tilapia (2019) +Maylandia zebra, Lake Malawi cichlid (2019) +Order Clupeiformes +Clupea harengus, Atlantic herring (2020) +Coilia nasus, Japanese grenadier anchovy (2020) +Sardina pilchardus, European pilchard (2019) +Order Cypriniformes +Anabarilius grahami, Kanglang fish (2018) +Danio rerio, zebrafish (2007) +Leuciscus baicalensis, Siberian dace (2014) +Megalobrama amblycephala, Wuchang bream (2017) +Metzia formosae, (2015) +Opsarius caudiocellatus, (2022) +Oxygymnocypris stewartii, (2019) +Pseudobrama simoni (2020) +Rhodeus ocellatus, Rosy bitterling (2020) +Triplophysa bleekeri, Tibetan stone loach (2020) +Order Cyprinodontiformes +Fundulus catenatus, Northern studfish (2020) +Fundulus olivaceus, Blackspotted topminnow (2020) +Fundulus nottii, Bayou topminnow (2020) +Fundulus xenicus, Diamond killifish (2020) +Gambusia affinis, western mosquitofish (2020) +Heterandria formosa, least killifish (2019) +Micropoecilia picta, swamp guppy (2021) +Xiphophorus maculatus, platyfish (2013) +Nothobranchius furzeri, turquoise killifish (2015) +Order Esociformes +Esox lucius, northern pike (2014) +Order Gadiformes +Gadus macrocephalus, Pacific cod (2022) +Gadus morhua, Atlantic cod (2011) +Order Gasterosteiformes +Gasterosteus aculeatus, three-spined stickleback (2006, 2012) +Order Gobiiformes +Oxyeleotris marmorata, marble goby (2020) +Periophthalmus modestus, shuttles hoppfish or shuttles mudskipper (2022) +Order Gymnotiformes +Electrophorus electricus, electric eel (2014) +Order Lampriformes +Lampris incognitus, Smalleye Pacific Opah (2021) +Order Osmeriformes +Neosalanx tangkahkeii, Chinese icefish (2015) +Protosalanx hyalocranius, clearhead icefish (2017) +Order Osteoglossiformes +Heterotis niloticus, African arowana (2020) +Paramormyrops kingsleyae, mormyrid electric fish (2017) +Scleropages formosus, Asian arowana (2016) +Order Perciformes +Centropyge bicolor, bicolor angelfish (2021) +Chaetodon trifasciatus, melon butterflyfish (2020) +Channa argus, northern snakehead (2017) +Channa maculata, blotched snakehead (2021) +Chelmon rostratus, copperband butterflyfish (2020) +Chrysiptera cyanea, Sapphite damselfish (2024) +Dissostichus mawsoni, Antarctic toothfish (2019) +Eleginops maclovinus, Patagonian robalo (2019) +Epinephelus moara, kelp grouper (2021) +Larimichthys crocea, large yellow croaker (2014) +Lutjanus campechanus, Northern red snapper (2020) +Naso vlamingii, bignose unicornfish (2020) +Parachaenichthys charcoti, Antarctic dragonfish (2017) +Rachycentron canadum, Cobia (2024) +Seriola dumerili, Greater amberjack (2017) +Sillago sinica, chinese sillago (2018) +Siniperca knerii, Big-Eye Mandarin Fish (2020) +Sparus aurata, gilt-head bream (2018) +Holacanthus passer, King Angelfish (2024) +Oplegnathus fasciatus, Barred knifejaw (2024) +Order Pleuronectiformes +Microstomus kitt, Lemon sole (2025) +Order Salmoniformes +Salmo salar, Atlantic salmon (2016) +Oncorhynchus mykiss, rainbow trout (2014) +Oncorhynchus tshawytscha, Chinook salmon (2018) +Salvelinus namaycush, Lake Trout (2021) +Order Scorpaeniformes +Sebastes schlegelii, Black rockfish (2018) +Order Siluriformes +Clarias batrachus, walking catfish (2018) +Ictalurus punctatus, channel catfish (2016) +Pangasianodon hypophthalmus, Iridescent shark catfish (2021) +Silurus glanis, Wels catfish (2020) +Order Spariformes +Datnioides pulcher, Siamese tigerfish (2020) +Datnioides undecimradiatus, Mekong tiger perch (2020) +Order Syngnathiformes +Syngnathus scovelli, Gulf pipefish (2016, 2023) +Entelurus aequoreus, Snake pipefish (2024) +Order Tetraodontiformes +Diodon holocanthus, Long-spine porcupinefish (2020) +Mola mola, ocean sunfish (2016) +Takifugu rubripes, a puffer fish (2002) +Tetraodon nigroviridis, a puffer fish (2004) + +=== Lobe-Finned Fish (Excluding Tetrapods) === + +==== Coelacanths (Actinistia) ==== + +===== Order Coelacanthiformes ===== + +==== Lungfish (Dipnoi) ==== + +===== Order Ceratodontiformes ===== + +=== Amphibians === + +==== Frogs (Anura) ==== +Taudactylus pleione, Kroombit tinker frog (2023) +Leptobrachium leishanense, Leishan Moustache toad (2019) +Limnodynastes dumerilii dumerilii, Eastern banjo frog (2020) +Nanorana parkeri, High Himalaya frog (2015) +Oophaga pumilio, Strawberry poison-dart frog (2018) +Platyplectrum ornatum, Ornate burrowing frog (2021) +Pyxicephalus adspersus, African bullfrog (2018) +Rana [Lithobates] catesbeiana, North American bullfrog (2017) +Rana kukunoris, Plateau brown frog (2023) +Rhinella marina, Cane toad (2018) +Vibrissaphora ailaonica, Moustache toad (2019) +Xenopus tropicalis, western clawed frog (2010) +Mixophyes australis, Australian southern stuttering frog (2024) +Spea multiplicata, spadefoot toad (2019) +Pelobates cultripes, Western spadefoot toad (2022) +Dendrobates tinctorius, Dyeing poison frog (2024) +Ranitomeya imitator, mimic poison frog (2024) +Phyllobates terribilis, Dart-poison frog (2025) +Staurois parvus, foot-flagging frog (2023) + +==== Salamanders (Urodela) ==== +Clade Salamandroidea +Family Salamandridae +Pleurodeles waltl, Iberian ribbed newt, (2025) +Triturus cristatus, great crested newt (2025) +Family Ambystomatidae (Tiger Salamanders) +Ambystoma mexicanum, Axolotl (2018) + +==== Caecillians ==== +Family Dermophiidae +Geotrypetes seraphini, Gaboon caecillian, (2023) +Family Siphonopidae +Microcaecilia unicolor, a caecillian, (2023) + +=== Birds === + +==== Ratites (Palaeognathae) ==== + +===== Order Struthioniformes ===== + +===== Order Rheiformes (Rheas) ===== + +===== † Order Dinornithiformes (Moas) ===== + +===== Order Tinamiformes (Tinamous) ===== + +===== Order Apterygiformes (Kiwis) ===== + +===== Order Casuariiformes ===== + +==== Fowl (Galloanserae) ==== + +===== Order Anseriformes (Waterfowl) ===== + +===== Order Galliformes (Landfowl) ===== + +==== Neoaves ==== + +===== Mirandornithes ===== + +====== Order Phoenicopteriformes (Flamingos) ====== + +====== Order Podicipediformes (Grebes) ====== + +===== Columbaves ===== + +====== Order Columbiformes ====== + +====== Order Mesitornithiformes (Mesites) ====== + +====== Order Pterocliformes (Sandgrouse) ====== + +====== Order Musophagiformes (Turacos) ====== + +====== Order Otidiformes (Bustards) ====== + +====== Order Cuculiformes (Cuckoos) ====== + +===== Gruae ===== + +====== Order Opisthocomiformes ====== + +====== Order Gruiformes ====== + +====== Order Charadriiformes ====== + +===== Strisores ===== + +====== Order Caprimulgiformes (Nightjars) ====== + +====== Order Apodiformes ====== + +===== Phaethoquornithes ===== +Order Phaethontiformes + +====== Order Eurypygiformes ====== + +====== Order Gaviiformes (Loons) ====== + +====== Order Procellariiformes (Petrels) ====== + +====== Order Sphenisciformes (Penguins) ====== \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-2.md b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-2.md new file mode 100644 index 000000000..14807e9fd --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-2.md @@ -0,0 +1,260 @@ +--- +title: "List of sequenced animal genomes" +chunk: 3/6 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_animal_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:50.483884+00:00" +instance: "kb-cron" +--- + +Genus Aptenodytes (Great Penguins) +Aptenodytes forsteri, Emperor penguin (2014) +Aptenodytes patagonicus, King penguin (2019) +Genus Eudyptes (Crested Penguins) +Eudyptes chrysocome, Western rockhopper penguin (2019) +Eudyptes chrysolophus chrysolophus, Macaroni penguin (2019) +Eudyptes chrysolophus schlegeli, Royal penguin (2019) +Eudyptes filholi, Eastern rockhopper penguin (2019) +Eudyptes moseleyi, Northern rockhopper penguin (2019) +Eudyptes pachyrhynchus, Fiordland penguin (2019) +Eudyptes robustus, Snares penguin (2019) +Eudyptes sclateri, Erect-crested penguin (2019) +Genus Eudyptula (Little Penguins) +Eudyptula minor albosignata, White-flippered penguin (2019) +Eudyptula minor minor, Little blue penguin (2019) +Eudyptula novaehollandiae, Fairy penguin (2019) +Genus Megadyptes (Hoiho Penguins) +Megadyptes antipodes antipodes, Yellow-eyed penguin (2019) +Pygoscelis (Brush-tailed Penguins) +Pygoscelis adeliae, Adélie penguin (2014) +Pygoscelis antarctica, Chinstrap penguin (2019) +Pygoscelis papua, Gentoo penguin (2019) +Genus Spheniscus (Banded Penguins) +Spheniscus demersus, African penguin (2019) +Spheniscus humboldti, Humboldt penguin (2019) +Spheniscus magellanicus, Magellanic penguin (2019) +Spheniscus mendiculus, Galápagos penguin (2019) + +====== Order Ciconiiformes (Storks) ====== + +====== Order Suliformes ====== + +====== Order Pelecaniformes ====== + +===== Afroaves ===== + +====== Order Strigiformes (Owls) ====== + +====== Order Accipitriformes ====== +Add 87 hawk genomes found here: The Complete Genome Sequences of 87 Species of Hawks (Accipitriformes, Aves) + +====== Order Coliiformes (Mousebirds) ====== + +====== Order Leptosomiformes ====== + +====== Order Trogoniformes (Trogons) ====== + +====== Order Bucerotiformes ====== + +====== Order Coraciiformes ====== + +====== Order Piciformes ====== + +===== Australaves ===== + +====== Order Cariamiformes ====== + +====== Order Falconiformes (Falcons) ====== + +====== Order Psittaciformes (Parrots) ====== + +====== Order Passeriformes (Passerines) ====== + +=== Crocodilians === + +=== Turtles === + +==== Crytodira (Hidden-Neck Turtles) ==== + +===== Trionychia (Softshell Turtles) ===== + +===== Testudinoidea ===== + +===== Chelonioidea (Sea Turtles) ===== + +===== Chelydroidea ===== + +==== Pleurodira ==== + +=== Rhynchocephalia === + +==== Neosphenodontia ==== + +=== Squamates === + +==== Gekkota (Gekkos) ==== +Clade Gekkomorpha +Family Eublepharidae +Eublepharis macularius, Leopard gecko (2016) +Family Gekkonidae +Lepidodactylus listeri, Lister's gecko (2025) +Family Diplodactylidae +Correlophus ciliatus, crested gecko (2024) + +==== Scinciformata ==== +Clade Cordylomorpha +Family Cordylidae +Hemicordylus capensis, Cape cliff lizard, (2023) +Cryptoblepharus egeriae, Christmas Island blue-tailed skink (2025) + +==== Laterata ==== +Clade Teiformata +Family Teiidae +Salvator merianae, Argentine black and white tegu, (2018) +Clade Lacertiformata +Family Lacertidae +Zootoca vivipara, Viviparous lizard (2020) + +==== Toxicofera ==== + +===== Anguimorpha ===== +Clade Paleoanguimorpha +Family Shinisauridae +Shinisaurus crocodilurus, Chinese crocodile lizard, (2017) +Clade Neoanguimorpha +Family Helodermatidae +Heloderma charlesbogerti, Guatemalan beaded lizard, (2022) +Family Anguidae +Dopasia gracilis, Burmese glass lizard, (2015) + +===== Iguania ===== +Clade Acrodonta +Family Agamidae +Pogona vitticeps, Central bearded dragon, (2015) +Clade Pleurodonta +Family Dactyloidae +Anolis carolinensis, Carolina anole, (2011) +Family Phrynosomatidae +Phrynosoma platyrhinos, Dessert horned lizard, (2021) +Phrynosoma cornutum, Texas horned lizard, (2021) +Sceloporus undulatus, Eastern fence lizard (2021) + +===== Serpentes (Snakes) ===== +Clade Scolecophidia (Blindsnakes) +Family Typhlopidae +Anilios bituberculatus, Prong-snouted blind snake (2021) +Indotyphlops braminus, Brahminy blindsnake, (2022) +Clade Booidea +Family Pythonidae +Morelia viridis, Green Tree Python (2022) +Python bivittatus, Burmese python (2013) +Python regius, Ball python (2020) +Simalia boeleni, Boelen's Python (2022) +Family Boidae +Boa constrictor, Boa constrictor (2019) +Charina bottae, Rubber boa, (2022) +Clade Caenophidia +Family Viperidae +Azemiops feae, Fea's viper (2022) +Bothrops jararaca, Jararaca lancehead, (2021) +Crotalus adamanteus, Eastern diamondback rattlesnake (2021) +Crotalus mitchellii pyrrhus, southwestern speckled rattlesnake (2014) +Crotalus oreganus helleri, southern Pacific rattlesnake (2023) +Crotalus tigris, Tiger rattlesnake (2021) +Crotalus viridis, Great Plains rattlesnake (2018) +Daboia siamensis, Eastern Russell's viper (2022) +Deinagkistrodon acutus, Five-pacer viper (2016) +Protobothrops flavoviridis, Okinawa Habu (2018) +Protobothrops mucrosquamatus, Taiwanese Habu (2017, 2024) +Trimeresurus albolabris, White-lipped tree pit viper (2024) +Cerastes gasperetti, Arabian horned viper (2025) +Family Homalopsidae +Myanophis thanlyinesis, (No common name), (2021) +Family Colubridae +Ahaetulla prasina, Asian vine snake (2023) +Arizona elegans occidentalis, California glossy snake (2022) +Chrysopelea ornata, Ornate Flying Snake (2023) +Diadophis punctatus, ring-necked snake (2023) +Dolichophis caspius, Caspian whipsnake (2020) +Elaphe carinata, King ratsnake (2024) +Pantherophis guttatus, corn snake (2014) +Pantherophis obsoletus, Leucistic Texas Rat Snake (2021) +Ptyas mucosa, Oriental rat snake (2024) +Thamnophis sirtalis, Common garter snake (2018) +Thermophis baileyi, Tibetan hot-spring snake (2018) +Family Elapidae +Bungarus multicinctus, Many-banded krait (2022) +Emydocephalus ijimae, Ijima's turtle-headed sea snake, (2019) +Hydrophis curtus, Shaw's Sea Snake (2020) +Hydrophis cyanocinctus, blue-banded sea snakes (2021) +Hydrophis melanocephalus, slender-necked sea snake, (2019) +Laticauda colubrina, yellow-lipped sea krait, (2019) +Laticauda laticaudata, blue-lipped sea krait, (2019) +Naja atra, Chinese cobra (2024) +Naja naja, Indian cobra (2020) +Notechis scutatus, mainland tiger snake (2022) +Ophiophagus hannah, king cobra (2013) +Pseudonaja textilis, eastern brown snake (2022) + +=== Mammals === + +==== Monotremes ==== + +==== Marsupials ==== +Order Didelphimorphia +Family Didelphidae (opossums) +Monodelphis domestica, gray short-tailed opossum (2007) +Order Dasyuromorphia +Family Dasyuridae +Antechinus stuartii, brown antechinus (2020) +Sarcophilus harrisii, Tasmanian devil () +Sminthopsis crassicaudata, fat-tailed dunnart (ongoing) +Dasyurus hallucatus, northern quoll (ongoing) +Family Myrmecobiidae +Myrmecobius fasciatus, numbat (ongoing) +† Family Thylacinidae +† Thylacinus cynocephalus, thylacine () +Order Peramelemorphia +Family Peramelidae +Perameles gunnii, eastern barred bandicoot (ongoing) +Family Thylacomyidae +Macrotis lagotis, greater bilby (ongoing) +Order Notoryctemorphia, Family Notoryctidae +Notoryctes typhlops, southern marsupial mole (ongoing) +Order Diprotodontia +Family Macropodidae +Macropus eugenii, tammar wallaby (2011) +Petrogale penicillata, brush-tailed rock-wallaby (ongoing) +Family Potoroidae +Bettongia gaimardi, eastern bettong (ongoing) +Bettongia penicillata ogilbyi, woylie (2021) +Family Petauridae +Gymnobelideus leadbeateri, Leadbeater's possum (ongoing) +Family Burramyidae +Burramys parvus, mountain pygmy possum (ongoing) +Family Vombatidae +Vombatus ursinus, common wombat (ongoing) +Family Phascolarctidae +Phascolarctos cinereus, koala (2013 draft) + +==== Placentals ==== + +===== Afrotheria ===== + +====== Order Hyracoidea ====== +Family Procaviidae +Procavia capensis, Rock hyrax, (2011) + +====== Order Proboscidea ====== +Family Elephantidae (Elephants) +Elephas maximus, Asian elephant, (2015, 2024) +† Mammuthus primigenius, Wooly mammoth, (2015) +Loxodonta africana, African bush elephant, (2009, 2024) +Loxodonta cyclotis, African forest elephant, (2018) + +====== Order Sirenia (Sea Cows) ====== +Family Trichechidae +Trichechus manatus, West Indian manatee, (2015) +Family Dugongidae +Dugong dugon, Dugong, (2024) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-3.md b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-3.md new file mode 100644 index 000000000..f8e239791 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-3.md @@ -0,0 +1,196 @@ +--- +title: "List of sequenced animal genomes" +chunk: 4/6 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_animal_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:50.483884+00:00" +instance: "kb-cron" +--- + +===== Euarchontoglires ===== +Order Lagomorpha +Family Leporidae +Oryctolagus cuniculus, European rabbit (2010) +Order Primates +Family Callitrichidae +Callithrix jacchus, Common marmoset (2010, whole genome 2014) +Family Cercopithecidae +Macaca mulatta, rhesus macaque (2007 & Chinese rhesus macaque Macaca mulatta lasiota in 2011) +Macaca fascicularis, Cynomolgus or crab-eating macaque (2011) +Papio anubis, olive baboon (2020) +Papio cynocephalus, yellow baboon (2016) +Rhinopithecus roxellana, golden snub-nosed monkey (2019) +Family Galagidae +Otolemur garnettii, small-eared galago, or bushbaby () +Family Hominidae +Subfamily Ponginae +Pongo pygmaeus/Pongo abelii, orangutan (Borneo/Sumatra) (2011) +Subfamily Homininae +Gorilla gorilla, western gorilla (2012) +Homo sapiens, modern human (draft 2001, whole genome 2022) +† Homo neanderthalensis, Neanderthal (draft 2010) +Pan troglodytes, chimpanzee (2005) +Pan paniscus, bonobo (2012) +Order Rodentia +Family Caviidae +Hydrochoerus hydrochaeris, capybara (2018) +Family Cricetidae +Microtus montanus, Montane vole (2021) +Microtus richardsoni, North American Water Vole (2021) +Peromyscus leucopus, white-footed mouse (2019) +Family Heteromyidae +Perognathus longimembris pacificus, Pacific Pocket Mouse +Family Muridae +Mastomys coucha, Southern multimammate mouse (2019) +Mus musculus Strain: C57BL/6J, House mouse (2002) +Rattus norvegicus, Brown rat (2004) + +===== Laurasiatheria ===== +Order Artiodactyla (even-toed ungulates) +Family Antilocapridae +Antilocapra americana, pronghorn (2019) +Family Balaenidae +Balaena mysticetus, bowhead whale (2015) +Eubalaena glacialis, North Atlantic right whale (2018) +Family Balaenopteridae +Balaenoptera acutorostrata, common minke whale (2014) +Balaenoptera borealis, sei whale (2018) +Balaenoptera musculus, blue whale (2018) +Balaenoptera physalus, fin whale (2014) +Megaptera novaeangliae, humpback whale (2018) +Family Bovidae +Ammotragus lervia, Barbary sheep (2019) +Antidorcas marsupialis, Springbox (2019) +Bison bonasus, European bison (2017) +Bos grunniens, yak 2012 () +Bos primigenius indicus, zebu or Brahman cattle (2012) +Bos primigenius taurus, cow 2009 () +Bubalus bubalis, river buffalo (2017) +Budorcas taxicolor, Takin (2023) +Capra ibex, Goats (2019) +Cephalophus harveyi, Harvey's duiker (2019) +Connochaetes taurinus, blue wildebeest (2019) +Damaliscus lunatus, common tsessebe (2019) +Gazella thomsoni, Thomson's gazelle (2019) +Hippotragus niger, Sable Antelope (2019) +Kobus ellipsiprymnus, Waterbuck (2019) +Litocranius walleri, Gerenuk (2019) +Oreotragus oreotragus, Klipspringer (2019) +Oryx gazella, Gemsbok (2019) +Ourebia ourebi, Oribi (2019) +Ovis ammon, Argali (2019) +Ovis ammon polii, marco polo sheep (2017) +Nanger granti, Grant's gazelle (2019) +Neotragus moschatus, Suni (2019) +Neotragus pygmaeus, Royal antelope (2019) +Philantomba maxwellii, Maxwell's duiker (2019) +Procapra przewalskii, Przewalski's gazelle (2019) +Pseudois nayaur, Bharal (2019) +Pseudoryx nghetinhensis, Saola (2025) +Raphicerus campestris, Steenbox (2019) +Redunca redunca, Bohor reedbuck (2019) +Syncerus caffer, African buffalo (2019) +Sylvicapra grimmia, common duiker (2019) +Tragelaphus, Spiral-horned bovine (2019) +Tragelaphus buxtoni, Mountain nyala (2019) +Tragelaphus strepsiceros, Greater kudu (2019) +Tragelaphus imberbis, Lesser kudu (2019) +Tragelaphus spekii, Sitatunga (2019) +Tragelaphus scriptus, Bushbuck (2019) +Taurotragus oryx, Common eland (2019) +Family Camelidae +Camelus ferus, Wild Bactrian camel (2007) +Family Cervidae +Cervus albirostris, Tharold's deer (2019) +Elaphurus davidianus, Père David's deer (2018) +Muntiacus crinifrons, hairy-fronted muntjac (2019) +Muntiacus muntjak, Indian muntjac (2019) +Muntiacus reevesi, Reeves's muntjac (2019) +Odocoileus hemionus, mule deer (2021) +Rangifer tarandus, Reindeer (2017) +Rusa alfredi, Visayan spotted deer (2025) +Family Delphinidae +Tursiops truncatus, bottlenosed dolphin (2012) +Neophocaena phocaenoides, finless porpoise (2014) +Orcinus orca, killer whale (2015) +Sousa chinensis, Indo-Pacific humpback dolphin (2019) +Family Eschrichtiidae +Eschrichtius robustus, gray whale (2018) +Family Giraffidae +Giraffa camelopardalis, Giraffe (2019) +Giraffa camelopardalis tippelskirchi, Masai giraffe (2019) +Okapia johnstoni, Okapi (2019) +Family Monodontidae +Delphinapterus, beluga whale (2017) +Family Moschidae +Moschus berezovskii, forest musk deer (2018) +Moschus chrysogaster, Alpine musk deer (2019) +Family Phocoenidae +Neophocaena asiaeorientalis sunameri, East Asian finless porpoise (2024) +Neophocaena asiaorientalis asiaorientalis, Yangtze finless porpoise (2024) +Family Physeteridae +Physeter macrocephalus, sperm whale (2019) +Family Suidae +Sus scrofa, pig (2012) +Family Tragulidae +Tragulus javanicus, Java mouse-deer (2019) +Order Carnivora +Family Felidae +Acinonyx jubatus, cheetah (2015) +Felis catus, cat (2007) +Panthera leo, lion (2013) +Panthera pardus, Amur leopard (2016) +Panthera tigris tigris, Siberian tiger (2013) +Panthera tigris tigris, Bengal tiger (2013) +Panthera uncia, snow leopard (2013) +Prionailurus bengalensis, leopard cat (2016) +Family Canidae +Canis familiaris, dog (2005) +Canis lupus lupus, wolf (2017). +Lycaon pictus, african wild dog (2018) +Family Ursidae +Ailuropoda melanoleuca, giant panda (2010) +Ursus arctos ssp. horribilis, Grizzly bear (2018) +Ursus americanus, American black bear (2019) +Ursus maritimus, Polar bear (2014) +Family Odobenidae +Odobenus rosmarus, walrus (2015) +Family Phocidae +Pusa sibirica, Baikal seal (2024) +Pusa caspica, Caspian seal (2024) +Phoca vitulina, Harbor seal (2024) +Pusa hispida, Ringed seal (2024) +Family Mustelidae +Enhydra lutris kenyoni, sea otter (2017) +Mustela erminea, stoat (2018) +Mustela furo, ferret (2014) +Pteronura brasiliensis, giant otter (2019) +Order Chiroptera +Family Megadermatidae +Megaderma lyra, greater false vampire bat (2013) +Family Mormoopidae +Pteronotus parnellii, Parnell's mustached bat (2013) +Family Pteropodidae +Pteropus vampyrus, fruit bat (2012) +Eidolon helvum, Old World fruit bat (2013) +Family Rhinolophidae +Rhinolophus ferrumequinum, greater horseshoe bat (2013) +Family Vespertilionidae +Myotis lucifugus, little brown bat (2010) +Myotis mystacinus, whiskered bat (2024) +Family Phyllostomidae +Leptonycteris yerbabuenae, long nosed bat (2020) +Leptonycteris nivalis, greater long nosed bat (2020) +Musonycteris harrisoni, banana bat (2020) +Artibeus jamaicensis, Jamaican fruit bat (2020) +Macrotus waterhousii, Waterhouse's leaf-nosed bat (2020 +Order Erinaceomorpha, Family Erinaceidae +Erinaceus europaeus, western European hedgehog () +Order Eulipotyphla, Family Solenodontidae +Solenodon parodoxus, Hispaniolan solenodon (2018) +Order Perissodactyla (odd-toed ungulates) +Family Equidae +Equus caballus, horse (2009 2018) + +== Arthropods == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-4.md b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-4.md new file mode 100644 index 000000000..2ccb8565c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-4.md @@ -0,0 +1,221 @@ +--- +title: "List of sequenced animal genomes" +chunk: 5/6 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_animal_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:50.483884+00:00" +instance: "kb-cron" +--- + +=== Insects === +Order Blattodea +Blattella germanica, German cockroach (2018) +Periplaneta americana, American cockroach (2018) +Zootermopsis nevadensis, a dampwood termite (2014 +Cryptotermes secundus, a drywood termite(2018) +Macrotermes natalensis, a higher termite (2014 +Order Coleoptera +Dendroctonus ponderosae Hopkins, beetle (mountain pine beetle) (2013) +Aquatica lateralis, Japanese aquatic firefly "Heike-botaru" (firefly) (2018) +Photinus pyralis, Big Dipper firefly (2018) +Protaetia brevitarsis, White-spotted flower chafer (2019) +Tribolium castaneum Strain:GA-2, beetle (red flour beetle) (2008) +Allomyrina dichotoma, Japanese rhinoceros beetle (2022) +Pachyrhynchus sulphureomaculatus, Easter Egg Weevil (2021) +Order Collembola +Family Isotomidae +Desoria tigrina, (2021) +Family Sminthurididae +Sminthurides aquaticus, (2021) +Order Diptera +Family Calliphoridae +Aldrichina grahami, Forensic blowfly (2020) +Family Chironomidae +Dasypogon diadema, Hunting Robber fly (2019) +Parochlus steinend, Antarctic winged midge (2017) +Proctacanthus coquilletti, Assassin fly (2017) +Family Culicidae (mosquitoes) +Aedes aegypti Strain:LVPib12, mosquito (vector of dengue fever, etc.) (2007) +Aedes albopictus (2015) +Anopheles darlingi +Anopheles gambiae Strain: PEST, mosquito (vector of malaria) (2002) +Anopheles gambiae Strain: M, mosquito (vector of malaria) (2010) +Anopheles gambiae Strain: S, mosquito (vector of malaria) (2010) +Anopheles sinensis, mosquito (vector of vivax malaria, lymphatic filariasis and Setaria infections), (2014) +Anopheles stephensii +Anopheles arabiensis (2015) +Anopheles quadriannulatus (2015) +Anopheles merus (2015) +Anopheles melas (2015) +Anopheles christyi (2015) +Anopheles epiroticus (2015) +Anopheles maculatus (2015) +Anopheles culicifacies (2015) +Anopheles minimus (2015) +Anopheles funestus (2015, 2019) +Anopheles dirus (2015) +Anopheles farauti (2015) +Anopheles atroparvus (2015) +Anopheles sinensis (2015) +Anopheles albimanus (2015) +Culex quinquefasciatus, mosquito (vector of West Nile virus, filariasis etc.) (2010) +Family Drosophilidae (fruit flies) +Drosophila albomicans, fruit fly (2012) +Drosophila ananassae, fruit fly (2007) +Drosophila biarmipes, fruit fly (2011) +Drosophila bipectinata, fruit fly (2011) +Drosophila erecta, fruit fly (2007) +Drosophila elegans, fruit fly (2011) +Drosophila eugracilis, fruit fly (2011) +Drosophila ficusphila, fruit fly (2011) +Drosophila grimshawi, fruit fly (2007) +Drosophila kikkawai, fruit fly (2011) +Drosophila melanogaster, fruit fly (model organism) (2000) +Drosophila mojavensis, fruit fly (2007) +Drosophila neotestacea, fruit fly (transcriptome 2014) +Drosophila persimilis, fruit fly (2007) +Drosophila pseudoobscura, fruit fly (2005) +Drosophila rhopaloa, fruit fly (2011) +Drosophila santomea, fruit fly () +Drosophila sechellia, fruit fly (2007) +Drosophila simulans, fruit fly (2007) +Drosophila takahashi, fruit fly (2011) +Drosophila virilis, fruit fly (2007) +Drosophila willistoni, fruit fly (2007) +Drosophila yakuba, fruit fly (2007) +Family Phoridae +Megaselia abdita, scuttle fly (transcriptome 2013) +Family Psychodidae (drain flies) +Clogmia albipunctata, moth midge (transcriptome 2013) +Family Sarcophagidae (flesh flies) +Sarcophaga Bullata, Flesh fly (2019) +Family Syrphidae (hoverflies) +Episyrphus balteatus, hoverfly (transcriptome 2011) +Order Hemiptera +Acyrthosiphon pisum, aphid (pea aphid) (2010) +Ericerus pela, Chinese wax scale insect (2019) +Laodelphax striatellus, small brown planthopper (2017) +Lycorma delicatula, spotted lanternfly (2019) +Rhodnius prolixus, kissing-bug (2015) +Rhopalosiphum maidis, Corn leaf aphid (2019) +Sitobion miscanthi, Indian grain aphid (2019) +Triatoma rubrofasciata, assassin bug (2019) +Order Hymenoptera +Acromyrmex echinatior colony Ae372, ant (Panamanian leafcutter) (2011) +Apis mellifera, bee (honey bee), (model for eusocial behavior) (2006) +Atta cephalotes, ant (leaf-cutter ant) (2011) +Camponotus floridanus, ant (2010) +Cerapachys biroi, ant (clonal raider ant)(2014) +Euglossa dilemma, Green orchid bee (2017) +Harpegnathos saltator, ant (2010) +Lasius niger, ant (black garden ant)(2017) +Linepithema humile, ant (Argentine ant) (2011) +Nasonia giraulti, wasp (parasitoid wasp) (2010) +Nasonia longicornis, wasp (parasitoid wasp) (2010) +Nasonia vitripennis, wasp (parasitoid wasp; model organism) (2010) +Nomia Melanderi, Alkali bee (2019) +Pogonomyrmex barbatus, ant (red harvester ant) (2011) +Solenopsis invicta, ant (fire ant) (2011) +Order Lepidoptera +Abrostola tripartita Hufnagel, Spectacle (2021) +Achalarus lyciades, Hoary Edge Skipper (2017) +Ahamus jianchuanensis, Jianchuan ghost moth (2024) +Antharaea yamamai, Japanese oak silk moth (2019) +Arctia plantaginis, Wood tiger moth (2020) +Bicyclus anynana, squinting bush brown (2017) +Bombyx mori Strain:p50T, moth (domestic silk worm) (2004) +Calycopis cecrops, Red-Banded Groundstreak (2016) +Calycopis isobeon, Dusky-Blue Groundstreak (2016) +Coenonympha arcania, Pearly Heath (2024) +Cydia pomonella, codling moth (2019) +Danaus plexippus, monarch butterfly) (2011) +Heliconius melpomene, butterfly (2012) +Keiferia lycopersicella, Tomato pinworm (2024) +Melitaea cinxia, Glanville fritillary butterfly (2014) +Megathymus ursus violae, bear giant skipper butterfly (2018) +Morpho helenor, Common blue morpho (2023) +Morpho achilles, Blue-banded morpho (2023) +Morpho deidamia (2023) +Papilio bianor, Chinese peacock butterfly (2019) +Phthorimaea absoluta, Tomato leafminer (2024) +Pieris rapae, small cabbage white butterfly (2016) +Plodia interpunctella, Indianmeal moth (2022) +Plutella xylostella, moth (diamondback moth) (2013) +Scrobipalpa atriplicella, Goosefoot groundling moth (2024) +Spodoptera frugiperda, Fall armyworm (2017) +Thitarodes armoricanus, Himalaya ghost moth (2024) +Thitarodes xiaojinensis, Xiaojin ghost moth (2024) +Troides aeacus, Golden birdwing (2024) +Eudocima phalonia, fruit-piercing moth (2017) +Order Orthoptera +Locusta migratoria, migratory locust (2014) +Schistocerca gregaria, desert locust (2020) +Gryllus bimaculatus, two-spotted cricket (2021) +Order Phthiraptera +Pediculus humanus, louse (sucking louse; parasite) (2010) +Menopon gallinae, Poutlry shaft louse (2024) +Psocoptera +Liposcelis brunnea, booklouse (2022) +Order Raphidioptera +Venustoraphidia nigricollis, black-necked snakefly (2023) +Order Trichoptera +Eubasilissa regina, purple caddisfly (2022,) +Stenopsyche tienmushanensisi, Caddisfly (2018) +Order Mantodea +Tenodera sinensis, chinese praying mantis (2023) + +=== Crustaceans === +Acartia tonsa dana, cosmopolitan calanoid copepod (2019) +Cherax quadricarinatus, Red claw crayfish (2020) +Daphnia pulex, water flea (2007) +Eulimnadia texana, Clam Shrimp (2018) +Macrobrachium nipponense, oriental river prawn (2021) +Neocaridina denticulata, shrimp (2014) +Parhyale hawaiensis, amphipod (2016) +Pollicipes pollicipes, Gooseneck barnacle (2022) +Portunus trituberculatus, swimming crab (2020) +Procambarus virginalis, marbled crayfish (2018) +Sphaeroma terebrans, a wood-boring isopod (2019) +Tigriopus kingsejongensis, antarctic-endemic copepod (2017) + +=== Chelicerates === +Order Xiphosura: + +Limulus polyphemus, Atlantic horseshoe crab (2014) +Carcinoscorpius rotundicauda, mangrove horseshoe crab (2021) +Tachypleus tridentatus, tri-spine horseshoe crab (2021) +Order Ixodida: + +Ixodes scapularis, deer tick (2016) +Order Mesostigmata: + +Tropilaelaps mercedesae, honeybee mite (2017) +Order Trombidiformes: + +Tetranychus urticae, spider mite (2011) +Order Scorpiones: + +Mesobuthus martensii, Chinese scorpion (2013) +Order Araneae: + +Acanthoscurria geniculata, Brazilian whiteknee tarantula (2014) +Argiope bruennichi, European wasp spider (2021) +Dysdera silvatica, Canary Island nocturnal endemic woodlouse spider (2019) +Latrodectus elegans, Black widow spider (2022) +Nephila clavipes, (golden silk orb-weaver) (2017) +Parasteatoda tepidariorum, (common house spider) (2017) +Stegodyphus mimosarum, African social velvet spider (2014) +Uloborus diversus, Cribellate orb-weaving spider, (2023) +Order Uropygi: + +Mastigoproctus giganteus, giant whip scorpion or vinegaroon (2025) + +=== Myriapods === +Strigamia maritima, centipede +Trigoniulus corallinus, millipede + +== Onychophora (Velvet Worms) == + +== Tardigrades == +Hypsibius dujardini, water bear (2015) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-5.md b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-5.md new file mode 100644 index 000000000..bc160023c --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_animal_genomes-5.md @@ -0,0 +1,147 @@ +--- +title: "List of sequenced animal genomes" +chunk: 6/6 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_animal_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:50.483884+00:00" +instance: "kb-cron" +--- + +== Nematodes == +Ancylostoma ceylanicum, zoonotic hookworm infecting both humans and other mammals (2015) +Aplectana chamaeleonis, amphibian parasite (2023) +Ascaris suum, pig-infecting giant roundworm, closely related to human-infecting giant roundworm Ascaris lumbricoides (2011) +Brugia malayi (Strain:TRS), human-infecting filarial parasite (2007) +Bursaphelenchus xylophilus, infects pine trees (2011) +Caenorhabditis angaria (Strain:PS1010) (2010) +Caenorhabditis brenneri, a gonochoristic (male-female obligate) species more closely related to C. briggsae than C. elegans +Caenorhabditis briggsae (2003) +Caenorhabditis elegans (Strain:Bristol N2), model organism (1998) +Caenorhabditis remanei, a gonochoristic (male-female obligate) species more closely related to C. briggsae than C. elegans +Dirofilaria immitis, dog-infecting filarial parasite (2012) +Globodera pallida, plant pathogen (2014) +Haemonchus contortus, blood-feeding parasite infecting sheep and goats (2013) +Heterodera glycines, soybean cyst nematode (2019) +Heterorhabditis bacteriophora, (2013) +Loa loa, human-infecting filarial parasite (2013) +Meloidogyne hapla, northern root-knot nematode (plant pathogen) (2008) +Meloidogyne incognita, southern root-knot nematode (plant pathogen) (2008) +Necator americanus, human-infecting hookworm (2014) +Onchocerca volvulus, human-infecting filarial parasite +Pristionchus pacificus, model invertebrate (2008) +Romanomermis culicivorax, entomopathogenic nematode that invades larvae of various mosquito species (2013) +Trichuris suis, pig-infecting whipworm (2014) +Trichuris muris, mouse-infecting whipworm (2014) +Trichuris trichiura, human-infecting whipworm (2014) +Wuchereria bancrofti, human-infecting filarial parasite + +== Nematomorpha == + +== Priapulida == + +== Kinorhyncha == + +== Loricifera == + +== Molluscs == + +=== Polyplacophora (Chitons) === + +=== Caudofoveata === + +=== Cephalopods === +Architeuthis dux, giant squid (2020) +Euprymna scolopes, Hawaiian bobtail squid (2019) +Hapalochlaena maculosa, Southern blue-ringed octopus (2020) +Octopus bimaculoides, California two-spot octopus (2015) +Octopus minor, common long-arm octopus (2018) +Octopus vulgaris, common octopus (2019) + +=== Bivalves === +Argopecten purpuratus, peruvian scallop (2018) +Bathymodiolus platifrons, seep mussel (2017) +Chlamys farreri, Zhikong scallop (2017) +Crassostrea angulata, Portuguese oyster (2023) +Crassostrea gigas, Pacific oyster (2012) +Dreissena rostriformis, Quagga mussel (2019) +Limnoperna fortunei, invasive golden mussel (2017) +Margaritifera margaritifera, European freshwater pearl mussel (2023) +Modiolus philippinarum, shallow water mussel (2017) +Mytilus galloprovincialis, Mediterranean mussel (2016) +Panopea generosa, Pacific geoduck (2023) +Patinopecten yessoensis, Yesso scallop (2017) +Pecten maximus, Great scallop (2020) +Pinctada fucata, Pearl oyster (2012) +Ruditapes philippinarum, Manila clam (2017) +Saccostrea glomerata, Sydney rock oyster (2018) +Scapharca broughtonii, Blood clam (2019) +Tridacna crocea, Giant clam (2023) +Venustaconcha ellipsiformis, freshwater mussel (2018) + +=== Gastropods === +Achatina fulica, giant African snail (2019) +Biomphalaria glabrata, a medically important air-breathing freshwater snail in the family Planorbidae (2017) +Biomphalaria straminea, Ramshorn snail (2022) +Candidula unifasciata, Land snail (2021) +Conus ventricosus, Mediterranean cone snail (2021) +Elysia chlorotica, a solar-powered sea slug (2019) +Haliotis discus hannai, pacific abalone (2017) +Kalloconus canariensis, Canary Island cone shell (2023) +Kelletia kelletii, Kellet's whelk (2023) +Lottia gigantea, owl limpet (2013) +Plakobranchus ocellatus, Kleptoplastic sea slug (2021) +Pomacea canaliculata, golden apple snail (2018) +Littorina brevicula, periwinkle snail (2024) +Littoraria sinensis (2024) + +=== Scaphopods === + +==== Dentaliida ==== + +==== Gadilida ==== + +== Platyhelminthes == +Clonorchis sinensis, liver fluke (human pathogen) (draft 2011) +Echinococcus granulosus, tapeworm (dog pathogen) (2013, 2013) +Echinococcus multilocularis, tapeworm (2013) +Hymenolepis microstoma, tapeworm (2013) +Schistosoma haematobium, schistosome (human pathogen) (2012 2019) +Schistosoma japonicum, schistosome (human pathogen) (2009) +Schistosoma mansoni, schistosome (human pathogen) (2009, 2012) +Schmidtea mediterranea, planarian (model organism) (2006) +Taenia solium, tapeworm (2013) + +== Annelids == +Capitella teleta, polychaete (2007, 2013) +Helobdella robusta, leech (2007, 2013) +Eisenia fetida, earthworm (2015, 2016) +Paraescarpia echinospica, deep-sea tubeworm (2021,) +Hirudinaria manillensis, Asian Buffalo leech (2023) +Hirudo nipponia, Japanese blood-sucking leech (2023) +Whitmania pigra, Asian freshwater leech (2023) + +== Bryozoa == +Bugula neritina, bryozoan (2020,) + +== Brachiopoda == +Lingula anatina, brachiopod (2015,) + +== Rotifera == +Adineta vaga, rotifer (2013,) + +== See also == +Lists of sequenced genomes +List of sequenced bacterial genomes +List of sequenced archaeal genomes +List of sequenced eukaryotic genomes +List of sequenced mitochondrial genomes +List of sequenced plastomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant genomes +List of sequenced plant mitochondrial genomes +List of sequenced protist genomes + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_archaeal_genomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_archaeal_genomes-0.md new file mode 100644 index 000000000..022c75a5e --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_archaeal_genomes-0.md @@ -0,0 +1,100 @@ +--- +title: "List of sequenced archaeal genomes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_archaeal_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:51.865642+00:00" +instance: "kb-cron" +--- + +This list of sequenced archaeal genomes contains all the archaea known to have publicly available complete genome sequences that have been assembled, annotated and deposited in public databases. Methanococcus jannaschii was the first archaeon whose genome was sequenced, in 1996. +Currently in this list there are 39 genomes belonging to Crenarchaeota species, 105 belonging to the Euryarchaeota, 1 genome belonging to Korarchaeota and to the Nanoarchaeota, 3 belonging to the Thaumarchaeota and 1 genome belonging to an unclassified Archaea, totalling 150 Archaeal genomes. + + +== Crenarchaeota == + + +=== Acidilobales === + + +=== Desulforococcales === + + +=== Sulfolobales === + + +=== Thermoproteales === + + +== Euryarchaeota == + + +=== Archaeoglobi === + + +=== Halobacteria === + + +=== Methanobacteria === + + +=== Methanococci === + + +=== Methanomicrobia === + + +=== Methanopyri === + + +=== Thermococci === + + +=== Thermoplasmata === + + +=== Unclassified Euryarchaeota === + + +== Korarchaeota == + + +== Nanoarchaeota == + + +== Thaumarchaeota == + + +=== Cenarchaeales === + + +=== Nitrosopumilales === + + +== Unclassified Archaea == + + +== See also == +Genome project +Human microbiome project +Lists of sequenced genomes +List of sequenced bacterial genomes +List of sequenced eukaryotic genomes +List of sequenced mitochondrial genomes +List of sequenced plastomes +List of sequenced animal genomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant genomes +List of sequenced plant mitochondrial genomes +List of sequenced protist genomes + + +== References == + + +== External links == +GOLD:Genomes OnLine Database v 2.0 +SUPERFAMILY comparative genomics database Includes genomes of completely sequenced archaea, and sophisticated datamining plus visualisation tools for analysis \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_bacterial_genomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_bacterial_genomes-0.md new file mode 100644 index 000000000..ac30be9f0 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_bacterial_genomes-0.md @@ -0,0 +1,135 @@ +--- +title: "List of sequenced bacterial genomes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_bacterial_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:10.694185+00:00" +instance: "kb-cron" +--- + +This list of sequenced eubacterial genomes contains most of the eubacteria known to have publicly available complete genome sequences. Most of these sequences have been placed in the International Nucleotide Sequence Database Collaboration, a public database which can be searched on the web. A few of the listed genomes may not be in the INSDC database, but in other public databases. +Genomes listed as "Unpublished" are in a database, but not in the peer-reviewed scientific literature. +For the genomes of archaea see list of sequenced archaeal genomes. +For the genomes of organelles with a bacterial origin, see list of sequenced mitochondrial genomes and list of sequenced plastomes + + +== Abditibacteriota == + + +== Actinomycetota == + + +== Aquificota == + + +== Armatimonadota == + + +== Bacteroidota/Chlorobiota group == + + +== Caldisericota == + + +== Chlamydiota/Verrucomicrobiota group == + + +== Chloroflexota == + + +== Chrysiogenota == + + +== Cyanobacteria == + + +== Deferribacterota == + + +== Deinococcota == + + +== Dictyoglomota == + + +== Elusimicrobiota == + + +== Fibrobacterota/Acidobacteriota group == + + +== Bacillota == + + +== Fusobacteriota == + + +== Gemmatimonadota == + + +== Nitrospirota == + + +== Planctomycetota == + + +== Pseudomonadota == + + +=== Alphaproteobacteria === + + +=== Betaproteobacteria === + + +=== Gammaproteobacteria === + + +=== Zetaproteobacteria === + + +== Myxococcota–Campylobacterota == + + +== Spirochaetota == + + +== Synergistota == + + +== Mycoplasmatota == + + +== Thermodesulfobacteriota == + + +== Thermotogota == + + +== See also == +Genome project +Human microbiome project +List of sequenced archaeal genomes +List of sequenced eukaryotic genomes +List of sequenced mitochondrial genomes +List of sequenced plastomes +List of sequenced animal genomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant genomes +List of sequenced plant mitochondrial genomes +List of sequenced protist genomes + + +== References == + +In silico analysis of complete bacterial genomes: PCR, AFLP–PCR and endonuclease restriction +Combining diverse evidence for gene recognition in completely sequenced bacterial genomes +Intragenomic heterogeneity between multiple 16S ribosomal RNA operons in sequenced bacterial genomes + + +== External links == +BacMap — an up-to-date electronic atlas of annotated bacterial genomes +SUPERFAMILY comparative genomics database Includes genomes of completely sequenced prokaryotes, and sophisticated datamining plus visualisation tools for analysis \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_eukaryotic_genomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_eukaryotic_genomes-0.md new file mode 100644 index 000000000..4c500d8f9 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_eukaryotic_genomes-0.md @@ -0,0 +1,61 @@ +--- +title: "List of sequenced eukaryotic genomes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_eukaryotic_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:16.090445+00:00" +instance: "kb-cron" +--- + +This list of "sequenced" eukaryotic genomes contains all the eukaryotes known to have publicly available complete nuclear and organelle genome sequences that have been sequenced, assembled, annotated and published; draft genomes are not included, nor are organelle-only sequences. +DNA was first sequenced in 1977. The first free-living organism to have its genome completely sequenced was the bacterium Haemophilus influenzae, in 1995. In 1996 Saccharomyces cerevisiae (baker's yeast) was the first eukaryote genome sequence to be released and in 1998 the first genome sequence for a multicellular eukaryote, Caenorhabditis elegans, was released. +For mitochondrial genomes, see list of mitochondrial genomes. + + +== Protists == +Following are the nine earliest sequenced genomes of protists. For a more complete list, see the List of sequenced protist genomes. + + +== Plants == +Following are the five earliest sequenced genomes of plants. For a more complete list, see the List of sequenced plant genomes. + + +== Fungi == +Following are the five earliest sequenced genomes of fungi. For a more complete list, see the List of sequenced fungi genomes. + + +== Animals == +Following are the five earliest sequenced genomes of animals. For a more complete list, see the List of sequenced animal genomes. + + +== See also == +Genome project, Human genome +Genomic organization +History of genetics +Lists of sequenced genomes +List of sequenced bacterial genomes +List of sequenced archaeal genomes +List of sequenced mitochondrial genomes +List of sequenced plastomes +List of sequenced animal genomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant genomes +List of sequenced plant mitochondrial genomes +List of sequenced protist genomes + + +== References == + + +== External links == +Diark - a resource for eukaryotic genome research +EMBL-EBL Eukaryotic Genomes +UCSC Genome Browser +International Sequencing Consortium - Large-scale Sequencing Project Database +Ensembl The Ensembl Genome Browser (includes draft and low coverage genomes) +GOLD:Genomes OnLine Database v 3.0 +SUPERFAMILY comparative genomics database Includes genomes of all completely sequenced eukaryotes, and sophisticated datamining plus visualisation tools for analysis +Rat Genome Database \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-0.md new file mode 100644 index 000000000..3e6ea965b --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-0.md @@ -0,0 +1,190 @@ +--- +title: "List of sequenced fungi genomes" +chunk: 1/2 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:53.310491+00:00" +instance: "kb-cron" +--- + +This list of sequenced fungi genomes contains all the fungal species known to have publicly available complete genome sequences that have been assembled, annotated and published; draft genomes are not included, nor are organelle only sequences. For all kingdoms, see lists of sequenced genomes. + +== Ascomycota == + +=== Dothideomycetes === +Aureobasidium pullulans, A. melanogenum, A. subglaciale and A. namibiae, polyextremotolerant (2014) +Hortaea werneckii, extremely halotolerant (2013 2017) +Leptosphaeria maculans, plant pathogen (2011) + Macrophomina phaseolina, plant pathogen (2012) +Mycosphaerella fijiensis, plant pathogen (2007) +Mycosphaerella graminicola IPO323, wheat pathogen (2008) +Phaeosphaeria nodorum SN15, wheat pathogen (2005) +Pyrenophora tritici-repentis Pt-1C-BFP, wheat pathogen (2007) + +=== Eurotiomycetes === +Ajellomyces capsulata several strains, Darling's disease (2009, unpubl.) +Ajellomyces dermatitidis several strains (2009, unpubl.) +Arthroderma benhamiae CBS 112371, skin infection (2010, unpubl.) +Arthroderma gypseum CBS 118893, athlete's foot (2008) +Arthroderma otae CBS 113480, athlete's foot (2008) +Aspergillus aculeatus ATCC16872, industrial use (2010) +Aspergillus carbonarius ITEM 5010, food pathogen (2009) +Aspergillus clavatus Strain:NRRL1 (2008) +Aspergillus fumigatus Strain:A1163, human pathogen (2008) +Aspergillus fumigatus Strain:Af293, human pathogen (2005) +Aspergillus kawachii IFO 4308, food industry (2011) +Aspergillus nidulans Strain:FGSC A4, model organism (2005) +Aspergillus niger Strain:ATCC 1015 (DOE Joint Genome institute) +Aspergillus niger Strain:CBS 513.88, industrial use (2007) +Aspergillus oryzae Strain:RIB40, industrial use (2005) +Aspergillus terreus NIH 2624, statin producer and pathogen (2005, unpubl.) +Coccidioides immitis, human pathogen, Valley fever (2009) +Coccidioides posadasii C735 delta SOWgp, human pathogen, Valley fever (2009) +Neosartorya fischeri Strain:NRRL181 (2008) +Paracoccidioides brasiliensis, several strains, human pathogen (2007 +Penicillium chrysogenum Strain: Wisconsin54-1255, industrial use (2008) +Penicillium digitatum Strain PHI26 (2012) +Penicillium digitatum Strain Pd1 (2012 +Talaromyces marneffei, human pathogen (2011 +Uncinocarpus reesii (2009) + +=== Leotiomycetes === +Blumeria graminis ffsp hordei Strain:DH14, plant pathogen (2010) +Botrytis cinerea (Botryotinia fuckeliana) Strain:B05.10 and T4, plant pathogen (2011) +Glarea lozoyensis (2012) +Sclerotinia sclerotiorum Strain:1980 (2011) +Ascocoryne sarcoides Strain: NRRL50072 (2012) +Podosphaera macularis Strain: HPM-609, plant pathogen (2023) + +=== Pezizomycetes === +Cladobotryum protrusum (2019) +Tuber melanosporum Mel28, Périgord black truffle (2010) + +=== Saccharomycetes === +Ashbya gossypii Strain:ATCC 10895, plant pathogen (2004) +Candida albicans Strain:SC5314, human pathogen (2004) +Candida albicans Strain:WO-1, human pathogen (2009) +Candida dubliniensis CD36, human pathogen (2009) +Candida glabrata Strain:CBS138, human pathogen (2004) +Candida guilliermondii, human pathogen (2009) +Candida lusitaniae, human pathogen (2009) +Candida parapsilosis, human pathogen (2009) +Candida orthopsilosis, human pathogen (2012) +Candida tropicalis, human pathogen (2009) +Debaryomyces hansenii Strain:CBS767, industrial use (2004) +Debaryomyces hansenii Strain:MTCC 234, salt-tolerant (2012) +Dekkera bruxellensis Strain:CBS2499, wine yeast (2012) +Hansenula polymorpha NCYC 495 leu1.1, industrial use (2010) +Kluyveromyces aestuarii ATCC 18862 (2010, unpubl.) +Kluyveromyces lactis Strain:CLIB210, industrial use (2004) +Kluyveromyces wickerhamii UCD 54-210 (2010, unpubl.) +Lachancea kluyveri (Saccharomyces kluyveri) NRRL Y-12651, plant pathogen (2009) +Lodderomyces elongisporus, human pathogen (2009) +Naumovozyma castellii Strain:AS 2.2404, CBS 4309 (Saccharomyces castellii; 2003, 2011) +Naumovozyma dairenensis Strain:CBS 421 (2011) +Saccharomyces bayanus (2003, 2011) +Saccharomyces arboricolus (2013,) +Saccharomyces cerevisiae Strain:JAY291, industrial/model (2009) +Saccharomyces cerevisiae Strain:S288C, industrial/model (1996) +Saccharomyces cerevisiae Strain:Sigma1278b, industrial/model (2010) +Saccharomyces kudriavzevii (2003) +Saccharomyces mikatae (2003, 2011) +Saccharomyces paradoxus (2003 2009) +Saccharomyces pastorianus Weihenstephan 34/70, industrial, beer (2009) +Scheffersomyces stipitis (Pichia stipitis) CBS 6054, lignin/xylose degrader (2007) +Spathaspora passalidarum NRRL Y-27907, model xylose fermenter (2010) +Tetrapisispora phaffii van der Walt Y 89, CBS 4417 (2011) +Torulaspora delbrueckii Strain:Wallerstein 129, CBS 1146 (2011) +Vanderwaltozyma polyspora DSM 70294 (2007) +Yarrowia lipolytica Strain:CLIB99, industrial use (2004) +Zygosaccharomyces rouxii strain CBS732, food spoiler (2009) + +=== Schizosaccharomycetes === +Schizosaccharomyces japonicus yFS275, model for invasive growth (2006) +Schizosaccharomyces pombe Strain:972h, model eukaryote (2002) + +=== Sordariomycetes === +Colletotrichum graminicola, corn pathogen (2012) +Colletotrichum higginsianum, Arabidopsis thaliana pathogen (2012) +Chaetomium cochliodes Strain:CCM F-232, soil fungus (2016) +Chaetomium globosum Strain:CBS 148.51, soil fungus (2005) +Chaetomium thermophilum Strain:CBS 144.50, soil fungus (2011) +Fusarium oxysporum f. sp. lycopersici 4287, human/plant pathogen (2010) +Gibberella moniliformis 7600, plant pathogen (2010) +Gibberella zeae PH-1, plant pathogen (2008) +Gaeumannomyces graminis tritici R3-111a-1 (2010, unpubl.) +Grosmannia clavigera kw1407, plant pathogen (2011) +Magnaporthe grisea, plant pathogen (20054) +Metarhizium acridum CQMa 102, and +Metarhizium anisopliae ARSEF 23, insect pathogens (2011) +Neurospora crassa, model eukaryote (2003) +Neurospora tetrasperma FGSC 2508 mat A, model (2010) +Nectria haematococca MPVI, plastic/pest./lignin degrader (2009) +Podospora anserina :S mat+ +Sporotrichum thermophile, thermophilic cellulose degrader (2010) +Thielavia terrestris, model thermophile/industrial (2010) +Trichoderma atroviride, industrial/soil, (2010) +Trichoderma reesei QM6a, biomass-degrading (2008) +Trichoderma virens Gv29-8, industrial/pathogen (2007) +Verticillium albo-atrum VaMs.102, plant pathogen (2008, unpubl.) + +== Basidiomycota == + +=== Agaricomycetes === +Agaricus bisporus var. bisporus Strain:H97, Champignon (2009) +Agrocybe aegerita, ack Poplar or Sword-belt Mushroom (2018) ) +Auricularia delicata (2012) +Auricularia heimuer, Chinese Auricularia (2019) +Coniophora puteana (2012) +Coprinopsis cinerea (Coprinus cinereus), model organism for multicellular fungi (2010) +Dichomitus squalens (2012) +Fibroporia radiculosa Strain:TFFH 294 (2012) +Fomitiporia mediterranea (2012) +Fomitopsis pinicola (2012) +Ganoderma leucocontextum strain:GL72 (2023) +Gloeophyllum trabeum (2012) +Hebeloma cylindrosporum http://genome.jgi.doe.gov/Hebcy2/Hebcy2.home.html +Heterobasidion annosum, plant pathogen (2009) +Laccaria bicolor Strain:S238N-H82, mycorrhiza (2008) +Lentinula edodes, Shiitake mushroom (2016) +Moniliophthora perniciosa, Witches' Broom Disease of cacao (2008) +Oudemansiella raphanipes, edible mushroom "Changgengu"(2023) +Phanerochaete chrysosporium Strain:RP78, mycoremediation (2004) +Piriformospora indica endophyte (2011) +Pleurotus ostreatus, industrial/lignin degrader (2010) +Pleurotus tuber-regium, White-rot fungus (2018) +Polyporus umbellatus - a well-known medicinal fungus in Asia +Postia placenta, cellulose degrader (2008) +Punctularia strigosozonata (2012) +Schizophyllum commune, mushroom (2010) +Serpula lacrymans, plant pathogen (2011) +Stereum hirsutum (2012) +Trametes versicolor (2012) +Wolfiporia cocos (2012) + +=== Dacrymycetes === +Dacryopinax spathularia, edible jelly fungus (2024) + +=== Pucciniomycetes (formerly Urediniomycetes) === +Melampsora laricis-populina, pathogen of poplars (2008) +Puccinia graminis f. sp. tritici, plant pathogen (2011) +Puccinia polysora f.sp. zeae - a giga-scale fungal pathogen causing southern corn rust +Puccinia triticina 1-1 BBBD Race 1, pathogen of wheat() +Rhodotorula graminis strain WP1, plant symbiont (2010) +Sporobolomyces roseus, associated with plants () + +=== Tremellomycetes === +Cryptococcus (Filobasidiella) neoformans JEC21, human pathogen (2005, other strains unpubl.) +Dacryopinax sp. (2012) +Tremella mesenterica (2012) + +=== Ustilaginomycetes === +Malassezia globosa CBS 7966, dandruff-associated (2007) +Malassezia restricta CBS 7877, dandruff-associated (2007) +Sporisorium rellianum, plant pathogen (2010) +Ustilago maydis, plant pathogen (2006) + +=== Wallemiomycetes === +Wallemia ichthyophaga, obligate halophile (2013) +Wallemia sebi, xerophile (2012) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-1.md b/data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-1.md new file mode 100644 index 000000000..4266893db --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes-1.md @@ -0,0 +1,135 @@ +--- +title: "List of sequenced fungi genomes" +chunk: 2/2 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_fungi_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:53.310491+00:00" +instance: "kb-cron" +--- + +== Chytridiomycota == +Chytridiomycota includes fungi with spores that have flagella (zoospores) and are a sister group to more advanced land fungi that lack flagella. Several chytrid species are pathogens, but have not had their genomes sequenced yet. + +Batrachochytrium dendrobatidis JEL423, amphibian pathogen (2006) +Batrachochytrium dendrobatidis JAM81, amphibian pathogen (2006) +Spizellomyces punctatus DAOM BR117 (2009) +Gonapodya prolifera JEL478 (Monoblepharidomycetes) (2011) +Chytriomyces sp. MP 71 +Entophlycits helioformis JEL805 +Gaertneriomyces semiglobifer Barr43 +Globomyces pollinis-pini +Rhizoclomsatium globosum + +== Blastocladiomycota == +Allomyces macrogynus ATCC 38327 (Blastocladiomycota) (2009) +Catenaria anguillulae PL171 (Blastocladiomycota) + +== Neocallimastigomycota == +Piromyces sp. E2 (Neocallimastigomycota) (2011) +Anaeromyces sp. S4 +Neocallimastix sp. G1 +Orpinomyces sp. C1A + +== Microsporidia == +Encephalitozoon cuniculi, human pathogen (2001) +Encephalitozoon intestinalis ATCC 50506, human pathogen (2010) +Enterocytozoon bieneusi, human pathogen particularly in the context of HIV infection (~60% of genome 2009, 2010) +Nosema ceranae, honey bee pathogen (2009) +Octosporea bayeri OER 3-3, Daphnia pathogen (2009) + +== Mucoromycota == + +=== Mucoromycotina === +Absidia padenii +Absidia repens +Backusella circina +Circinella umbellata +Cokeromyces recurvatus +Cunninghamella echinulata +Dichotomocladium elegans +Fennellomyces sp. +Gilbertella persicaria var. persicaria +Gongronella butleri +Hesseltinella vesiculosa +Lichtheimia corymbifera +Lichtheimia hyalospora +Mucor circinelloides +Mucor cordense +Mucor indicus +Mucor heterogamus +Mycotypha africana +Parasitella parasitica +Phascolomyces articulosus +Phycomyces blakesleeanus +Phycomyces nitens +Pilaira anomala +Pilobolus umbonatus +Radiomyces spectabilis +Rhizopus delemar +Rhizopus oryzae, human pathogen (mucormycosis) (2009) +Rhizopus microsporus +Saksenaea vasiformis +Spinellus fuiger +Sporodiniella umbellata +Syncephalastrum racemosum +Thamnidium elegans +Umbelopsis isabellina +Umbelopsis ramanniana +Zychaea mexicana + +=== Glomeromycotina === +Rhizophagus irregularis + +=== Mortierellomycotina === +Mortierella alpina Strain: ATCC 32222, commercial source of arachidonic acid (2011) +Lobosporangium transversale +Mortierella elongata +Mortierella humilis +Mortierella multidivaricata +Mortierella verticillata + +== Zoopagomycota == + +=== Kickxellomycotina === +Coemansia reversa +Coemansia spiralis +Kickxella alabastrina +Linderina pennicpora +Martensiomyces pterosporus +Ramicandelaber brevisporus +Smittium culicis +Smittium mucronatum +Zancudomyces culisetae + +=== Entomophthoromycotina === +Basidiobolus meristosporus +Conidiobolus coronatus +Condidiobolus thromboides +Massospora cicadina + +=== Zoopagomycotina === +Syncephalis fuscata +Syncephalis plumigaleata +Syncephalis pseudoplumigaleata +Piptocephalis cylindrospora + +== See also == +Lists of sequenced genomes +List of sequenced bacterial genomes +List of sequenced archaeal genomes +List of sequenced eukaryotic genomes +List of sequenced mitochondrial genomes +List of sequenced plastomes +List of sequenced animal genomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant genomes +List of sequenced plant mitochondrial genomes +List of sequenced protist genomes + +== External links == +Fungal Genome Initiative (includes draft genomes) +UniProt query (complete proteome and fungi) + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_plant_genomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_plant_genomes-0.md new file mode 100644 index 000000000..de3077d20 --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_plant_genomes-0.md @@ -0,0 +1,102 @@ +--- +title: "List of sequenced plant genomes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_plant_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:56.257480+00:00" +instance: "kb-cron" +--- + +This list of sequenced plant genomes contains plant species known to have publicly available complete genome sequences that have been assembled, annotated and published. Unassembled genomes are not included, nor are organelle only sequences. For all kingdoms, see the list of sequenced genomes. For mitochondrial genomes, see list of sequenced plant mitochondrial genomes, For plastid genomes, see list of sequenced plastomes. +See also List of sequenced algae genomes. + + +== Bryophytes == + + +== Vascular plants == + + +=== Lycophytes === + + +=== Ferns === + + +=== Gymnosperms === + + +=== Angiosperms === + + +==== Amborellales ==== + + +==== Chloranthales ==== + + +==== Magnoliids ==== + + +==== Eudicots ==== + + +===== Proteales ===== + + +===== Ranunculales ===== + + +===== Trochodendrales ===== + + +===== Caryophyllales ===== + + +===== Rosids ===== + + +===== Asterids ===== + + +==== Monocots ==== + + +===== Grasses ===== + + +===== Other non-grasses ===== + + +== Press releases announcing sequencing == +Not meeting criteria of the first paragraph of this article in being nearly full sequences with high quality, published, assembled and publicly available. This list includes species where sequences are announced in press releases or websites, but not in a data-rich publication in a refereed peer-review journal with DOI. + +Corchorus olitorius (Jute mallow), fibre plant 2017 +Corchorus capsularis 2017 +Fraxinus excelsior, European ash (2013 draft) + + +== See also == +Lists of sequenced genomes +List of sequenced bacterial genomes +List of sequenced archaeal genomes +List of sequenced eukaryotic genomes +Lists of sequenced mitochondrial genomes +List of sequenced plastomes +List of sequenced animal genomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant mitochondrial genomes +List of sequenced protist genomes + + +== External links == +http://plabipd.de/timeline_view.ep +http://genomevolution.org/wiki/index.php/Sequenced_plant_genomes +https://phytozome.jgi.doe.gov/pz/portal.html +https://bioinformatics.psb.ugent.be/plaza/ + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_plastomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_plastomes-0.md new file mode 100644 index 000000000..7516316ff --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_plastomes-0.md @@ -0,0 +1,91 @@ +--- +title: "List of sequenced plastomes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_plastomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:57.675480+00:00" +instance: "kb-cron" +--- + +A plastome is the genome of a plastid, a type of organelle found in plants and in a variety of protists. The number of known plastid genome sequences grew rapidly in the first decade of the twenty-first century. For example, 25 chloroplast genomes were sequenced for one molecular phylogenetic study. +The flowering plants are especially well represented in complete chloroplast genomes. As of January, 2017, all of their orders are represented except Commelinales, Picramniales, Huerteales, Escalloniales, Bruniales, and Paracryphiales. +A compilation of most complete plastid genomes is maintained by the NCBI in a public repository. + + +== Plants == + + +=== Bryophytes s.l. === + + +=== Ferns and lycophytes === + + +=== Gymnosperms === + + +=== Flowering plants === +This sortable table is expected to compile complete plastid genomes representing the largest range of sizes, number of genes, and angiosperm families. + + +== Green algae == + + +== Red algae == + + +== Glaucophytes == + + +== Meta-algae and apicomplexans == +Meta-algae are organisms with photosynthetic organelles of secondary or tertiary endosymbiotic origin, and their close non-photosynthetic, plastid-bearing, relatives. Apicomplexans are a secondarily non-photosynthetic group of chromalveoates which retain a reduced plastid organelle. + + +=== Photosynthetic chromalveolates === +Dinoflagellate plastid genomes are not organised into a single circular DNA molecule like other plastid genomes, but into an array of mini-circles. + + +=== Chlorarachniophytes === + + +=== Euglenophytes === + + +=== Apicomplexans === + + +== Nucleomorph genomes == +In some photosynthetic organisms, that ability was acquired via symbiosis with a unicellular green alga (chlorophyte) or red alga (rhodophyte). In some such cases, not only does the chloroplast of the former unicellular alga retain its own genome, but a remnant of the alga is also retained. When this retains a nucleus and a nuclear genome, it is termed a nucleomorph. + + +== Cyanelle genomes == +The unicellular eukaryote Paulinella chromatophora possesses an organelle (the cyanelle) which represents an independent case of the acquisition of photosynthesis by cyanobacterial endosymbiosis. (Note: the term "cyanelle" is also applied to the plastids of glaucophytes.) + + +== See also == +Genome skimming +Lists of sequenced genomes +List of sequenced bacterial genomes +List of sequenced archaeal genomes +List of sequenced eukaryotic genomes +List of sequenced mitochondrial genomes +List of sequenced animal genomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant genomes +List of sequenced plant mitochondrial genomes +List of sequenced protist genomes + + +== References == + + +== External links == +HAMAP proteomes: Plastids +Complete Plastid Genomes +Chloroplast Genome Database +NCBI Eukaryotic Plastid Genomes +chloroplast genome list Archived 2012-04-20 at the Wayback Machine In: Montreal genomics Archived 2012-04-20 at the Wayback Machine +Psilotum nudum \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/List_of_sequenced_protist_genomes-0.md b/data/en.wikipedia.org/wiki/List_of_sequenced_protist_genomes-0.md new file mode 100644 index 000000000..e27255d9f --- /dev/null +++ b/data/en.wikipedia.org/wiki/List_of_sequenced_protist_genomes-0.md @@ -0,0 +1,50 @@ +--- +title: "List of sequenced protist genomes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/List_of_sequenced_protist_genomes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:59.051434+00:00" +instance: "kb-cron" +--- + +This list of sequenced protist genomes contains all the protist species known to have publicly available complete genome sequences that have been assembled, annotated and published; draft genomes are not included, nor are organelle only sequences. + + +== Alveolata == +Alveolata are a group of protists which includes the Ciliophora, Apicomplexa and Dinoflagellata. Members of this group are of particular interest to science as the cause of serious human and livestock diseases. + + +== Amoebozoa == +Amoebozoa are a group of motile amoeboid protists, members of this group move or feed by means of temporary projections, called pseudopods. The best known member of this group is the slime mold, which has been studied for centuries; other members include the Archamoebae, Tubulinea and Flabellinia. Some Amoeboza cause disease. + + +== Chromista == +The Chromista are a group of protists that contains the algal phyla Heterokontophyta (stramenopiles), Haptophyta and Cryptophyta. Members of this group are mostly studied for evolutionary interest. + + +== Excavata == +Excavata is a group of related free living and symbiotic protists; it includes the Metamonada, Loukozoa, Euglenozoa and Percolozoa. They are researched for their role in human disease. + + +== Opisthokonts, basal == +Opisthokonts are a group of eukaryotes that include both animals and fungi as well as basal groups that are not classified in these groups. These basal opisthokonts are reasonably categorized as protists and include choanoflagellates, which are the sister or near-sister group of animals. + + +== See also == +Lists of sequenced genomes +List of sequenced bacterial genomes +List of sequenced archaeal genomes +List of sequenced eukaryotic genomes +Lists of sequenced mitochondrial genomes +List of sequenced plastomes +List of sequenced animal genomes +List of sequenced animal mitochondrial genomes +List of sequenced fungi genomes +List of sequenced fungi mitochondrial genomes +List of sequenced plant genomes +List of sequenced plant mitochondrial genomes +List of sequenced algae genomes + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Lists_of_human_genes-0.md b/data/en.wikipedia.org/wiki/Lists_of_human_genes-0.md new file mode 100644 index 000000000..2f6aa1ecb --- /dev/null +++ b/data/en.wikipedia.org/wiki/Lists_of_human_genes-0.md @@ -0,0 +1,38 @@ +--- +title: "Lists of human genes" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/Lists_of_human_genes" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:34.120829+00:00" +instance: "kb-cron" +--- + +Lists of human genes are as follows: + + +== By chromosome == +Human chromosomes, each of which contains an incomplete list of genes located on that chromosome, are as follows: + + +== Protein-coding genes == +The lists below constitute a complete list of all known human protein-coding genes: + + +== Transcription factors == +1639 genes which encode proteins that are known or expected to function as human transcription factors: + +List of human transcription factors + + +== See also == +List of enzymes +List of proteins +List of disabled human pseudogenes + + +== External links == +iHOP-Protein Information Database +NextBio-Life Science Search Engine +Entrez-Cross Database Query Search System +TranscriptomeBrowser \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Lists_of_mammals_by_population-0.md b/data/en.wikipedia.org/wiki/Lists_of_mammals_by_population-0.md new file mode 100644 index 000000000..5a386447a --- /dev/null +++ b/data/en.wikipedia.org/wiki/Lists_of_mammals_by_population-0.md @@ -0,0 +1,75 @@ +--- +title: "Lists of mammals by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/Lists_of_mammals_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:18.572951+00:00" +instance: "kb-cron" +--- + +This is a collection of lists of mammal species by the estimated global population, divided by orders. Lists only exist for some orders; for example, the most diverse order - rodents - is missing. Much of the data in these lists were created by the International Union for Conservation of Nature (IUCN) Global Mammal Assessment Team, which consists of 1700 mammalogists from over 130 countries. They recognize 5488 species in the class. +These lists are not comprehensive, as not all mammals have had their numbers estimated. For example, a live specimen of the spade-toothed whale was first observed in December 2010, and the event only recognized as such in November 2012; no estimate yet exists for the global population. The accuracy of the quote numbers may only be an order of magnitude. +It is estimated that the total number of wild mammals in the world is about 130 billion. + + +== Lists by taxonomic order == +Monotremata + +List of monotremes by population – platypus, echidnas +Marsupialia (infraclass containing 7 extant orders) + +List of marsupials by population – shrew opossums, opossums, marsupial moles, bandicoots, dasyurids, diprodonts (kangaroos, wallabies, wombats, koalas). +Xenarthra (superorder containing 2 extant orders) + +List of xenarthrans by population – anteaters, tree sloths, armadillos. +Afrotheria (superorder containing 6 extant orders) + +Proboscidea +List of elephant species by population – elephants. +Hyracoidea, Sirenia, Tubulidentata, Macroscelidea, Afrosoricida +List of non-proboscid afrotheres by population – hyraxes, sea cows, aardvarks, elephant shrews, golden moles, otter shrews, tenrecs +Eulipotyphla + +List of eulipotyphlans by population – hedgehogs, shrews, moles, solenodons +Chiroptera + +List of bats by population – bats. +Pholidota + +List of pangolin species by population – pangolins +Carnivora + +List of carnivorans by population – cats, viverrids, hyenas, mongoose, canines, procyonids, bears, mustelids, skunks, and pinnipeds. +Perissodactyla + +List of odd-toed ungulates by population – equines, rhinoceroses, tapirs. +Artiodactyla + +List of even-toed ungulates by population – swine, hippopotamus, giraffes, chevrotains, cervids, bovids. +List of cetacean species with population estimates – dolphins, porpoises, whales. +Scandentia + +List of tree shrews by population – tree shrews. +Lagomorpha + +List of lagomorphs by population – rabbits, hares, pikas. +Rodentia + +List of rodents by population – beavers, squirrels, mice, rats, etc. +Dermoptera + +List of colugos by population – colugos. +Primates + +List of primates by population – lemurs, lorises, tarsiers, monkeys, apes. + + +== See also == + +List of birds by population +Lists of organisms by population +World population (humans) + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Lists_of_organisms_by_population-0.md b/data/en.wikipedia.org/wiki/Lists_of_organisms_by_population-0.md new file mode 100644 index 000000000..b89ba117f --- /dev/null +++ b/data/en.wikipedia.org/wiki/Lists_of_organisms_by_population-0.md @@ -0,0 +1,95 @@ +--- +title: "Lists of organisms by population" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/Lists_of_organisms_by_population" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:34.046405+00:00" +instance: "kb-cron" +--- + +This is a collection of lists of organisms by their population. While most of the numbers are estimates, they have been made by the experts in their fields. Wildlife population measurement is a science falling under the purview of population ecology and biogeography. Individuals are counted by census, as carried out for the piping plover; using the transect method, as done for the mountain plover; and beginning in 2012 by satellite, with the emperor penguin being first subject counted in this manner. + + +== Number of species == +More than 99 percent of all species, amounting to over five billion species, that ever lived on Earth are estimated to be extinct. Estimates on the number of Earth's current species range from 10 million to 14 million, of which about 1.2 million have been documented and over 86 percent have not yet been described. According to another study, the number of described species has been estimated at 1,899,587. 2000–2009 saw approximately 17,000 species described per year. The total number of undescribed organisms is unknown, but marine microbial species alone could number 20,000,000. For this reason, the number of quantified species will always lag behind the number of described species, and species contained in these lists tend to be on the K side of the r/K selection continuum. More recently, in May 2016, scientists reported that 1 trillion species are estimated to be on Earth currently with only one-thousandth of one percent described. The total number of related DNA base pairs on Earth is estimated at 5.0 × 1037 and weighs 50 billion tonnes. In comparison, the total mass of the biosphere has been estimated to be as much as 4 TtC (trillion [million million] tonnes of carbon). In July 2016, scientists reported identifying a set of 355 genes from the Last universal common ancestor (LUCA) of all organisms living on Earth. + + +== By domain == +The domain of eukaryotes represent a small minority of the number of organisms; however, due to their generally much larger size, their collective global biomass is estimated to be about equal to that of prokaryotes. Prokaryotes number about 4–6 × 1030 cells and 350–550 Pg of C. + + +== Microbes == +It is estimated that the most numerous bacteria are of a species of the Pelagibacterales (or SAR11) clade, perhaps Pelagibacter ubique, and the most numerous viruses are bacteriophages infecting these species. It is estimated that the oceans contain about 2.4 × 1028 (24 octillion) SAR11 cells. +The Deep Carbon Observatory has been exploring living forms in the interior of the Earth. "Life in deep Earth totals 15 to 23 billion tons of carbon". + + +== Animalia == + + +=== Vertebrates === + + +==== Mammals (Mammalia) ==== + +Mammals by population +Artiodactyla (even-toed ungulates) +Carnivora (carnivorans) +Cetacea (cetaceans) +Chiroptera (bats) +Perissodactyla (odd-toed ungulates) +Primates (primates) +Proboscidea (elephants) +Marsupialia (marsupials) + + +==== Birds (Aves) ==== +Birds by population +Anseriformes (waterfowl) +Apodiformes (swifts and hummingbirds) +Caprimulgiformes (nightjars and relatives) +Charadriiformes (gulls and relatives) +Ciconiiformes (storks and relatives) +Columbiformes (doves and pigeons) +Coraciiformes (kingfishers and relatives) +Cuculiformes (cuckoos and relatives) +Falconiformes (falcons and relatives) +Galliformes (gamebirds) +The domesticated chicken (Gallus gallus domesticus), a Galliform, has an estimated population of 23.7 billion, which is higher than any other bird. +Gaviiformes (loons or divers) +Gruiformes (cranes and relatives) +Passeriformes (perching birds) +Pelecaniformes (pelicans and relatives) +Phoenicopteriformes (flamingos) +Piciformes (woodpeckers and relatives) +Podicipediformes (grebes) +Procellariiformes (albatrosses and petrels) +Psittaciformes (parrots) +Sphenisciformes (penguins) +Strigiformes (owls) +Struthioniformes (ratites) +Tinamiformes (tinamous) +Trogoniformes (trogons and quetzals) + + +==== Reptiles (Reptilia) ==== + + +=== Hexapoda === + + +==== Insects (Insecta) ==== +Recent figures indicate that there are more than 1.4 billion insects for each human on the planet, or roughly 1019 (10 quintillion) individual living insects on the earth at any given time. An article in The New York Times claimed that the world holds 300 pounds of insects for every pound of humans. Ants have colonised almost every landmass on Earth. Their population is estimated as between 1016–1017 (10-100 quadrillion). With an estimated 20 quadrillion ants their biomass comes to 12 megatons of dry carbon, which is more than all wild birds and non-human mammals combined. + + +== Plantae == + + +=== Trees === +According to NASA in 2005, there were over 400 billion trees on Earth. However, more recently, in 2015, using better methods, the global tree count has been estimated at 3 trillion. Other studies show that the Amazonian forest alone yields approximately 430 billion trees. Extrapolations from data compiled over a period of 10 years suggest that greater Amazonia, which includes the Amazon Basin and the Guiana Shield, harbors around 390 billion individual trees. + + +== See also == + + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Lists_of_sequenced_genomes-0.md b/data/en.wikipedia.org/wiki/Lists_of_sequenced_genomes-0.md index 57b9f0945..4834d129a 100644 --- a/data/en.wikipedia.org/wiki/Lists_of_sequenced_genomes-0.md +++ b/data/en.wikipedia.org/wiki/Lists_of_sequenced_genomes-0.md @@ -4,7 +4,7 @@ chunk: 1/1 source: "https://en.wikipedia.org/wiki/Lists_of_sequenced_genomes" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T07:51:47.429056+00:00" +date_saved: "2026-05-05T07:57:54.563940+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/Outline_of_ants-0.md b/data/en.wikipedia.org/wiki/Outline_of_ants-0.md new file mode 100644 index 000000000..20bcf28ed --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_ants-0.md @@ -0,0 +1,85 @@ +--- +title: "Outline of ants" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/Outline_of_ants" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:26.219128+00:00" +instance: "kb-cron" +--- + +The following outline is provided as an overview of and topical guide to ants: +Ants – social insects with geniculate (elbowed) antennae and a distinctive node-like structure that forms a slender waist. Ants are of the family Formicidae and evolved from wasp-like ancestors in the mid-Cretaceous period between 110 and 130 million years ago, diversifying after the rise of flowering plants. More than 12,500 out of an estimated total of 22,000 species have been classified. + + +== Essence of ants == +Ant colony +Myrmecology – scientific study of ants + + +=== Biological classification === + +Kingdom: Animalia +Phylum: Arthropoda +Class: Insecta +Order: Hymenoptera +Suborder: Apocrita +Superfamily: Vespoidea +Family: Formicidae (family authority: Latreille, 1809) + + +== Kinds of ants == +Ant + +List of ant genera +List of ants of Great Britain + + +=== Subfamilies === +Extant subfamilies +Agroecomyrmecinae +Amblyoponinae +Aneuretinae +Dolichoderinae +Dorylinae +Ectatomminae +Formicinae +Heteroponerinae +Leptanillinae +Martialinae +Myrmeciinae +Myrmicinae +Paraponerinae +Ponerinae +Proceratiinae +Pseudomyrmecinae +Fossil subfamilies +†Armaniinae (sometimes treated as the family Armaniidae within the superfamily Formicoidea) +†Brownimeciinae +†Formiciinae +†Sphecomyrminae + + +== General myrmecology concepts == +Ant colony optimization algorithms +Ant mill + + +== Myrmecologists == + +Murray S. Blum (1929–2015) +Barry Bolton +Horace Donisthorpe (1870–1951) +Auguste Forel (1848–1931) +William Gould (1715–1799) +Bert Hölldobler (born 1936) +Thomas C. Jerdon (1811–1872) +Sir John Lubbock (1st Lord and Baron Avebury) (1834–1913) +Derek Wragge Morley (1920–1969) +Frederick Smith (1805–1879) +John Obadiah Westwood (1805–1893) +William Morton Wheeler (1865–1937) +E.O. Wilson (1929–2021) + + +== External links == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_biochemistry-0.md b/data/en.wikipedia.org/wiki/Outline_of_biochemistry-0.md index bdda32e80..bfd585cdc 100644 --- a/data/en.wikipedia.org/wiki/Outline_of_biochemistry-0.md +++ b/data/en.wikipedia.org/wiki/Outline_of_biochemistry-0.md @@ -4,7 +4,7 @@ chunk: 1/1 source: "https://en.wikipedia.org/wiki/Outline_of_biochemistry" category: "reference" tags: "science, encyclopedia" -date_saved: "2026-05-05T06:14:36.329988+00:00" +date_saved: "2026-05-05T07:54:59.503336+00:00" instance: "kb-cron" --- diff --git a/data/en.wikipedia.org/wiki/Outline_of_biology-0.md b/data/en.wikipedia.org/wiki/Outline_of_biology-0.md new file mode 100644 index 000000000..536476a7a --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_biology-0.md @@ -0,0 +1,131 @@ +--- +title: "Outline of biology" +chunk: 1/4 +source: "https://en.wikipedia.org/wiki/Outline_of_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:00.731791+00:00" +instance: "kb-cron" +--- + +The following outline is provided as an overview of and topical guide to biology: +Biology – The natural science that studies life. Areas of focus include structure, function, growth, origin, evolution, distribution, and taxonomy. + +== History of biology == + +History of anatomy +History of biochemistry +History of biotechnology +History of botany +History of ecology +History of genetics +History of evolutionary thought: +Darwinism +Eclipse of Darwinism (Lamarckism, Orthogenesis, Structuralism, and Mutationism) +Modern (evolutionary) synthesis +History of molecular evolution +History of speciation +History of marine biology +History of medicine +History of model organisms +History of molecular biology +Natural history +History of neuroscience +History of plant systematics +History of pathology +History of virology +History of zoology + +== Overview == +Biology +Science +Life +Properties: Adaptation – Energy processing – Growth – Order – Regulation – Reproduction – Response to environment +Biological organization: atom – molecule – cell – tissue – organ – organ system – organism – population – community – ecosystem – biosphere +Approach: Reductionism – emergent property – mechanistic +Biology as a science: +Natural science +Scientific method: observation – research question – hypothesis – testability – prediction – experiment – data – statistics +Scientific theory – scientific law +Research method +List of research methods in biology +Scientific literature +List of biology journals: peer review + +== Chemical basis == +Outline of biochemistry + +Atoms and molecules +matter – element – atom – proton – neutron – electron– Bohr model – isotope – chemical bond – ionic bond – ions – covalent bond – hydrogen bond – molecule +Water: +properties of water – solvent – cohesion – adhesion – surface tension – pH +Organic compounds: +carbon – carbon-carbon bonds – hydrocarbon – monosaccharide – amino acids – nucleotide – functional group – monomer – adenosine triphosphate (ATP) – lipids – oil – sugar – vitamins – neurotransmitter – wax +Macromolecules: +polysaccharide: cellulose – carbohydrate – chitin – glycogen – starch +proteins: primary structure – secondary structure – tertiary structure – conformation – native state – protein folding – enzyme – receptor – transmembrane receptor – ion channel – membrane transporter – collagen – pigments: chlorophyll – carotenoid – xanthophyll – melanin – prion +lipids: cell membrane – fats – phospholipids +nucleic acids: DNA – RNA + +== Cells == +Outline of cell biology + +Cell structure: +Cell coined by Robert Hooke +Techniques: cell culture – flow cytometry – microscope – light microscope – electron microscopy – SEM – TEM – live cell imaging +Organelles: Cytoplasm – Vacuole – Peroxisome – Plastid +Cell nucleus +Nucleoplasm – Nucleolus – Chromatin – Chromosome +Endomembrane system +Nuclear envelope – Endoplasmic reticulum – Golgi apparatus – Vesicles – Lysosome +Energy creators: Mitochondrion and Chloroplast +Biological membranes: +Plasma membrane – Mitochondrial membrane – Chloroplast membrane +Other subcellular features: Cell wall – pseudopod – cytoskeleton – mitotic spindle – flagellum – cilium +Cell transport: Diffusion – Osmosis – isotonic – active transport – phagocytosis +Cellular reproduction: cytokinesis – centromere – meiosis +Nuclear reproduction: mitosis – interphase – prophase – metaphase – anaphase – telophase +programmed cell death – apoptosis – cell senescence +Metabolism: +enzyme - activation energy - proteolysis – cooperativity +Cellular respiration +Glycolysis – Pyruvate dehydrogenase complex – Citric acid cycle – electron transport chain – fermentation +Photosynthesis +light-dependent reactions – Calvin cycle +Cell cycle +mitosis – chromosome – haploid – diploid – polyploidy – prophase – metaphase – anaphase – telophase – cytokinesis – meiosis + +== Genetics == +Outline of Genetics + +Inheritance +heredity – Mendelian inheritance – gene – locus – trait – allele – polymorphism – homozygote – heterozygote – hybrid – hybridization – dihybrid cross – Punnett square – inbreeding +genotype–phenotype distinction – genotype – phenotype – dominant gene – recessive gene +genetic interactions – Mendel's law of segregation – genetic mosaic – maternal effect – penetrance – complementation – suppression – epistasis – genetic linkage +Model organisms: Drosophila – Arabidopsis – Caenorhabditis elegans – mouse – Saccharomyces cerevisiae – Escherichia coli – Lambda phage – Xenopus – chicken – zebrafish – Ciona intestinalis – amphioxus +Techniques: genetic screen – linkage map – genetic map +DNA +Nucleic acid double helix +Nucleobase: adenine (A) – cytosine (C) – guanine (G) – thymine (T) – uracil (U) +DNA replication – mutation – mutation rate – proofreading – DNA mismatch repair – point mutation – crossover – recombination – plasmid – transposon +Gene expression +Central dogma of molecular biology: nucleosome – genetic code – codon – transcription factor – transcription – translation – RNA – histone – telomere +heterochromatin – promoter – RNA polymerase +Protein biosynthesis – ribosomes +Gene regulation +operon – activator – repressor – corepressor – enhancer – alternative splicing +Genomes +DNA sequencing – high throughput sequencing – bioinformatics +Proteome – proteomics – metabolome – metabolomics +DNA paternity testing +Biotechnology (see also Outline of biochemical techniques and Molecular biology): +DNA fingerprinting – genetic fingerprint – microsatellite – gene knockout – imprinting – RNA interference Genomics – computational biology – bioinformatics – gel electrophoresis – transformation – PCR – PCR mutagenesis – primer – chromosome walking – RFLP – restriction enzyme – sequencing – shotgun sequencing – cloning – culture – DNA microarray – electrophoresis – protein tag – affinity chromatography – x-ray diffraction – proteomics – mass spectrometry – CRISPR – gene therapy +Genes, development, and evolution +Apoptosis +French flag model +Pattern formation +Evo-devo gene toolkit +Transcription factor + +== Evolution == +Outline of evolution (see also evolutionary biology) \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_biology-1.md b/data/en.wikipedia.org/wiki/Outline_of_biology-1.md new file mode 100644 index 000000000..ed8406ca3 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_biology-1.md @@ -0,0 +1,158 @@ +--- +title: "Outline of biology" +chunk: 2/4 +source: "https://en.wikipedia.org/wiki/Outline_of_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:00.731791+00:00" +instance: "kb-cron" +--- + +Evolutionary processes +evolution +microevolution: adaptation – selection – natural selection – directional selection – sexual selection – genetic drift – sexual reproduction – asexual reproduction – colony – allele frequency – neutral theory of molecular evolution – population genetics – Hardy–Weinberg principle +Speciation +Species +Phylogeny +Lineage (evolution) – evolutionary tree – cladistics – species – taxon – clade – monophyletic – polyphyly – paraphyly – heredity – phenotypic trait – nucleic acid sequence – synapomorphy – homology – molecular clock – outgroup (cladistics) – maximum parsimony (phylogenetics) – Computational phylogenetics +Linnaean taxonomy: Carl Linnaeus – domain (biology) – kingdom (biology) – phylum – class (biology) – order (biology) – family (biology) – genus – species +Three-domain system: archaea – bacteria – eukaryote – protist – fungi – plant – animal +Binomial nomenclature: scientific classification – Homo sapiens +History of life +Origin of life – hierarchy of life – Miller–Urey experiment +Macroevolution: adaptive radiation – convergent evolution – extinction – mass extinction – fossil – taphonomy – geologic time – plate tectonics – continental drift – vicariance – Gondwana – Pangaea – endosymbiosis + +== Life == + +Bacteria and Archaea +Protists +Plant diversity +Green algae +Chlorophyta +Charophyta +Bryophytes +Marchantiophyta +Anthocerotophyta +Moss +Pteridophytes +Lycopodiophyta +Polypodiophyta +Seed plants +Cycadophyta +Ginkgophyta +Pinophyta +Gnetophyta +Magnoliophyta +Fungi +Yeast – mold (fungus) – mushroom +Animal diversity +Invertebrates: +sponge – cnidarian – coral – jellyfish – Hydra (genus) – sea anemone +flatworms – nematodes +arthropods: crustacean – chelicerata – myriapoda – arachnids – insects – annelids – molluscs +Vertebrates: +fishes: – agnatha – chondrichthyes – osteichthyes +Tiktaalik +tetrapods +amphibians +reptiles +birds +flightless birds – Neognathae – dinosaurs +mammals +placental: primates +marsupial +monotreme +Viruses +DNA viruses – RNA viruses – retroviruses + +== Plant form and function == + +Plant body +Organ systems: root – shoot – stem – leaf – flower +Plant nutrition and transport +Vascular tissue – bark (botany) – Casparian strip – turgor pressure – xylem – phloem – transpiration – wood – trunk (botany) +Plant development +tropism – taxis +seed – cotyledon – meristem – apical meristem – vascular cambium – cork cambium +alternation of generations – gametophyte – antheridium – archegonium – sporophyte – spore – sporangium +Plant reproduction +angiosperms – flower – reproduction – sperm – pollination – self-pollination – cross-pollination – nectar – pollen +Plant responses +Plant hormone – ripening – fruit – Ethylene as a plant hormone – toxin – pollinator – phototropism – skototropism – phototropin – phytochrome – auxin – photoperiodism – gravity + +== Animal form and function == + +General features: morphology (biology) – anatomy – physiology – biological tissues – organ (biology) – organ systems +Water and salt balance +Body fluids: osmotic pressure – ionic composition – volume +Diffusion – osmosis) – Tonicity – sodium – potassium – calcium – chloride +Excretion +Nutrition and digestion +Digestive system: stomach – intestine – liver – nutrition – primary nutritional groups metabolism – kidney – excretion +Breathing +Respiratory system: lungs +Circulation +Circulatory system: heart – artery – vein – capillary – Blood – blood cell +Lymphatic system: lymph node +Muscle and movement +Skeletal system: bone – cartilage – joint – tendon +Muscular system: muscle – actin – myosin – reflex +Nervous system +Neuron – dendrite – axon – nerve – electrochemical gradient – electrophysiology – action potential – signal transduction – synapse – receptor – +Central nervous system: brain – spinal cord +limbic system – memory – vestibular system +Peripheral nervous system +Sensory nervous system: eye – vision – audition – proprioception – olfaction – +Integumentary system: skin cell +Hormonal control +Endocrine system: hormone + +Animal reproduction +Reproductive system: testes – ovary – pregnancy +Fish#Reproductive system +Mammalian reproductive system +Human reproductive system +Mammalian penis +Os penis +Penile spines +Genitalia of bottlenose dolphins +Genitalia of marsupials +Equine reproductive system +Even-toed ungulate#Genitourinary system +Bull#Reproductive anatomy +Carnivora#Reproductive system +Fossa (animal)#External genitalia +Female genitalia of spotted hyenas +Cat anatomy#Genitalia +Genitalia of dogs +Canine penis +Bulbus glandis +Animal development +stem cell – blastula – gastrula – egg (biology) – fetus – placenta - gamete – spermatid – ovum – zygote – embryo – cellular differentiation – morphogenesis – homeobox +Immune system +antibody – host – vaccine – immune cell – AIDS – T cell – leucocyte +Animal behavior +Behavior: mating – animal communication – seek shelter – migration (ecology) +Fixed action pattern +Altruism (biology) + +== Ecology == +Outline of ecology + +Ecosystems: +Ecology – Biodiversity – habitat – plankton – thermocline – saprobe +Abiotic component: water – light – radiation – temperature – humidity – atmosphere – acidity +Microbe – biomass – organic matter – decomposer – decomposition – carbon – nutrient cycling – solar energy – topography – tilt – Windward and leeward – precipitation Temperature – biome +Populations +Population ecology: organism – geographical area – sexual reproduction – population density – population growth – birth rate – death Rate – immigration rate – exponential growth – carrying capacity – logistic function – natural environment – competition (biology) – mating – biological dispersal – endemic (ecology) – growth curve (biology) – habitat – drinking water – resource – human population – technology – Green revolution +Communities +Community (ecology) – ecological niche – keystone species – mimicry – symbiosis – pollination – mutualism – commensalism – parasitism – predation – invasive species – environmental heterogeneity – edge effect +Consumer–resource interactions: food chain – food web – autotroph – heterotrophs – herbivore – carnivore – trophic level +Biosphere +lithosphere – atmosphere – hydrosphere +biogeochemical cycle: nitrogen cycle – carbon cycle – water cycle +Climate change: Fossil fuel – coal – oil – natural gas – World energy consumption – Climate change feedback – Albedo – water vapor Carbon sink +Conservation +Biodiversity – habitats – Ecosystem services – biodiversity loss – extinction – Sustainability – Holocene extinction – bioremediation + +== Branches == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_biology-2.md b/data/en.wikipedia.org/wiki/Outline_of_biology-2.md new file mode 100644 index 000000000..6aae8a0c2 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_biology-2.md @@ -0,0 +1,34 @@ +--- +title: "Outline of biology" +chunk: 3/4 +source: "https://en.wikipedia.org/wiki/Outline_of_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:00.731791+00:00" +instance: "kb-cron" +--- + +Anatomy – study of form in animals, plants and other organisms, or specifically in humans. Simply, the study of internal structure of living organisms. Physiology – study of the internal workings of organisms and the functions of anatomical structures. Comparative anatomy – the study of evolution of species through similarities and differences in their anatomy. Gross anatomy – study of anatomy at the macroscopic level +Histology – also known as microscopic anatomy or microanatomy, the branch of biology which studies the microscopic anatomy of biological tissues. Neuroanatomy – the study of the nervous system. Osteology – study of bones. Radiographic anatomy – study of anatomy through radiography +Surface anatomy – study of external features of a body +Biochemistry – study of the chemical reactions required for life to exist and function, usually a focus on the cellular level. Biophysics – study of biological processes through the methods traditionally used in the physical sciences. Biomechanics – the study of the mechanics of living beings. Cellular biophysics – study of physical principles underlying cell function +Neurophysics – study of the development of the nervous system on a molecular level. Molecular biophysics – study of physical properties of biomolecules at the molecular level +Quantum biology – application of quantum mechanics and theoretical chemistry to biological objects and problems. Virophysics – study of mechanics and dynamics driving the interactions between virus and cells. Biotechnology – new and sometimes controversial branch of biology that studies the manipulation of living matter, including genetic modification and synthetic biology. Bioinformatics – use of information technology for the study, collection, and storage of genomic and other biological data. Bioengineering – study of biology through the means of engineering with an emphasis on applied knowledge and especially related to biotechnology. Synthetic biology – research integrating biology and engineering; construction of biological functions not found in nature. Botany – study of plants. Economic botany – study of relationship between people and plants, including the practical uses of plants +Ethnobotany – study of a region's plants and their usage by people +Photobiology – scientific study of the interactions of light (technically, non-ionizing radiation) and living organisms. The field includes the study of photosynthesis, photomorphogenesis, visual processing, circadian rhythms, bioluminescence, and ultraviolet radiation effects. Phycology – scientific study of algae. Plant anatomy – study of internal structure of plants +Plant ecology – study of how plants interact with each other and their environment +Plant genetics – study of heredity and variation in plants +Plant pathology – study of plant diseases +Plant physiology – subdiscipline of botany concerned with the functioning, or physiology, of plants. Cell biology – study of the cell as a complete unit, and the molecular and chemical interactions that occur within a living cell. Histology – study of the anatomy of cells and tissues of plants and animals using microscopy. Chronobiology – field of biology that examines periodic (cyclic) phenomena in living organisms and their adaptation to solar- and lunar-related rhythms. Dendrochronology – study of tree rings, using them to date the exact year they were formed in order to analyze atmospheric conditions during different periods in natural history. Developmental biology – study of the processes through which an organism forms, from zygote to full structure +Embryology – study of the development of embryo (from fecundation to birth). Gerontology – study of aging processes. Ecology – study of the interactions of living organisms with one another and with the non-living elements of their environment. Behavioral ecology – the study of the evolutionary basis for animal behavior due to ecological pressure +Ecosystem ecology – study of biotic and abiotic components of ecosystems and their interactions within an ecosystem +Landscape ecology – study of relationships between ecological processes in the environment and particular ecosystems +Microbial ecology – study of the relationships between microorganisms and their environments +Population ecology – study of dynamics of species populations and how these populations interact with the environment +Urban ecology – study of the relationships between living organisms with each other and their urban environment. Biogeography – study of the distribution of species spatially and temporally. Evolutionary biology – study of the origin and descent of species over time. Evolutionary developmental biology – field of biology that compares the developmental processes of different organisms to determine the ancestral relationship between them, and to discover how developmental processes evolved. Paleobiology – discipline which combines the methods and findings of the life sciences with the methods and findings of the earth science, paleontology. Paleoanthropology – the study of fossil evidence for human evolution, mainly using remains from extinct hominin and other primate species to determine the morphological and behavioral changes in the human lineage, as well as the environment in which human evolution occurred. Paleobotany – study of fossil plants. Paleontology – study of fossils and sometimes geographic evidence of prehistoric life. Paleopathology – the study of pathogenic conditions observable in bones or mummified soft tissue, and on nutritional disorders, variation in stature or morphology of bones over time, evidence of physical trauma, or evidence of occupationally derived biomechanic stress. Genetics – study of genes and heredity. Molecular genetics – study of the bimolecular mechanisms behind the structure and function of DNA +Quantitative genetics – study of phenotypes that vary continuously (in characters such as height or mass)—as opposed to discretely identifiable phenotypes and gene-products (such as eye-colour, or the presence of a particular biochemical). Marine biology – study of ocean ecosystems, plants, animals, and other living beings. Microbiology – study of microscopic organisms (microorganisms) and their interactions with other living things. Bacteriology – study of bacteria +Immunology – study of immune systems in all organisms. Mycology – study of fungi +Parasitology – study of parasites and parasitism. Virology – study of viruses +Biochemistry +Molecular biology – study of biology and biological functions at the molecular level, with some cross over from biochemistry. Structural biology – a branch of molecular biology, biochemistry, and biophysics concerned with the molecular structure of biological macromolecules. Health sciences and human biology – biology of humans. Medicine – Diagnosis, treatment, and prevention of illness. Endocrinology – study of the endocrine system. Oncology – study of cancer processes, including virus or mutation, oncogenesis, angiogenesis, and tissues remoldings. Pharmacology – study of medication and drugs +Epidemiology – major component of public health research, studying factors affecting the health of populations. Neuroscience – study of the nervous system, including anatomy, physiology and emergent proprieties. Behavioral neuroscience – study of physiological, genetic, and developmental mechanisms of behavior in humans and other animals. Cellular neuroscience – study of neurons at a cellular level. Cognitive neuroscience – study of biological substrates underlying cognition, with a focus on the neural substrates of mental processes. Computational neuroscience – study of the information processing functions of the nervous system, and the use of digital computers to study the nervous system. Developmental neuroscience – study of the cellular basis of brain development and addresses the underlying mechanisms. Molecular neuroscience – studies the biology of the nervous system with molecular biology, molecular genetics, protein chemistry and related methodologies. Neuroanatomy – study of the anatomy of nervous tissue and neural structures of the nervous system. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_biology-3.md b/data/en.wikipedia.org/wiki/Outline_of_biology-3.md new file mode 100644 index 000000000..bc670946b --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_biology-3.md @@ -0,0 +1,60 @@ +--- +title: "Outline of biology" +chunk: 4/4 +source: "https://en.wikipedia.org/wiki/Outline_of_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:55:00.731791+00:00" +instance: "kb-cron" +--- + +Neuroendocrinology – studies the interaction between the nervous system and the endocrine system, that is how the brain regulates the hormonal activity in the body. Neuroethology – study of animal behavior and its underlying mechanistic control by the nervous system. Neuroimmunology – study of the nervous system, and immunology, the study of the immune system. Neuropharmacology – study of how drugs affect cellular function in the nervous system. Neurophysiology – study of the function (as opposed to structure) of the nervous system. Systems neuroscience – studies the function of neural circuits and systems. Theoretical biology – the mathematical modeling of biological phenomena. Systems biology – computational modeling of biological systems. Zoology – study of animals, including classification, physiology, development, and behavior. Subbranches include: +Arthropodology – biological discipline concerned with the study of arthropods, a phylum of animals that include the insects, arachnids, crustaceans and others that are characterized by the possession of jointed limbs. Acarology – study of the taxon of arachnids that contains mites and ticks. Arachnology – scientific study of spiders and related animals such as scorpions, pseudoscorpions, harvestmen, collectively called arachnids. Entomology – study of insects. Coleopterology – study of beetles. Lepidopterology – study of a large order of insects that includes moths and butterflies (called lepidopterans). Myrmecology – scientific study of ants. Carcinology – study of crustaceans. Myriapodology – study of centipedes, millipedes, and other myriapods. Ethology – scientific study of animal behavior, usually with a focus on behavior under natural conditions. Helminthology – study of worms, especially parasitic worms. Herpetology – study of amphibians (including frogs, toads, salamanders, newts, and gymnophiona) and reptiles (including snakes, lizards, amphisbaenids, turtles, terrapins, tortoises, crocodilians, and the tuataras). Batrachology – subdiscipline of herpetology concerned with the study of amphibians alone. Ichthyology – study of fishes. This includes bony fishes (Osteichthyes), cartilaginous fishes (Chondrichthyes), and jawless fishes (Agnatha). Malacology – branch of invertebrate zoology which deals with the study of the Mollusca (mollusks or molluscs), the second-largest phylum of animals in terms of described species after the arthropods. Teuthology – branch of Malacology which deals with the study of cephalopods. Mammalogy – study of mammals, a class of vertebrates with characteristics such as homeothermic metabolism, fur, four-chambered hearts, and complex nervous systems. Mammalogy has also been known as "mastology," "theriology," and "therology." There are about 4,200 different species of animals which are considered mammals. Cetology – branch of marine mammal science that studies the approximately eighty species of whales, dolphins, and porpoise in the scientific order Cetacea. Primatology – scientific study of primates +Human biology – interdisciplinary field studying the range of humans and human populations via biology/life sciences, anthropology/social sciences, applied/medical sciences +Biological anthropology – subfield of anthropology that studies the physical morphology, genetics and behavior of the human genus, other hominins and hominids across their evolutionary development +Human behavioral ecology – the study of behavioral adaptations (foraging, reproduction, ontogeny) from the evolutionary and ecologic perspectives (see behavioral ecology). It focuses on human adaptive responses (physiological, developmental, genetic) to environmental stresses. Nematology – scientific discipline concerned with the study of nematodes, or roundworms. Ornithology – scientific study of birds. Interdisciplinary fields +Astrobiology – study of potential life outside of Earth. Bioarchaeology – study of human and animal remains from archaeological sites. Comparative biology – study of patterns and natural variation in species through similarities and differences at all levels, from genes to communities. Geobiology – study of the interactions between the physical Earth and the biosphere. Biolinguistics – biological study of language. Biological anthropology – study of the development of the human species. + +== Biologists == + +Lists of notable biologists +List of notable biologists +List of Nobel Prize winners in physiology or medicine +Lists of biologists by author abbreviation +List of authors of names published under the ICZN +Lists of biologists by subject + +List of biochemists +List of ecologists +List of neuroscientists +List of physiologists + +== See also == + +Bibliography of biology +Earliest known life forms +Invasion biology terminology +List of omics topics in biology +Related outlines + +Outline of life forms +Outline of zoology +Outline of engineering +Outline of technology +List of social sciences +Journals + +Biology journals + +== References == + +== External links == + +OSU's Phylocode +The Tree of Life: A multi-authored, distributed Internet project containing information about phylogeny and biodiversity. +MIT video lecture series on biology +A wiki site for protocol sharing run from MIT. +Biology and Bioethics. +Biology online wiki dictionary. +Biology Video Sharing Community. +What is Biotechnology Archived 19 April 2012 at the Wayback Machine : a voluntary program as Biotech for Beginners. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_cell_biology-0.md b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-0.md new file mode 100644 index 000000000..bedd39494 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-0.md @@ -0,0 +1,63 @@ +--- +title: "Outline of cell biology" +chunk: 1/6 +source: "https://en.wikipedia.org/wiki/Outline_of_cell_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:35.262817+00:00" +instance: "kb-cron" +--- + +The following outline is provided as an overview of and topical guide to cell biology: +Cell biology – A branch of biology that includes study of cells regarding their physiological properties, structure, and function; the organelles they contain; interactions with their environment; and their life cycle, division, and death. This is done both on a microscopic and molecular level. Cell biology research extends to both the great diversities of single-celled organisms like bacteria and the complex specialized cells in multicellular organisms like humans. Formerly, the field was called cytology (from Greek κύτος, kytos, "a hollow;" and -λογία, -logia). + +== A branch of science == +Cell biology can be described as all of the following: + +Branch of science – A systematic enterprise that builds and organizes knowledge in the form of testable explanations and predictions about the universe. +Branch of natural science – The branch of science concerned with the description, prediction, and understanding of natural phenomena based on observational and empirical evidence. Validity, accuracy, and social mechanisms ensuring quality control, such as peer review and repeatability of findings, are among the criteria and methods used for this purpose. +Branch of biology – The study of life and living organisms, including their structure, function, growth, evolution, distribution, and taxonomy. +Academic discipline – Focused study in one academic field or profession. A discipline incorporates expertise, people, projects, communities, challenges, studies, inquiry, and research areas that are strongly associated with a given discipline. + +== Essence of cell biology == +Cell – The structural and functional unit of all known living organisms. It is the smallest unit of an organism that is classified as living, and also known as the building block of life. Cell comes from the Latin cellula, meaning, a small room. Robert Hooke first coined the term in his book, Micrographia, where he compared the structure of cork cells viewed through his microscope to that of the small rooms (or monks' "cells") of a monastery. +Cell theory – The scientific theory which states that all organisms are composed of one or more cells. Vital functions of an organism occur within cells. All cells come from preexisting cells and contain the hereditary information necessary for regulating cell functions and for transmitting information to the next generation of cells. +Cell biology – (formerly cytology) The study of cells. +Cell division – The process of one parent cell separating into two or more daughter cells. +Endosymbiotic theory – The evolutionary theory that certain eukaryotic organelles originated as separate prokaryotic organisms which were taken inside the cell as endosymbionts. +Cellular respiration – The metabolic reactions and processes that take place in a cell or across the cell membrane to convert biochemical energy from fuel molecules into adenosine triphosphate (ATP) and then release the cell's waste products. +Lipid bilayer – A membrane composed of two layers of lipid molecules (usually phospholipids). The lipid bilayer is a critical component of the cell membrane. + +== Aspects of cells == +Homeostasis – The property of either an open system or a closed system, especially a living organism, that regulates its internal environment so as to maintain a stable, constant condition. +Life – A condition of growth through metabolism, reproduction, and the power of adaptation to environment through changes originating internally. +Microscopic – The scale of objects, like cells, that are too small to be seen easily by the naked eye and which require a lens or microscope to see them clearly. +Unicellular – Organisms which are composed of only one cell. +Multicellular – Organisms consisting of more than one cell and having differentiated cells that perform specialized functions. +Tissues – A collection of interconnected cells that perform a similar function within an organism. +Cellular differentiation – A concept in developmental biology whereby less specialized cells become a more specialized cell type in multicellular organisms. + +== Types of cells == +Cell type – Distinct morphological or functional form of cell. When a cell switches state from one cell type to another, it undergoes cellular differentiation. There are at least several hundred distinct cell types in the adult human body. + +=== By organism === +Eukaryote – Organisms whose cells are organized into complex structures enclosed within membranes, including plants, animals, fungi, and protists. +Animal cell – Eukaryotic cells belonging to kingdom Animalia, characteristically having no cell wall or chloroplasts. +Plant cell – Eukaryotic cells belonging to kingdom Plantae and having chloroplasts, cellulose cell walls, and large central vacuoles. +Fungal hypha – The basic cellular unit of organisms in kingdom fungi. Typically tubular, multinucleated, and with a chitinous cell wall. +Protist – A highly variable kingdom of eukaryotic organisms which are mostly unicellular and not plants, animals, or fungi. +Prokaryote – A group of organisms whose cells lack a membrane-bound cell nucleus, or any other membrane-bound organelles, including bacteria. +Bacterial cells – A prokaryotic cell belonging to the mostly unicellular Domain Bacteria. +Archea cell – A cell belonging to the prokaryotic and single-celled microorganisms in Domain Archea. + +=== By function === +Gamete – A haploid reproductive cell. Sperm and ova are gametes. Gametes fuse with another gamete during fertilization (conception) in organisms that reproduce sexually. +Sperm – Male reproductive cell (a gamete). +Ovum – Female reproductive cell (a gamete). +Zygote – A cell that is the result of fertilization (the fusing of two gametes). +Egg – The zygote of most birds and reptiles, resulting from fertilization of the ovum. The largest existing single cells currently known are (fertilized) eggs. +Meristemic cell – Undifferentiated plants cells analogous to animal stem cells. +Stem cell – Undifferentiated cells found in most multi-cellular organisms which are capable of retaining the ability to reinvigorate themselves through mitotic cell division and can differentiate into a diverse range of specialized cell types. +Germ cell – Gametes and gonocytes, these are often . Germ cells should not be confused with "germs" (pathogens). +Somatic cell – Any cells forming the body of an organism, as opposed to germline cells. +more... \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_cell_biology-1.md b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-1.md new file mode 100644 index 000000000..da647486f --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-1.md @@ -0,0 +1,42 @@ +--- +title: "Outline of cell biology" +chunk: 2/6 +source: "https://en.wikipedia.org/wiki/Outline_of_cell_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:35.262817+00:00" +instance: "kb-cron" +--- + +== General cellular anatomy == +Cellular compartment – All closed parts within a cell whose lumen is usually surrounded by a single or double lipid layer membrane. +Organelles – A specialized subunit within a cell that has a specific function, and is separately enclosed within its own lipid membrane or traditionally any subcellular functional unit. + +=== Organelles === +Endomembrane system +Endoplasmic reticulum – An organelle composed of an interconnected network of tubules, vesicles and cisternae. +Membrane bound polyribosome – Polyribosomes that are attached to a cell's endoplasmic reticulum. +Smooth endoplasmic reticulum – A section of endoplasmic reticulum on which ribosomes are not attached is termed as smooth endoplasmic reticulum. It has functions in several metabolic processes, including synthesis of lipids, metabolism of carbohydrates and calcium concentration, drug detoxification, and attachment of receptors on cell membrane proteins. +Rough endoplasmic reticulum – A section of the endoplasmic reticulum on with the protein manufacturing organelle i.e. ribosomes are attached is termed as rough endoplasmic reticulum which give it a "rough" appearance (hence its name). Its primary function is the synthesis of enzymes and other proteins. +Vesicle – A relatively small intracellular, membrane-enclosed sac that stores or transports substances. +Golgi apparatus – A eukaryotic organelle that processes and packages macromolecules such as proteins and lipids that are synthesized by the cell. +Nuclear envelope – It is the double lipid bilayer membrane which surrounds the genetic material and nucleolus in eukaryotic cells. The nuclear membrane consists of two lipid bilayers: +Inner nuclear membrane +Outer nuclear membrane +Perinuclear space – Space between the nuclear membranes, a region contiguous with the lumen (inside) of the endoplasmic reticulum. The nuclear membrane has many small holes called nuclear pores that allow material to move in and out of the nucleus. +Lysosomes – It is a membrane-bound cell organelle found in most animal cells (they are absent in red blood cells). Structurally and chemically, they are spherical vesicles containing hydrolytic enzymes capable of breaking down virtually all kinds of biomolecules, including proteins, nucleic acids, carbohydrates, lipids, and cellular debris. lysosomes act as the waste disposal system of the cell by digesting unwanted materials in the cytoplasm, both from outside of the cell and obsolete components inside the cell. For this function they are popularly referred to as "suicide bags" or "suicide sacs" of the cell. +Endosomes – It is a membrane-bounded compartment inside eukaryotic cells. It is a compartment of the endocytic membrane transport pathway from the plasma membrane to the lysosome. Endosomes represent a major sorting compartment of the endomembrane system in cells. +Cell nucleus – A membrane-enclosed organelle found in most eukaryotic cells. It contains most of the cell's genetic material, organized as multiple long linear DNA molecules in complex with a large variety of proteins, such as histones, to form chromosomes. +Nucleoplasm – Viscous fluid, inside the nuclear envelope, similar to cytoplasm. +Nucleolus – Where ribosomes are assembled from proteins and RNA. +Chromatin – All DNA and its associated proteins in the nucleus. +Chromosome – A single DNA molecule with attached proteins. +Energy creators +Mitochondrion – A membrane-enclosed organelle found in most eukaryotic cells. Often called "cellular power plants", mitochondria generate most of cells' supply of adenosine triphosphate (ATP), the body's main source of energy. +Chloroplast – An organelles found in plant cells and eukaryotic algae that conduct photosynthesis. +Centrosome – The main microtubule organizing center of animal cells as well as a regulator of cell-cycle progression. +Lysosome – The organelles that contain digestive enzymes (acid hydrolases). They digest excess or worn-out organelles, food particles, and engulfed viruses or bacteria. +Peroxisome – A ubiquitous organelle in eukaryotes that participates in the metabolism of fatty acids and other metabolites. Peroxisomes have enzymes that rid the cell of toxic peroxides. +Ribosome – It is a large and complex molecular machine, found within all living cells, that serves as the site of biological protein synthesis (translation). Ribosomes build proteins from the genetic instructions held within messenger RNA. +Symbiosome – A temporary organelle that houses a nitrogen-fixing endosymbiont. +Vacuole – A membrane-bound compartments within some eukaryotic cells that can serve a variety of secretory, excretory, and storage functions. \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_cell_biology-2.md b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-2.md new file mode 100644 index 000000000..14da57e4f --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-2.md @@ -0,0 +1,43 @@ +--- +title: "Outline of cell biology" +chunk: 3/6 +source: "https://en.wikipedia.org/wiki/Outline_of_cell_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:35.262817+00:00" +instance: "kb-cron" +--- + +=== Structures === +Cell membrane – (also called the plasma membrane, plasmalemma or "phospholipid bilayer") A semipermeable lipid bilayer found in all cells; it contains a wide array of functional macromolecules. +Cell wall – A fairly rigid layer surrounding a cell, located external to the cell membrane, which provides the cell with structural support, protection, and acts as a filtering mechanism. +Centriole – A barrel shaped microtubule structure found in most eukaryotic cells other than those of plants and fungi. +Cluster of differentiation – A cell surface molecules present on white blood cells initially but found in almost any kind of cell of the body, providing targets for immunophenotyping of cells. Physiologically, CD molecules can act in numerous ways, often acting as receptors or ligands (the molecule that activates a receptor) important to the cell. A signal cascade is usually initiated, altering the behavior of the cell (see cell signaling). +Cytoskeleton – A cellular "scaffolding" or "skeleton" contained within the cytoplasm that is composed of three types of fibers: microfilaments, intermediate filaments, and microtubules. +Cytoplasm – A gelatinous, semi-transparent fluid that fills most cells, it includes all cytosol, organelles and cytoplasmic inclusions. +Cytosol – It is the internal fluid of the cell, and where a portion of cell metabolism occurs. +Inclusions – A chemical substances found suspended directly in the cytosol. +Photosystem – They are functional and structural units of protein complexes involved in photosynthesis that together carry out the primary photochemistry of photosynthesis: the absorption of light and the transfer of energy and electrons. They are found in the thylakoid membranes of plants, algae and cyanobacteria (in plants and algae these are located in the chloroplasts), or in the cytoplasmic membrane of photosynthetic bacteria. +Plasmid – An extrachromosomal DNA molecule separate from the chromosomal DNA and capable of sexual replication, it is typically ring shaped and found in bacteria. +Spindle fiber – The structure that separates the chromosomes into the daughter cells during cell division. +Stroma – The colorless fluid surrounding the grana within the chloroplast. Within the stroma are grana, stacks of thylakoids, the sub-organelles, the daughter cells, where photosynthesis is commenced before the chemical changes are completed in the stroma. +Thylakoid membrane – It is the site of the light-dependent reactions of photosynthesis with the photosynthetic pigments embedded directly in the membrane. + +=== Molecules === +DNA – Deoxyribonucleic acid (DNA) is a nucleic acid that contains the genetic instructions used in the development and functioning of all known living organisms and some viruses. +DNA helicase +DNA polymerase +DNA ligase +RNA – Ribonucleic acid is a nucleic acid made from a long chain of nucleotide, in a cell it is typically transcribed from DNA. +RNA polymerase +mRNA +rRNA +tRNA +Proteins – Biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function. +List of proteins +Enzymes – Proteins that catalyze (i.e. accelerate) the rates of specific chemical reactions within cells. +Pigments +Chlorophyll – It is a term used for several closely related green pigments found in cyanobacteria and the chloroplasts of algae and plants. Chlorophyll is an extremely important biomolecule, critical in photosynthesis, which allows plants to absorb energy from light. +Carotenoid – They are organic pigments that are found in the chloroplasts and chromoplasts of plants and some other photosynthetic organisms, including some bacteria and some fungi. Carotenoids can be produced from fats and other basic organic metabolic building blocks by all these organisms. There are over 600 known carotenoids; they are split into two classes, xanthophylls (which contain oxygen) and carotenes (which are purely hydrocarbons, and contain no oxygen). + +== Biological activity of cells == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_cell_biology-3.md b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-3.md new file mode 100644 index 000000000..77849d5a9 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-3.md @@ -0,0 +1,53 @@ +--- +title: "Outline of cell biology" +chunk: 4/6 +source: "https://en.wikipedia.org/wiki/Outline_of_cell_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:35.262817+00:00" +instance: "kb-cron" +--- + +=== Cellular metabolism === +Cellular respiration – +Glycolysis – The foundational process of both aerobic and anaerobic respiration, glycolysis is the archetype of universal metabolic processes known and occurring (with variations) in many types of cells in nearly all organisms. +Pyruvate dehydrogenase – Enzyme in the eponymous complex linking glycolysis and the subsequent citric acid cycle. +Citric acid cycle – Also known as the Krebs cycle, an important aerobic metabolic pathway. +Electron transport chain – A biochemical process which associates electron carriers (such as NADH and FADH2) and mediating biochemical reactions that produce adenosine triphosphate (ATP), which is a major energy intermediate in living organisms. Typically occurs across a cellular membrane. +Photosynthesis – The conversion of light energy into chemical energy by living organisms. +Light-dependent reactions – A series of biochemical reactions driven by light that take place across thylakoid membrane to provide for the Calvin cycle reactions. +Calvin cycle – A series of anabolic biochemical reactions that takes place in the stroma of chloroplasts in photosynthetic organisms. It is one of the light-independent reactions or dark reactions. +Electron transport chain – A biochemical process which associates electron carriers (such as NADH and FADH2) and mediating biochemical reactions that produce adenosine triphosphate (ATP), which is a major energy intermediate in living organisms. Typically occurs across a cellular membrane. +Metabolic pathway – A series of chemical reactions occurring within a cell which ultimately leads to sequestering of energy. +Alcoholic fermentation – The anaerobic metabolic process by which sugars such as glucose, fructose, and sucrose, are converted into cellular energy and thereby producing ethanol, and carbon dioxide as metabolic waste products. +Lactic acid fermentation – An anaerobic metabolic process by which sugars such as glucose, fructose, and sucrose, are converted into cellular energy and the metabolic waste product lactic acid. +Chemosynthesis – The biological conversion of one or more carbon molecules (usually carbon dioxide or methane) and nutrients into organic matter using the oxidation of inorganic molecules (e.g. hydrogen gas, hydrogen sulfide) or methane as a source of energy, rather than sunlight, as in photosynthesis. +Important molecules: +ADP – Adenosine diphosphate (ADP) (Adenosine pyrophosphate (APP)) is an important organic compound in metabolism and is essential to the flow of energy in living cells. A molecule of ADP consists of three important structural components: a sugar backbone attached to a molecule of adenine and two phosphate groups bonded to the 5 carbon atom of ribose. +ATP – A multifunctional nucleotide that is most important as a "molecular currency" of intracellular energy transfer. +NADH – A coenzyme found in all living cells which serves as an important electron carrier in metabolic processes. +Pyruvate – It is the "energy-molecule" output of the aerobic metabolism of glucose known as glycolysis. +Glucose – An important simple sugar used by cells as a source of energy and as a metabolic intermediate. Glucose is one of the main products of photosynthesis and starts cellular respiration in both prokaryotes and eukaryotes. + +=== Cellular reproduction === + +Cell cycle – The series of events that take place in a eukaryotic cell leading to its replication. +Interphase – The stages of the cell cycle that prepare the cell for division. +Mitosis – In eukaryotes, the process of division of the nucleus and genetic material. +Prophase – The stage of mitosis in which the chromatin condenses into a highly ordered structure called chromosomes and the nuclear membrane begins to break up. +Metaphase – The stage of mitosis in which condensed chromosomes, carrying genetic information, align in the middle of the cell before being separated into each of the two daughter cells. +Anaphase – The stage of mitosis when chromatids (identical copies of chromosomes) separate as they are pulled towards opposite poles within the cell. +Telophase – The stage of mitosis when the nucleus reforms and chromosomes unravel into longer chromatin structures for reentry into interphase. +Cytokinesis – The process cells use to divide their cytoplasm and organelles. +Meiosis – The process of cell division used to create gametes in sexually reproductive eukaryotes. +Chromosomal crossover – (or crossing over) It is the exchange of genetic material between homologous chromosomes that results in recombinant chromosomes during sexual reproduction. It is one of the final phases of genetic recombination, which occurs in the pachytene stage of prophase I of meiosis during a process called synapsis. +Binary fission – The process of cell division used by prokaryotes. + +=== Transcription and Translation === +Transcription – Fundamental process of gene expression through turning DNA segment into a functional unit of RNA. +Translation – It is the process in which cellular ribosomes create proteins. +mRNA +rRNA +tRNA +Introns +Exons \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_cell_biology-4.md b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-4.md new file mode 100644 index 000000000..5b1208907 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-4.md @@ -0,0 +1,53 @@ +--- +title: "Outline of cell biology" +chunk: 5/6 +source: "https://en.wikipedia.org/wiki/Outline_of_cell_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:35.262817+00:00" +instance: "kb-cron" +--- + +=== Miscellaneous cellular processes === +Cell transport +Osmosis – The diffusion of water through a cell wall or membrane or any partially permeable barrier from a solution of low solute concentration to a solution with high solute concentration. +Passive transport – Movement of molecules into and out of cells without the input of cellular energy. +Active transport – Movement of molecules into and out of cells with the input of cellular energy. +Bulk transport +Endocytosis – It is a form of active transport in which a cell transports molecules (such as proteins) into the cell by engulfing them in an energy-using process. +Exocytosis – It is a form of active transport in which a cell transports molecules (such as proteins) out of the cell by expelling them. +Phagocytosis – The process a cell uses when engulfing solid particles into the cell membrane to form an internal phagosome, or "food vacuole." +Tonicity – This is a measure of the effective osmotic pressure gradient (as defined by the water potential of the two solutions) of two solutions separated by a semipermeable membrane. +Programmed cell death – The death of a cell in any form, mediated by an intracellular program (ex. apoptosis or autophagy). +Apoptosis – A series of biochemical events leading to a characteristic cell morphology and death, which is not caused by damage to the cell. +Autophagy – The process whereby cells "eat" their own internal components or microbial invaders. +Cell senescence – The phenomenon where normal diploid differentiated cells lose the ability to divide after about 50 cell divisions. +Cell signaling – Regulation of cell behavior by signals from outside. +Cell adhesion – Holding together cells and tissues. +Motility and Cell migration – The various means for a cell to move, guided by cues in its environment. +Cytoplasmic streaming – Flowing of cytoplasm in eukaryotic cells. +DNA repair – The process used by cells to fix damaged DNA sections. + +== Applied cell biology concepts == +Cell therapy – The process of introducing new cells into a tissue in order to treat a disease. +Cloning – Processes used to create copies of DNA fragments (molecular cloning), cells (cell cloning), or organisms. +Cell disruption – A method or process for releasing biological molecules from inside a cell. + +=== Laboratory procedures === +Bacterial conjugation – Transfer of genetic material between bacterial cells by direct cell-to-cell contact or by a bridge-like connection between two cells. Conjugation is a convenient means for transferring genetic material to a variety of targets. In laboratories, successful transfers have been reported from bacteria to yeast, plants, mammalian cells and isolated mammalian mitochondria. +Cell culture – The process by which cells are grown under controlled conditions, generally outside of their natural environment. In practice, the term "cell culture" now refers to the culturing of cells derived from multi-cellular eukaryotes, especially animal cells. +Cell disruption, and cell unroofing – Methods for releasing molecules from cells. +Cell fractionation – Separation of homogeneous sets from a larger population of cells. +Cell incubator – The device used to grow and maintain microbiological cultures or cell cultures. The incubator maintains optimal temperature, humidity and other conditions such as the carbon dioxide (CO2) and oxygen content of the atmosphere inside. +Cyto-Stain – Commercially available mix of staining dyes for polychromatic staining in histology. +Fluorescent-activated cell sorting – Specialized type of flow cytometry. It provides a method for sorting a heterogeneous mixture of biological cells into two or more containers, one cell at a time, based upon the specific light scattering and fluorescent characteristics of each cell. +Spinning – Using a special bioreactor which features an impeller, stirrer or similar device to agitate the contents (usually a mixture of cells, medium and products like proteins that can be harvested). + +== History of cell biology == +See also Cell biologists below +History of cell biology – is intertwined with the history of biochemistry and the history of molecular biology. Other articles pertaining to the history of cell biology include: + +History of cell theory, embryology and germ theory +History of biochemistry, microbiology, and molecular biology +History of the optical microscope +Timeline of microscope technology \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_cell_biology-5.md b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-5.md new file mode 100644 index 000000000..4bd3d7ef6 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_cell_biology-5.md @@ -0,0 +1,49 @@ +--- +title: "Outline of cell biology" +chunk: 6/6 +source: "https://en.wikipedia.org/wiki/Outline_of_cell_biology" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:35.262817+00:00" +instance: "kb-cron" +--- + +== Cell biologists == +Karl August Möbius – In 1884 first observed the structures that would later be called "organelles". +Bengt Lidforss – Coined the word "organells" which later became "organelle". +Robert Hooke – Coined the word "cell" after looking at cork under a microscope. +Anton van Leeuwenhoek – First observed microscopic single celled organisms in apparently clean water. +Hans Adolf Krebs – Discovered the citric acid cycle in 1937. +Konstantin Mereschkowski – Russian botanist who in 1905 described the Theory of Endosymbiosis. +Edmund Beecher Wilson – Known as America's first cellular biologist, discovered the sex chromosome arrangement in humans. +Albert Claude – Shared the Nobel Prize in 1974 "for describing the structure and function of organelles in biological cells" +Theodor Boveri – In 1888 identified the centrosome and described it as the 'special organ of cell division.' +Peter D. Mitchell – British biochemist who was awarded the 1978 Nobel Prize for Chemistry for his discovery of the chemiosmotic mechanism of ATP synthesis. +Lynn Margulis – An American biologist best known for her theory on the origin of eukaryotic organelles, and her contributions and support of the endosymbiotic theory. +Günter Blobel – An American biologist who won a Nobel Prize for protein targeting in cells. +Peter Agre – An American chemist who won a Nobel Prize for discovering cellular aquaporins. +Christian de Duve – Shared the Nobel Prize in 1974 "for describing the structure and function of organelles in biological cells" +George Emil Palade – Shared the Nobel Prize in 1974 "for describing the structure and function of organelles in biological cells.” +Ira Mellman – An American cell biologist who discovered endosomes. +Paul Nurse – Shared a 2001 Nobel Prize for discoveries regarding cell cycle regulation by cyclin and cyclin dependent kinases. +Leland H. Hartwell – Shared a 2001 Nobel Prize for discoveries regarding cell cycle regulation by cyclin and cyclin dependent kinases. +R. Timothy Hunt – Shared a 2001 Nobel Prize for discoveries regarding cell cycle regulation by cyclin and cyclin dependent kinases. + +== Closely allied sciences == +Cytopathology – A branch of pathology that studies and diagnoses diseases on the cellular level. The most common use of cytopathology is the Pap smear, used to detect cervical cancer at an early treatable stage. +Genetics – The science of heredity and variation in living organisms. +Biochemistry – The study of the chemical processes in living organisms. It deals with the structure and function of cellular components, such as proteins, carbohydrates, lipids, nucleic acids, and other biomolecules. +Cytochemistry – The biochemistry of cells, especially that of the macromolecules responsible for cell structure and function. +Molecular biology – The study of biology at a molecular level, including the various systems of a cell, including the interactions between DNA, RNA and protein biosynthesis and learning how these interactions are regulated. +Developmental biology – The study of the process by which organisms grow and develop, including the genetic control of cell growth, differentiation and "morphogenesis", which is the process that gives rise to tissues, organs and anatomy. +Microbiology – The study of microorganisms, which are unicellular or cell-cluster microscopic organisms as well as viruses. +Cellular microbiology – A discipline bridging microbiology and cell biology. + +== See also == + +Outline of biology + +== Further reading == +Young John K (2010). Introduction to Cell Biology. ISBN 978-981-4307-31-4 & ISBN 978-981-4307-32-1 (pbk). + +== References == \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Outline_of_neuroscience-0.md b/data/en.wikipedia.org/wiki/Outline_of_neuroscience-0.md new file mode 100644 index 000000000..25d070ba1 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Outline_of_neuroscience-0.md @@ -0,0 +1,219 @@ +--- +title: "Outline of neuroscience" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/Outline_of_neuroscience" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:57:28.802178+00:00" +instance: "kb-cron" +--- + +The following outline is provided as an overview of and topical guide to neuroscience: +Neuroscience is the scientific study of the structure and function of the nervous system. It encompasses the branch of biology that deals with the anatomy, biochemistry, molecular biology, and physiology of neurons and neural circuits. It also encompasses cognition, and human behavior. Neuroscience has multiple concepts that each relate to learning abilities and memory functions. Additionally, the brain is able to transmit signals that cause conscious/unconscious behaviors that are responses verbal or non-verbal. This allows people to communicate with one another. + + +== Branches of neuroscience == + + +=== Neurophysiology === +Neurophysiology is the study of the function (as opposed to structure) of the nervous system. + +Brain mapping +Electrophysiology +Extracellular recording +Intracellular recording +Brain stimulation +Electroencephalography +Intermittent rhythmic delta activity +Category: Neurophysiology +Category: Neuroendocrinology +Neuroendocrinology + + +=== Neuroanatomy === +Neuroanatomy is the study of the anatomy of nervous tissue and neural structures of the nervous system. + +Immunostaining +Category: Neuroanatomy + + +=== Neuropharmacology === +Neuropharmacology is the study of how drugs affect cellular function in the nervous system. + +Drug +Psychoactive drug +Anaesthetic +Narcotic + + +=== Behavioral neuroscience === +Behavioral neuroscience, also known as biological psychology, biopsychology, or psychobiology, is the application of the principles of biology to the study of mental processes and behavior in human and non-human animals. + +Neuroethology + + +=== Developmental neuroscience === +Developmental neuroscience aims to describe the cellular basis of brain development and to address the underlying mechanisms. The field draws on both neuroscience and developmental biology to provide insight into the cellular and molecular mechanisms by which complex nervous systems develop. + +Human brain development timeline +Development of the nervous system in humans +Prenatal development - Cognitive development +Aging and memory +(see also Child development - Mechanisms) + + +=== Cognitive neuroscience === +Cognitive neuroscience is concerned with the scientific study of biological substrates underlying cognition, with a focus on the neural substrates of mental processes. + +Neurolinguistics +Neuroimaging +Functional magnetic resonance imaging +Positron emission tomography + + +=== Systems neuroscience === +Systems neuroscience is a subdiscipline of neuroscience which studies the function of neural circuits and systems. It is an umbrella term, encompassing a number of areas of study concerned with how nerve cells behave when connected together to form neural networks. + +Neural circuit +Neural network (biology) +Neural oscillation + + +=== Molecular neuroscience === +Molecular neuroscience is a branch of neuroscience that examines the biology of the nervous system with molecular biology, molecular genetics, protein chemistry and related methodologies (ie. concerning neurotransmitters moving via physiology of synapses etc) + +Neurochemistry +Nutritional neuroscience +Neuropeptide +[ also see Neuropharmacology above] + + +=== Computational neuroscience === +Computational neuroscience includes both the study of the information processing functions of the nervous system, and the use of digital computers to study the nervous system. It is an interdisciplinary science that links the diverse fields of neuroscience, cognitive science and psychology, electrical engineering, computer science, physics and mathematics. + +Neural network +Neuroinformatic +Neuroengineering +Brain–computer interface +Mathematical neuroscience + + +=== Neurophilosophy === +Neurophilosophy or "philosophy of neuroscience" is the interdisciplinary study of neuroscience and philosophy. Work in this field is often separated into two distinct approaches. The first approach attempts to solve problems in philosophy of mind with empirical information from the neurosciences. The second approach attempts to clarify neuroscientific results using the conceptual rigor and methods of philosophy of science. + +Philosophy of mind +Neuroethics +Neuroscience of free will + + +=== Neurology === +Neurology is the medical specialty dealing with disorders of the nervous system. It deals with the diagnosis and treatment of all categories of disease involving the central, peripheral, and autonomic nervous systems. + +Stroke +Parkinson's disease +Alzheimer's disease +Huntington's disease +Multiple sclerosis +Amyotrophic lateral sclerosis +Rabies +Schizophrenia +Epilepsy +Hydrocephalus +Brain damage +Traumatic brain injury +Closed head injury +Coma +Paralysis +Level of consciousness +Neurosurgery + + +=== Neuropsychology === +Neuropsychology studies the structure and function of the brain related to psychological processes and behaviors. The term is used most frequently with reference to studies of the effects of brain damage in humans and animals. + +Agraphia +Agnosia +Alexia +Amnesia +Anosognosia +Aphasia +Apraxia +Dementia +Dyslexia +Hemispatial neglect +Neurobiological effects of physical exercise + + +=== Neuroevolution and neuroeconomics === +Evolution of nervous systems +Neuroevolution + + +== History of neuroscience == +History of neuroscience +Neuron doctrine +Category: History of neuroscience + + +== Nervous system == +Outline of the human nervous system + +Action potential +Acetylcholinesterase +Central nervous system (CNS) +Brain +Dendrite +Glial cells +List of regions in the human brain +Nervous system +Neurite +Neuron +Neuroplasticity +Synaptic plasticity +Long-term potentiation +Neurotransmitter +Acetylcholine +Dopamine +Synapse + + +== Neuroscience organizations == + + +== Persons influential in the field of neuroscience == +List of neuroscientists +Category: Neuroscientists + + +== Related sciences == +Genetics +Neurochemistry +Cognitive science +Psychology +Molecular biology +Psychiatry +Neurosurgery +Linguistics +Developmental biology +Biotechnology +Neurophilosophy + + +== See also == +Fundamentals of Neuroscience at Wikiversity + + +== References == + + +== External links == + +Neuroscience on In Our Time at the BBC +Neuroscience Information Framework (NIF) +American Society for Neurochemistry +Neuroscience Online (electronic neuroscience textbook) +Faculty for Undergraduate Neuroscience (FUN) +Neuroscience for Kids +Neuroscience Discussion Group in ResearchGate +Neuroscience Discussion Forum +HHMI Neuroscience lecture series - Making Your Mind: Molecules, Motion, and Memory Archived 2013-06-24 at the Wayback Machine \ No newline at end of file diff --git a/data/en.wikipedia.org/wiki/Taxonomy_of_Drosera-0.md b/data/en.wikipedia.org/wiki/Taxonomy_of_Drosera-0.md new file mode 100644 index 000000000..275ebc061 --- /dev/null +++ b/data/en.wikipedia.org/wiki/Taxonomy_of_Drosera-0.md @@ -0,0 +1,108 @@ +--- +title: "Taxonomy of Drosera" +chunk: 1/1 +source: "https://en.wikipedia.org/wiki/Taxonomy_of_Drosera" +category: "reference" +tags: "science, encyclopedia" +date_saved: "2026-05-05T07:56:03.507534+00:00" +instance: "kb-cron" +--- + +The genus Drosera was divided in 1994 by Seine & Barthlott into three subgenera and 11 sections on the basis of morphological characteristics. +Discovery and description of new species has been occurring since the 10th century, and as recently as the 1940s barely more than 80 species were known. In recent years, Australian Allen Lowrie has done extensive work in the genus, particularly in describing numerous new species from Australia. His classification of the genus was replaced by Jan Schlauer's work in 1996, although the correct classification is still disputed. + + +== Drosera subg. Arcturia == + +Drosera arcturi +Drosera murfetii +Drosera stenopetala + + +== Drosera subg. Bryastrum == + + +=== D. sect. Bryastrum === +Drosera pygmaea + + +=== Drosera sect. Lamprolepis === + + +== Drosera subg. Coelophylla == +Drosera glanduligera + + +== Drosera subg. Drosera == + + +=== Drosera sect. Arachnopus === +Drosera hartmeyerorum +Drosera serpens +Drosera fragrans +Drosera aurantiaca +Drosera aquatica +Drosera barrettorum +Drosera nana +Drosera glabriscapa +Drosera margaritacea +Drosera indica +Drosera finlaysoniana + + +=== Drosera sect. Drosera === + + +=== Drosera sect. Prolifera === +Drosera adelae +Drosera prolifera +Drosera schizandra +Drosera buubugujin + + +== Drosera subg. Ergaleium == + + +=== Drosera sect. Ergaleium === + + +=== Drosera sect. Erythrorhiza === + + +=== Drosera sect. Stolonifera === + + +== Drosera subg. Lasiocephala == + + +== Drosera subg. Meristocaulis == +Drosera meristocaulis + + +== Drosera subg. Phycopsis == +Drosera binata + + +== Drosera subg. Regiae == + +Drosera regia + + +== Drosera subg. Stelogyne == +Drosera hamiltonii + + +== Drosera subg. Thelocalyx == + +Drosera burmannii +Drosera sessilifolia + + +== Incertae sedis == +Drosera magnifica + + +== References == +Barthlott, Wilhelm; Porembski, Stefan; Seine, Rüdiger; Theisen, Inge: Karnivoren. Stuttgart, 2004, ISBN 978-3-8001-4144-9 +Lowrie, Allen (1987–1998) Carnivorous Plants of Australia, Vol. 1–3, Nedlands, Western Australia. +Schlauer, Jan (1996). "A dichotomous key to the genus Drosera L. (Droseraceae)". Carnivorous Plant Newsletter. 25 (3): 67–88. doi:10.55360/cpn253.js950. \ No newline at end of file