row_id string | dataset_id string | source_dataset string | source_file string | source_table string | source_sha string | row_index int64 | split string | subject_type string | entry_id int64 | sequence_id int64 | target_sequence_id int64 | source_sequence_length int64 | target_sequence_length int64 | protein_id int64 | protein_name string | organism string | isoform int64 | protein_ids string | protein_names string | organisms string | isoforms string | uniprot_accessions string | interpro_accessions string | ec_numbers string | megascale_ids string | other_references string | mutations string | substitutions string | deletions string | insertions string | mutation_count int64 | substitution_count int64 | deletion_count int64 | insertion_count int64 | first_position int64 | first_source_aa string | first_target_aa string | conservation float64 | feature_types string | pdb_ids string | afdb_ids string | structure_ids string | structure_methods string | structure_resolution_min float64 | residue_positions string | residue_chain_names string | residue_secondary_structures string | residue_in_pocket_any bool | residue_in_tunnel_any bool | residue_asa_mean float64 | residue_bfactor_mean float64 | experiment_id int64 | experiment_dataset string | ph float64 | measure string | method string | buffer string | buffer_conc string | exp_temperature float64 | ion string | ion_conc string | pdb_chain_mutation string | tm float64 | dtm float64 | dg float64 | dg_text string | ddg float64 | dh float64 | dcp float64 | dhvh float64 | cm float64 | m_value float64 | trypsin_ml float64 | chymotrypsin_ml float64 | stabilizing float64 | stabilizing_text string | domainome_fitness float64 | domainome_fitness_std float64 | domainome_ddg float64 | domainome_ddg_std float64 | reversibility string | state string | measurement_types string | measurement_datasets string | annotation_types string | publication_id string | publication_type string | publication_title string | publication_year int64 | publication_doi string | publication_pmid string | publication_journal string | publication_url string | publication_author_count int64 | publication_authors string | annotations_json string | measurements_json string | features_json string |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
fireprotdb:9816 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,816 | train | mutant | 2,027 | 183 | 2,263 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134H | D134H | 1 | 1 | 0 | 0 | 134 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,378 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134H | null | null | null | -1.94 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25709,"numValue":-1.94,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25710,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9817 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,817 | train | mutant | 2,027 | 183 | 2,263 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134H | D134H | 1 | 1 | 0 | 0 | 134 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,458 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | 52.5 | NaCl | 0.1 M | 2RN2_A:D134H | null | null | null | -1.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25909,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25910,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9818 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,818 | train | mutant | 2,027 | 183 | 2,263 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134H | D134H | 1 | 1 | 0 | 0 | 134 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,622 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.9 | NaCl | 0.1 M | 2RN2_A:D134H | null | null | null | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26309,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26310,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9819 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,819 | train | mutant | 2,027 | 183 | 2,263 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134H | D134H | 1 | 1 | 0 | 0 | 134 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,690 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134H | null | null | null | -0.53 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv"],"id":26451,"numValue":-0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26452,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9820 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,820 | train | mutant | 2,030 | 183 | 2,267 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134E | D134E | 1 | 1 | 0 | 0 | 134 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,937 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134E | 56.2 | 3.1 | null | null | null | null | 102.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14493,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14494,"numValue":3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14495,"numValue":102.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9821 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,821 | train | mutant | 2,030 | 183 | 2,267 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134E | D134E | 1 | 1 | 0 | 0 | 134 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,947 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134E | 52.4 | 2.4 | null | null | null | null | 107.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14533,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14534,"numValue":2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14535,"numValue":107.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9822 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,822 | train | mutant | 2,030 | 183 | 2,267 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134E | D134E | 1 | 1 | 0 | 0 | 134 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,379 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134E | null | null | null | -0.86 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25711,"numValue":-0.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25712,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9823 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,823 | train | mutant | 2,030 | 183 | 2,267 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134E | D134E | 1 | 1 | 0 | 0 | 134 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,691 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134E | null | null | null | -0.72 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26453,"numValue":-0.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26454,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9824 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,824 | train | mutant | 2,031 | 183 | 2,268 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134Q | D134Q | 1 | 1 | 0 | 0 | 134 | D | Q | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,938 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134Q | 57.9 | 4.8 | null | null | null | null | 96.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14497,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14498,"numValue":4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14499,"numValue":96.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9825 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,825 | train | mutant | 2,031 | 183 | 2,268 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134Q | D134Q | 1 | 1 | 0 | 0 | 134 | D | Q | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,948 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134Q | 51.6 | 1.6 | null | null | null | null | 113.6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14537,"numValue":51.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14538,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14539,"numValue":113.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9826 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,826 | train | mutant | 2,031 | 183 | 2,268 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134Q | D134Q | 1 | 1 | 0 | 0 | 134 | D | Q | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,380 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134Q | null | null | null | -1.32 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25713,"numValue":-1.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25714,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9827 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,827 | train | mutant | 2,031 | 183 | 2,268 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134Q | D134Q | 1 | 1 | 0 | 0 | 134 | D | Q | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,692 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134Q | null | null | null | -0.48 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26455,"numValue":-0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26456,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9829 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,829 | train | mutant | 2,032 | 183 | 2,269 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134S | D134S | 1 | 1 | 0 | 0 | 134 | D | S | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,949 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134S | 50.9 | 0.9 | null | null | null | null | 106.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14541,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14542,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14543,"numValue":106.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9830 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,830 | train | mutant | 2,032 | 183 | 2,269 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134S | D134S | 1 | 1 | 0 | 0 | 134 | D | S | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,381 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134S | null | null | null | -1.08 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25715,"numValue":-1.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25716,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9831 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,831 | train | mutant | 2,032 | 183 | 2,269 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134S | D134S | 1 | 1 | 0 | 0 | 134 | D | S | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,693 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134S | null | null | null | -0.26 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26457,"numValue":-0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26458,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9832 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,832 | train | mutant | 2,033 | 183 | 2,270 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134T | D134T | 1 | 1 | 0 | 0 | 134 | D | T | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,940 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134T | 57 | 3.9 | null | null | null | null | 90.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14505,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14506,"numValue":3.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14507,"numValue":90.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9833 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,833 | train | mutant | 2,033 | 183 | 2,270 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134T | D134T | 1 | 1 | 0 | 0 | 134 | D | T | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,950 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134T | 50.4 | 0.4 | null | null | null | null | 107.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14545,"numValue":50.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14546,"numValue":0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14547,"numValue":107.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9835 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,835 | train | mutant | 2,033 | 183 | 2,270 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134T | D134T | 1 | 1 | 0 | 0 | 134 | D | T | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,694 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134T | null | null | null | -0.12 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26459,"numValue":-0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26460,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,836 | train | mutant | 2,034 | 183 | 2,271 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134V | D134V | 1 | 1 | 0 | 0 | 134 | D | V | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,941 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134V | 57.2 | 4.1 | null | null | null | null | 99 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14509,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14510,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14511,"numValue":99.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9837 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,837 | train | mutant | 2,034 | 183 | 2,271 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134V | D134V | 1 | 1 | 0 | 0 | 134 | D | V | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,951 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134V | 51.1 | 1.1 | null | null | null | null | 106.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14549,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14550,"numValue":1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14551,"numValue":106.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,838 | train | mutant | 2,034 | 183 | 2,271 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134V | D134V | 1 | 1 | 0 | 0 | 134 | D | V | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,383 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134V | null | null | null | -1.12 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25719,"numValue":-1.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25720,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,839 | train | mutant | 2,034 | 183 | 2,271 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134V | D134V | 1 | 1 | 0 | 0 | 134 | D | V | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,695 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134V | null | null | null | -0.31 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26461,"numValue":-0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26462,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9840 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,840 | train | mutant | 2,035 | 183 | 2,272 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134I | D134I | 1 | 1 | 0 | 0 | 134 | D | I | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,942 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134I | 57.7 | 4.6 | null | null | null | null | 101.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14513,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14514,"numValue":4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14515,"numValue":101.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,841 | train | mutant | 2,035 | 183 | 2,272 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134I | D134I | 1 | 1 | 0 | 0 | 134 | D | I | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,952 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134I | 52.3 | 2.3 | null | null | null | null | 104.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14553,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14554,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14555,"numValue":104.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,842 | train | mutant | 2,035 | 183 | 2,272 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134I | D134I | 1 | 1 | 0 | 0 | 134 | D | I | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,384 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134I | null | null | null | -1.27 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25721,"numValue":-1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25722,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9843 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,843 | train | mutant | 2,035 | 183 | 2,272 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134I | D134I | 1 | 1 | 0 | 0 | 134 | D | I | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,696 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134I | null | null | null | -0.69 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26463,"numValue":-0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26464,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,844 | train | mutant | 2,036 | 183 | 2,273 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134L | D134L | 1 | 1 | 0 | 0 | 134 | D | L | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,943 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:D134L | 58.6 | 5.5 | null | null | null | null | 96.4 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":14517,"numValue":58.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14518,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14519,"numValue":96.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,845 | train | mutant | 2,036 | 183 | 2,273 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134L | D134L | 1 | 1 | 0 | 0 | 134 | D | L | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 3,953 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:D134L | 53.8 | 3.8 | null | null | null | null | 118.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14557,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14558,"numValue":3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14559,"numValue":118.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9846 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,846 | train | mutant | 2,036 | 183 | 2,273 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134L | D134L | 1 | 1 | 0 | 0 | 134 | D | L | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,385 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 53.1 | NaCl | 0.1 M | 2RN2_A:D134L | null | null | null | -1.51 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":53.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25723,"numValue":-1.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25724,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9847 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,847 | train | mutant | 2,036 | 183 | 2,273 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D134L | D134L | 1 | 1 | 0 | 0 | 134 | D | L | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 134 | A | H | true | true | 50.017412 | 17.535 | 7,697 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | NaCl | 0.1 M | 2RN2_A:D134L | null | null | null | -1.15 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 365 | ARTICLE | Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site-directed random mutagenesis. | 1,994 | 10.1111/j.1432-1033.1994.tb18664.x | 8125123 | Eur J Biochem;220;623-31 | 7 | Haruki M|Oobatake M|Kanaya S|Noguchi E|Nakai C|Itaya M|Liu Y Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26465,"numValue":-1.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26466,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":84,"numValue":null,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16643,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9848 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,848 | train | mutant | 2,079 | 183 | 2,320 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E135K | E135K | 1 | 1 | 0 | 0 | 135 | E | K | 3 | CONSERVATION | 2RN2 | 76 | null | 135 | A | H | false | true | 106.857811 | 20.721111 | 4,092 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:E135K | 51.9 | -0.8 | null | null | null | null | 89.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15116,"numValue":51.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15117,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15118,"numValue":89.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16644,"numValue":3.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,849 | train | mutant | 2,079 | 183 | 2,320 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E135K | E135K | 1 | 1 | 0 | 0 | 135 | E | K | 3 | CONSERVATION | 2RN2 | 76 | null | 135 | A | H | false | true | 106.857811 | 20.721111 | 4,105 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:E135K | 46.4 | -3.7 | null | null | null | null | 99 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15168,"numValue":46.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15169,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15170,"numValue":99.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16644,"numValue":3.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,850 | train | mutant | 2,079 | 183 | 2,320 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E135K | E135K | 1 | 1 | 0 | 0 | 135 | E | K | 3 | CONSERVATION | 2RN2 | 76 | null | 135 | A | H | false | true | 106.857811 | 20.721111 | 7,429 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:E135K | null | null | null | 0.22 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25827,"numValue":0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25828,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16644,"numValue":3.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9851 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,851 | train | mutant | 2,079 | 183 | 2,320 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E135K | E135K | 1 | 1 | 0 | 0 | 135 | E | K | 3 | CONSERVATION | 2RN2 | 76 | null | 135 | A | H | false | true | 106.857811 | 20.721111 | 7,666 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:E135K | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv"],"id":26397,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26398,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16644,"numValue":3.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9852 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,852 | train | sequence | 225 | 225 | -1 | 504 | -1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,240 | ProTherm | 7 | Fluorescence | Thermal | potassium phosphate | 20 mM | null | NaCl | 100 mM | 51.6 | null | null | null | null | null | 27 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 39 | ARTICLE | Increasing protein stability using a rational approach combining sequence homology and structural alignment: Stabilizing the WW domain. | 2,001 | 10.1110/ps.640101 | 11420447 | Protein Sci;10;1454-65 | 3 | Jiang X|Kowalski J|Kelly J W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl... | [{"datasets":[],"id":80403,"numValue":51.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80404,"numValue":27.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":80405,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:9853 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,853 | train | sequence | 225 | 225 | -1 | 504 | -1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,241 | ProTherm | 7 | Fluorescence | Thermal | potassium | 20 mM | null | NaCl | 2 M | 52.9 | null | null | null | null | null | 25 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 39 | ARTICLE | Increasing protein stability using a rational approach combining sequence homology and structural alignment: Stabilizing the WW domain. | 2,001 | 10.1110/ps.640101 | 11420447 | Protein Sci;10;1454-65 | 3 | Jiang X|Kowalski J|Kelly J W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":80406,"numValue":52.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80407,"numValue":25.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":80408,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:9855 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,855 | train | mutant | 4,905,551 | 225 | 4,912,139 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162A | Q162A | 1 | 1 | 0 | 0 | 162 | Q | A | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,014 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.137898 | 0.106157 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178710,"numValue":-0.137898448615802,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178711,"numValue":0.106156561314978,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9856 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,856 | train | mutant | 4,905,552 | 225 | 4,912,140 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162C | Q162C | 1 | 1 | 0 | 0 | 162 | Q | C | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,015 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.439621 | 0.485116 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178712,"numValue":-0.439621150531082,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178713,"numValue":0.485116332747862,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9857 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,857 | train | mutant | 4,905,553 | 225 | 4,912,141 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162D | Q162D | 1 | 1 | 0 | 0 | 162 | Q | D | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,016 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.150301 | 0.072112 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178714,"numValue":0.150301498615939,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178715,"numValue":0.0721119041562959,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9858 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,858 | train | mutant | 4,905,554 | 225 | 4,912,142 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162E | Q162E | 1 | 1 | 0 | 0 | 162 | Q | E | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,017 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.263988 | 0.093283 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178716,"numValue":-0.263987783847857,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178717,"numValue":0.0932829307649319,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,859 | train | mutant | 4,905,555 | 225 | 4,912,143 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162F | Q162F | 1 | 1 | 0 | 0 | 162 | Q | F | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,018 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.54525 | 0.963536 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178718,"numValue":0.545249768187046,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178719,"numValue":0.963535613157464,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9860 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,860 | train | mutant | 4,905,556 | 225 | 4,912,144 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162G | Q162G | 1 | 1 | 0 | 0 | 162 | Q | G | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,019 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.334281 | 0.172239 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178720,"numValue":-0.334281161413973,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178721,"numValue":0.172239153082065,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9861 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,861 | train | mutant | 4,905,557 | 225 | 4,912,145 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162H | Q162H | 1 | 1 | 0 | 0 | 162 | Q | H | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,020 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.770614 | 0.219112 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178722,"numValue":-0.770613977154631,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178723,"numValue":0.219112210233083,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9862 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,862 | train | mutant | 4,905,558 | 225 | 4,912,146 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162I | Q162I | 1 | 1 | 0 | 0 | 162 | Q | I | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,021 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.706454 | 0.192079 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178724,"numValue":0.706453883519471,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178725,"numValue":0.192079391819348,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9863 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,863 | train | mutant | 4,905,559 | 225 | 4,912,147 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162K | Q162K | 1 | 1 | 0 | 0 | 162 | Q | K | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,022 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.147896 | 0.0925 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178726,"numValue":0.147896019059694,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178727,"numValue":0.0924997176444181,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,864 | train | mutant | 4,905,560 | 225 | 4,912,148 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162L | Q162L | 1 | 1 | 0 | 0 | 162 | Q | L | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,023 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.132127 | 0.120171 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178728,"numValue":-0.132126603036015,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178729,"numValue":0.120170854751372,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,865 | train | mutant | 4,905,561 | 225 | 4,912,149 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162M | Q162M | 1 | 1 | 0 | 0 | 162 | Q | M | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,024 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.070643 | 0.067588 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178730,"numValue":-0.0706429226810122,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178731,"numValue":0.0675877315814345,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,866 | train | mutant | 4,905,562 | 225 | 4,912,150 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162N | Q162N | 1 | 1 | 0 | 0 | 162 | Q | N | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,025 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178732,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178733,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9867 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,867 | train | mutant | 4,905,563 | 225 | 4,912,151 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162P | Q162P | 1 | 1 | 0 | 0 | 162 | Q | P | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,026 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.404407 | 0.123192 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178734,"numValue":-0.404407018395979,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178735,"numValue":0.123191664245354,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,868 | train | mutant | 4,905,969 | 225 | 4,912,557 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162R | Q162R | 1 | 1 | 0 | 0 | 162 | Q | R | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,007 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.485748 | 0.047473 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180696,"numValue":-0.485748052145343,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180697,"numValue":0.0474730419131715,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9870 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,870 | train | mutant | 4,905,971 | 225 | 4,912,559 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162T | Q162T | 1 | 1 | 0 | 0 | 162 | Q | T | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,009 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180700,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180701,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9871 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,871 | train | mutant | 4,905,972 | 225 | 4,912,560 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | Q162V | Q162V | 1 | 1 | 0 | 0 | 162 | Q | V | 8 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,010 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.053823 | 0.078704 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180702,"numValue":-0.0538226957206439,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180703,"numValue":0.0787039261647006,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16826,"numValue":8.0,"position":162,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9874 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,874 | train | mutant | 4,905,564 | 225 | 4,912,152 | 504 | 503 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | delS163 | delS163 | 1 | 0 | 1 | 0 | 163 | S | - | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,027 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.27634 | 0.230886 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178736,"numValue":-1.27634030934975,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178737,"numValue":0.230886441625074,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9875 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,875 | train | mutant | 4,905,564 | 225 | 4,912,152 | 504 | 503 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | delS163 | delS163 | 1 | 0 | 1 | 0 | 163 | S | - | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,043 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178768,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178769,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,876 | train | mutant | 4,905,565 | 225 | 4,912,153 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163A | S163A | 1 | 1 | 0 | 0 | 163 | S | A | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,028 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.282895 | 0.038729 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178738,"numValue":-0.282895128734928,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178739,"numValue":0.0387292361318084,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,877 | train | mutant | 4,905,566 | 225 | 4,912,154 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163C | S163C | 1 | 1 | 0 | 0 | 163 | S | C | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,029 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.345702 | 0.08189 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178740,"numValue":-0.345702294224133,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178741,"numValue":0.0818896455323906,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9878 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,878 | train | mutant | 4,905,567 | 225 | 4,912,155 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163D | S163D | 1 | 1 | 0 | 0 | 163 | S | D | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,030 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.333834 | 0.08615 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178742,"numValue":0.333833714659013,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178743,"numValue":0.086149962309319,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9879 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,879 | train | mutant | 4,905,568 | 225 | 4,912,156 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163E | S163E | 1 | 1 | 0 | 0 | 163 | S | E | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,031 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.1881 | 0.074317 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178744,"numValue":-0.188099508851403,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178745,"numValue":0.0743169899332892,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9880 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,880 | train | mutant | 4,905,569 | 225 | 4,912,157 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163F | S163F | 1 | 1 | 0 | 0 | 163 | S | F | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,032 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.277422 | 0.114841 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178746,"numValue":-0.27742206445667,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178747,"numValue":0.114840726867608,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9882 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,882 | train | mutant | 4,905,571 | 225 | 4,912,159 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163H | S163H | 1 | 1 | 0 | 0 | 163 | S | H | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,034 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.314714 | 0.09026 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178750,"numValue":-0.314713886953136,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178751,"numValue":0.0902601632381488,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9883 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,883 | train | mutant | 4,905,572 | 225 | 4,912,160 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163I | S163I | 1 | 1 | 0 | 0 | 163 | S | I | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,035 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.387853 | 0.12761 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178752,"numValue":-0.387852938857119,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178753,"numValue":0.127610436639719,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9884 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,884 | train | mutant | 4,905,573 | 225 | 4,912,161 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163K | S163K | 1 | 1 | 0 | 0 | 163 | S | K | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,036 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.240037 | 0.064891 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178754,"numValue":-0.240036691504144,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178755,"numValue":0.0648907879647585,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9885 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,885 | train | mutant | 4,905,574 | 225 | 4,912,162 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163L | S163L | 1 | 1 | 0 | 0 | 163 | S | L | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,037 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.140175 | 0.056751 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178756,"numValue":-0.140174843046629,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178757,"numValue":0.0567507089637915,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,886 | train | mutant | 4,905,575 | 225 | 4,912,163 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163M | S163M | 1 | 1 | 0 | 0 | 163 | S | M | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,038 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.041816 | 0.076709 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178758,"numValue":-0.0418163286621004,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178759,"numValue":0.0767090533388586,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9888 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,888 | train | mutant | 4,905,577 | 225 | 4,912,165 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163P | S163P | 1 | 1 | 0 | 0 | 163 | S | P | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,040 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.649749 | 0.092003 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178762,"numValue":-0.64974881847587,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178763,"numValue":0.0920030299904922,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9889 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,889 | train | mutant | 4,905,578 | 225 | 4,912,166 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163Q | S163Q | 1 | 1 | 0 | 0 | 163 | S | Q | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,041 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.299138 | 0.07283 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178764,"numValue":-0.299138098617584,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178765,"numValue":0.072830407918714,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,890 | train | mutant | 4,905,579 | 225 | 4,912,167 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163R | S163R | 1 | 1 | 0 | 0 | 163 | S | R | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,042 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.190977 | 0.064061 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178766,"numValue":-0.190977091871958,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178767,"numValue":0.0640613072543476,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,891 | train | mutant | 4,905,965 | 225 | 4,912,553 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163T | S163T | 1 | 1 | 0 | 0 | 163 | S | T | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,003 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.268858 | 0.084805 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180688,"numValue":-0.268858209141719,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180689,"numValue":0.0848053739327035,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,892 | train | mutant | 4,905,966 | 225 | 4,912,554 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163V | S163V | 1 | 1 | 0 | 0 | 163 | S | V | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,004 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.325473 | 0.049859 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180690,"numValue":-0.325472914597528,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180691,"numValue":0.0498593399999371,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,893 | train | mutant | 4,905,967 | 225 | 4,912,555 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163W | S163W | 1 | 1 | 0 | 0 | 163 | S | W | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,005 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.484806 | 0.051461 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180692,"numValue":-0.484806020808725,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180693,"numValue":0.0514614241938681,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9894 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,894 | train | mutant | 4,905,968 | 225 | 4,912,556 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S163Y | S163Y | 1 | 1 | 0 | 0 | 163 | S | Y | 6 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,006 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.346158 | 0.149689 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180694,"numValue":-0.346157718149765,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180695,"numValue":0.149688924428071,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16827,"numValue":6.0,"position":163,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9895 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,895 | train | mutant | 4,905,580 | 225 | 4,912,168 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164A | S164A | 1 | 1 | 0 | 0 | 164 | S | A | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,044 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.419644 | 0.110644 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178770,"numValue":-0.419644139576642,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178771,"numValue":0.110644299975789,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9897 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,897 | train | mutant | 4,905,582 | 225 | 4,912,170 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164D | S164D | 1 | 1 | 0 | 0 | 164 | S | D | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,046 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.127844 | 0.522363 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178774,"numValue":-0.127843587582539,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178775,"numValue":0.522363120489898,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9898 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,898 | train | mutant | 4,905,583 | 225 | 4,912,171 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164E | S164E | 1 | 1 | 0 | 0 | 164 | S | E | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,047 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.232793 | 0.060351 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178776,"numValue":-0.232793420534058,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178777,"numValue":0.0603512702143137,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9899 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,899 | train | mutant | 4,905,584 | 225 | 4,912,172 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164F | S164F | 1 | 1 | 0 | 0 | 164 | S | F | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,048 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.621494 | 0.470239 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178778,"numValue":-0.621494477673067,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178779,"numValue":0.470239489602636,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9900 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,900 | train | mutant | 4,905,585 | 225 | 4,912,173 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164G | S164G | 1 | 1 | 0 | 0 | 164 | S | G | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,049 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.523332 | 0.287837 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178780,"numValue":-0.523332129167334,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178781,"numValue":0.287837276045103,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9901 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,901 | train | mutant | 4,905,586 | 225 | 4,912,174 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164H | S164H | 1 | 1 | 0 | 0 | 164 | S | H | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,050 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178782,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178783,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9902 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,902 | train | mutant | 4,905,587 | 225 | 4,912,175 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164I | S164I | 1 | 1 | 0 | 0 | 164 | S | I | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,051 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.272353 | 0.504092 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178784,"numValue":-0.272352935093345,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178785,"numValue":0.504092281302711,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9903 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,903 | train | mutant | 4,905,588 | 225 | 4,912,176 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164K | S164K | 1 | 1 | 0 | 0 | 164 | S | K | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,052 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.118446 | 0.04154 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178786,"numValue":-0.118446480531041,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178787,"numValue":0.0415403983285594,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9904 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,904 | train | mutant | 4,905,589 | 225 | 4,912,177 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164L | S164L | 1 | 1 | 0 | 0 | 164 | S | L | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,053 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.843655 | 0.209302 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178788,"numValue":-0.843655417497483,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178789,"numValue":0.20930210329998,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9906 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,906 | train | mutant | 4,905,591 | 225 | 4,912,179 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164N | S164N | 1 | 1 | 0 | 0 | 164 | S | N | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,055 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178792,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178793,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9907 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,907 | train | mutant | 4,905,592 | 225 | 4,912,180 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164P | S164P | 1 | 1 | 0 | 0 | 164 | S | P | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,056 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.087914 | 0.098632 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178794,"numValue":-0.0879142223830099,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178795,"numValue":0.0986317687399077,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9908 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,908 | train | mutant | 4,905,593 | 225 | 4,912,181 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164Q | S164Q | 1 | 1 | 0 | 0 | 164 | S | Q | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,057 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.044708 | 0.515266 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178796,"numValue":-1.04470796600698,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178797,"numValue":0.515265614183908,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9909 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,909 | train | mutant | 4,905,594 | 225 | 4,912,182 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164R | S164R | 1 | 1 | 0 | 0 | 164 | S | R | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,093,058 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.437881 | 0.128144 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178798,"numValue":-0.43788067692994,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178799,"numValue":0.128143964318203,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9911 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,911 | train | mutant | 4,905,962 | 225 | 4,912,550 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164V | S164V | 1 | 1 | 0 | 0 | 164 | S | V | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,000 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.660851 | 0.183673 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180682,"numValue":-0.660850646899953,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180683,"numValue":0.183673266924499,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9912 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,912 | train | mutant | 4,905,963 | 225 | 4,912,551 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164W | S164W | 1 | 1 | 0 | 0 | 164 | S | W | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,001 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180684,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180685,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9913 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,913 | train | mutant | 4,905,964 | 225 | 4,912,552 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | S164Y | S164Y | 1 | 1 | 0 | 0 | 164 | S | Y | 9 | CONSERVATION | 1K9Q | 347 | null | false | false | null | null | 5,094,002 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.700205 | 0.398208 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180686,"numValue":-0.700204568015105,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180687,"numValue":0.398208104106312,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16828,"numValue":9.0,"position":164,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:9914 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,914 | train | mutant | 4,905,595 | 225 | 4,912,183 | 504 | 503 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | delF165 | delF165 | 1 | 0 | 1 | 0 | 165 | F | - | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,093,059 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.37978 | 0.232922 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178800,"numValue":-1.37977994060953,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178801,"numValue":0.232922433139743,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9915 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,915 | train | mutant | 4,905,595 | 225 | 4,912,183 | 504 | 503 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | delF165 | delF165 | 1 | 0 | 1 | 0 | 165 | F | - | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,094,013 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.917885 | 0.252514 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180708,"numValue":-0.917884937405925,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180709,"numValue":0.252514437205242,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9916 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,916 | train | mutant | 4,905,596 | 225 | 4,912,184 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165A | F165A | 1 | 1 | 0 | 0 | 165 | F | A | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,093,060 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.241428 | 0.044355 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178802,"numValue":-0.241427619990389,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178803,"numValue":0.0443551067402727,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9917 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,917 | train | mutant | 4,905,596 | 225 | 4,912,184 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165A | F165A | 1 | 1 | 0 | 0 | 165 | F | A | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,094,014 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.034131 | 0.107127 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180710,"numValue":-0.0341312535893352,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180711,"numValue":0.107127302633974,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9918 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,918 | train | mutant | 4,905,597 | 225 | 4,912,185 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165C | F165C | 1 | 1 | 0 | 0 | 165 | F | C | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,093,061 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.060123 | 0.05591 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178804,"numValue":-0.0601232101567774,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178805,"numValue":0.05591006021444,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9919 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,919 | train | mutant | 4,905,597 | 225 | 4,912,185 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165C | F165C | 1 | 1 | 0 | 0 | 165 | F | C | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,094,015 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.070349 | 0.077615 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180712,"numValue":0.0703489792932703,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180713,"numValue":0.0776147073746779,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9920 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,920 | train | mutant | 4,905,598 | 225 | 4,912,186 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165D | F165D | 1 | 1 | 0 | 0 | 165 | F | D | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,093,062 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.042768 | 0.061898 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178806,"numValue":-0.0427677875640579,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178807,"numValue":0.0618979203240483,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9921 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,921 | train | mutant | 4,905,598 | 225 | 4,912,186 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165D | F165D | 1 | 1 | 0 | 0 | 165 | F | D | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,094,016 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.265545 | 0.192888 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180714,"numValue":0.265545391071512,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180715,"numValue":0.192888252001466,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9922 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,922 | train | mutant | 4,905,599 | 225 | 4,912,187 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165E | F165E | 1 | 1 | 0 | 0 | 165 | F | E | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,093,063 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.053443 | 0.049704 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12178808,"numValue":-0.0534426923177279,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12178809,"numValue":0.0497043943375954,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9923 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,923 | train | mutant | 4,905,599 | 225 | 4,912,187 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165E | F165E | 1 | 1 | 0 | 0 | 165 | F | E | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,094,017 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180716,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180717,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9924 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,924 | train | mutant | 4,905,946 | 225 | 4,912,534 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165G | F165G | 1 | 1 | 0 | 0 | 165 | F | G | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,093,984 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.612365 | 0.052132 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180650,"numValue":-0.612364895918011,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180651,"numValue":0.0521321447039615,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9925 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,925 | train | mutant | 4,905,946 | 225 | 4,912,534 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165G | F165G | 1 | 1 | 0 | 0 | 165 | F | G | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,094,918 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.208662 | 0.08748 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12182518,"numValue":-0.208662094583062,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12182519,"numValue":0.087480162701593,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||||
fireprotdb:9926 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,926 | train | mutant | 4,905,947 | 225 | 4,912,535 | 504 | 504 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | 29 | Transcriptional coactivator YAP1 | Homo sapiens | 1 | P46937 | IPR053819|IPR001202|IPR036020|IPR051583 | F165H | F165H | 1 | 1 | 0 | 0 | 165 | F | H | 5 | CONSERVATION | 1K9Q | 347 | null | 165 | A | L | false | false | 225.396918 | null | 5,093,985 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.021414 | 0.0736 | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12180652,"numValue":0.0214143520700488,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12180653,"numValue":0.0736002774082857,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":16829,"numValue":5.0,"position":165,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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