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:18414 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,414 | train | mutant | 1,166 | 358 | 1,312 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Q | K13Q | 1 | 1 | 0 | 0 | 13 | K | Q | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 2,264 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:K13Q | 58.4 | null | null | null | null | null | 44.93 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":8340,"numValue":58.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":8341,"numValue":44.93,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8342,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:18415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,415 | train | mutant | 1,166 | 358 | 1,312 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Q | K13Q | 1 | 1 | 0 | 0 | 13 | K | Q | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 2,310 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:K13Q | 62.6 | null | null | null | null | null | 48.52 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | Broom_S605.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":8478,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":8479,"numValue":48.52,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":8480,"numValue":null,"references":[],"strValue":"Unknown... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18416 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,416 | train | mutant | 1,166 | 358 | 1,312 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Q | K13Q | 1 | 1 | 0 | 0 | 13 | K | Q | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 7,223 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:K13Q | null | null | 0.1 | 0.24 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25256,"numValue":0.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25257,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25258,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:18417 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,417 | train | mutant | 1,166 | 358 | 1,312 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Q | K13Q | 1 | 1 | 0 | 0 | 13 | K | Q | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 7,247 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:K13Q | null | null | 0.45 | 0.17 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25328,"numValue":0.45,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25329,"numValue":0.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25330,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,418 | train | mutant | 1,166 | 358 | 1,312 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Q | K13Q | 1 | 1 | 0 | 0 | 13 | K | Q | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 7,278 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:K13Q | null | null | 1.03 | 0.07 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":25421,"numValue":1.03,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":25422,"numValue":0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25423,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:18419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,419 | train | mutant | 1,166 | 358 | 1,312 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Q | K13Q | 1 | 1 | 0 | 0 | 13 | K | Q | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,604 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.489262 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364696,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364697,"numValue":1.489262060377399,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364698,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,421 | train | mutant | 475,989 | 358 | 477,341 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13N | K13N | 1 | 1 | 0 | 0 | 13 | K | N | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,606 | MegaScale | null | null | null | null | 4.992794 | null | null | null | null | null | null | 2.143908 | 1.378688 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364702,"numValue":2.14390836543602,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364703,"numValue":1.3786881174328849,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364704,"numValue":4.99279431411083,"references":[],"strValue":null,"type"... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,422 | train | mutant | 475,989 | 358 | 477,341 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13N | K13N | 1 | 1 | 0 | 0 | 13 | K | N | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,496 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.225162 | 0.066627 | 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":12123674,"numValue":-0.225161898251052,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123675,"numValue":0.0666268888947089,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18423 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,423 | train | mutant | 475,990 | 358 | 477,342 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13H | K13H | 1 | 1 | 0 | 0 | 13 | K | H | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,607 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.147865 | 1.738572 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364705,"numValue":2.1478654087230264,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364706,"numValue":1.73857231739763,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364707,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18424 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,424 | train | mutant | 475,990 | 358 | 477,342 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13H | K13H | 1 | 1 | 0 | 0 | 13 | K | H | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,064,413 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.075937 | 0.08056 | 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":12121508,"numValue":-0.0759369851887703,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121509,"numValue":0.080559740474572,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18425 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,425 | train | mutant | 475,991 | 358 | 477,343 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13D | K13D | 1 | 1 | 0 | 0 | 13 | K | D | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,608 | MegaScale | null | null | null | null | 4.054449 | null | null | null | null | null | null | 1.916345 | 0.979376 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364708,"numValue":1.9163448020654996,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364709,"numValue":0.9793764665935611,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364710,"numValue":4.054448587701941,"references":[],"strValue":null,"ty... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,426 | train | mutant | 475,991 | 358 | 477,343 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13D | K13D | 1 | 1 | 0 | 0 | 13 | K | D | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,064,409 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.198801 | 0.073176 | 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":12121500,"numValue":-0.198801355232943,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121501,"numValue":0.0731763595647254,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,427 | train | mutant | 475,992 | 358 | 477,344 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13R | K13R | 1 | 1 | 0 | 0 | 13 | K | R | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,609 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | null | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364711,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364712,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364713,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18428 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,428 | train | mutant | 475,992 | 358 | 477,344 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13R | K13R | 1 | 1 | 0 | 0 | 13 | K | R | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,499 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.029049 | 0.028986 | 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":12123680,"numValue":0.0290488547135894,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123681,"numValue":0.028986250110633,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,429 | train | mutant | 475,993 | 358 | 477,345 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13T | K13T | 1 | 1 | 0 | 0 | 13 | K | T | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,610 | MegaScale | null | null | null | null | 4.973775 | null | null | null | null | null | null | 2.084699 | 1.475932 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364714,"numValue":2.0846985772596547,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364715,"numValue":1.4759317061275483,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364716,"numValue":4.973775371181442,"references":[],"strValue":null,"ty... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,430 | train | mutant | 475,993 | 358 | 477,345 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13T | K13T | 1 | 1 | 0 | 0 | 13 | K | T | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,501 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.140883 | 0.040293 | 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":12123684,"numValue":-0.140882743915525,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123685,"numValue":0.0402934191319593,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,431 | train | mutant | 475,994 | 358 | 477,346 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13S | K13S | 1 | 1 | 0 | 0 | 13 | K | S | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,611 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.068743 | 1.494253 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364717,"numValue":2.068742824102515,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364718,"numValue":1.494253150591415,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364719,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,432 | train | mutant | 475,994 | 358 | 477,346 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13S | K13S | 1 | 1 | 0 | 0 | 13 | K | S | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,500 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.167472 | 0.033967 | 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":12123682,"numValue":-0.167472066368362,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123683,"numValue":0.0339674898903104,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,433 | train | mutant | 475,995 | 358 | 477,347 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13A | K13A | 1 | 1 | 0 | 0 | 13 | K | A | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,612 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.161402 | 1.634748 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364720,"numValue":2.1614023712884287,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364721,"numValue":1.6347478667327808,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364722,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,435 | train | mutant | 475,996 | 358 | 477,348 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13G | K13G | 1 | 1 | 0 | 0 | 13 | K | G | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,613 | MegaScale | null | null | null | null | 4.475288 | null | null | null | null | null | null | 2.135693 | 1.145621 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364723,"numValue":2.1356926998137737,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364724,"numValue":1.1456209030116256,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364725,"numValue":4.475288479415979,"references":[],"strValue":null,"ty... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18436 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,436 | train | mutant | 475,996 | 358 | 477,348 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13G | K13G | 1 | 1 | 0 | 0 | 13 | K | G | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,064,412 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.192543 | 0.035814 | 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":12121506,"numValue":-0.19254273498638,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121507,"numValue":0.0358139300669723,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,437 | train | mutant | 475,997 | 358 | 477,349 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13M | K13M | 1 | 1 | 0 | 0 | 13 | K | M | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,614 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.206126 | 1.604908 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364726,"numValue":2.2061258272320776,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364727,"numValue":1.6049076474761328,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364728,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18438 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,438 | train | mutant | 475,997 | 358 | 477,349 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13M | K13M | 1 | 1 | 0 | 0 | 13 | K | M | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,495 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.087383 | 0.047417 | 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":12123672,"numValue":-0.0873827037717878,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123673,"numValue":0.0474169605787273,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,439 | train | mutant | 475,998 | 358 | 477,350 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13L | K13L | 1 | 1 | 0 | 0 | 13 | K | L | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,615 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.6113 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364729,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364730,"numValue":1.6113003345430972,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364731,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18441 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,441 | train | mutant | 475,999 | 358 | 477,351 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13V | K13V | 1 | 1 | 0 | 0 | 13 | K | V | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,616 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.152931 | 1.522794 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364732,"numValue":2.152931365589665,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364733,"numValue":1.5227939911888542,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364734,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18442 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,442 | train | mutant | 475,999 | 358 | 477,351 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13V | K13V | 1 | 1 | 0 | 0 | 13 | K | V | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,502 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.196894 | 0.038317 | 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":12123686,"numValue":-0.196894451043746,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123687,"numValue":0.0383174517675603,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18443 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,443 | train | mutant | 476,000 | 358 | 477,352 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13I | K13I | 1 | 1 | 0 | 0 | 13 | K | I | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,617 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.163823 | 1.604874 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364735,"numValue":2.163823007634141,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364736,"numValue":1.6048741612319928,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364737,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18444 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,444 | train | mutant | 476,000 | 358 | 477,352 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13I | K13I | 1 | 1 | 0 | 0 | 13 | K | I | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,064,414 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.117115 | 0.051894 | 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":12121510,"numValue":-0.117115443390798,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121511,"numValue":0.0518938183735402,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,445 | train | mutant | 476,001 | 358 | 477,353 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13W | K13W | 1 | 1 | 0 | 0 | 13 | K | W | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,618 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.589777 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364738,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364739,"numValue":1.589776519459417,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364740,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,446 | train | mutant | 476,001 | 358 | 477,353 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13W | K13W | 1 | 1 | 0 | 0 | 13 | K | W | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,503 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.122796 | 0.052776 | 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":12123688,"numValue":-0.122795674878785,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123689,"numValue":0.052775723226688,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,447 | train | mutant | 476,002 | 358 | 477,354 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Y | K13Y | 1 | 1 | 0 | 0 | 13 | K | Y | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,619 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.233819 | 1.55486 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364741,"numValue":2.233819195685604,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364742,"numValue":1.5548604134413706,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364743,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,448 | train | mutant | 476,002 | 358 | 477,354 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13Y | K13Y | 1 | 1 | 0 | 0 | 13 | K | Y | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,504 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.095513 | 0.056475 | 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":12123690,"numValue":-0.0955126539254717,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123691,"numValue":0.0564754730965505,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18449 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,449 | train | mutant | 476,003 | 358 | 477,355 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13F | K13F | 1 | 1 | 0 | 0 | 13 | K | F | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,620 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.231652 | 1.477121 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364744,"numValue":2.231651929259035,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364745,"numValue":1.477120979984846,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364746,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18450 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,450 | train | mutant | 476,003 | 358 | 477,355 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13F | K13F | 1 | 1 | 0 | 0 | 13 | K | F | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,064,411 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.12391 | 0.062049 | 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":12121504,"numValue":-0.12390951791757,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121505,"numValue":0.0620494601510693,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18451 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,451 | train | mutant | 476,004 | 358 | 477,356 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13P | K13P | 1 | 1 | 0 | 0 | 13 | K | P | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,621 | MegaScale | null | null | null | null | 2.822294 | null | null | null | null | null | null | 1.102346 | 0.051369 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364747,"numValue":1.1023456950521435,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364748,"numValue":0.0513694398230101,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364749,"numValue":2.822293910094542,"references":[],"strValue":null,"ty... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18452 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,452 | train | mutant | 476,004 | 358 | 477,356 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13P | K13P | 1 | 1 | 0 | 0 | 13 | K | P | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,065,497 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.547249 | 0.040668 | 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":12123676,"numValue":-0.547248626756043,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123677,"numValue":0.0406682677955899,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,453 | train | mutant | 476,005 | 358 | 477,357 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | K13C | K13C | 1 | 1 | 0 | 0 | 13 | K | C | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,622 | MegaScale | null | null | null | null | 4.574895 | null | null | null | null | null | null | 2.046521 | 1.123346 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364750,"numValue":2.046521032743142,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364751,"numValue":1.1233459766957088,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364752,"numValue":4.574895105261149,"references":[],"strValue":null,"typ... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,455 | train | mutant | 476,006 | 358 | 477,358 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insG13 | insG13 | 1 | 0 | 0 | 1 | 13 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,623 | MegaScale | null | null | null | null | 2.809166 | null | null | null | null | null | null | 0.997444 | 0.008912 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364753,"numValue":0.9974442172144984,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364754,"numValue":0.0089123019834411,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364755,"numValue":2.809166464045633,"references":[],"strValue":null,"ty... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18456 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,456 | train | mutant | 476,007 | 358 | 477,359 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insA13 | insA13 | 1 | 0 | 0 | 1 | 13 | - | A | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,624 | MegaScale | null | null | null | null | 2.743731 | null | null | null | null | null | null | 0.832864 | -0.085093 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364756,"numValue":0.8328636228376999,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364757,"numValue":-0.0850934506105534,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364758,"numValue":2.743730713978853,"references":[],"strValue":null,"t... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,457 | train | mutant | 476,008 | 358 | 477,360 | 67 | 66 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | delK13 | delK13 | 1 | 0 | 1 | 0 | 13 | K | - | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 501,625 | MegaScale | null | null | null | null | 3.891115 | null | null | null | null | null | null | 1.617868 | 0.75724 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364759,"numValue":1.6178684180295702,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364760,"numValue":0.7572395123833886,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364761,"numValue":3.891114529182304,"references":[],"strValue":null,"ty... | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,458 | train | mutant | 476,008 | 358 | 477,360 | 67 | 66 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | delK13 | delK13 | 1 | 0 | 1 | 0 | 13 | K | - | 9 | CONSERVATION | 1CSP | 247 | null | 13 | A | T | true | true | 137.707184 | 48.203333 | 5,064,406 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.040138 | 0.105994 | 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":12121494,"numValue":-1.04013837046358,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121495,"numValue":0.105994370799206,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,459 | train | mutant | 476,009 | 358 | 477,361 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14Q | G14Q | 1 | 1 | 0 | 0 | 14 | G | Q | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,626 | MegaScale | null | null | null | null | 3.292117 | null | null | null | null | null | null | 1.320073 | 0.253222 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364762,"numValue":1.3200728561935398,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364763,"numValue":0.2532224150354858,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364764,"numValue":3.2921165241376773,"references":[],"strValue":null,"t... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,460 | train | mutant | 476,009 | 358 | 477,361 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14Q | G14Q | 1 | 1 | 0 | 0 | 14 | G | Q | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,487 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.334879 | 0.046427 | 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":12123656,"numValue":-0.334878504319791,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123657,"numValue":0.0464265786992362,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18461 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,461 | train | mutant | 476,010 | 358 | 477,362 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14E | G14E | 1 | 1 | 0 | 0 | 14 | G | E | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,627 | MegaScale | null | null | null | null | 2.018793 | null | null | null | null | null | null | 0.52352 | -0.647601 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364765,"numValue":0.5235199293873922,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364766,"numValue":-0.6476010978599139,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364767,"numValue":2.01879304883614,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18462 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,462 | train | mutant | 476,010 | 358 | 477,362 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14E | G14E | 1 | 1 | 0 | 0 | 14 | G | E | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,064,419 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.438293 | 0.052796 | 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":12121520,"numValue":-0.43829294231391,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121521,"numValue":0.0527958288295577,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18463 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,463 | train | mutant | 476,011 | 358 | 477,363 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14N | G14N | 1 | 1 | 0 | 0 | 14 | G | N | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,628 | MegaScale | null | null | null | null | 3.283537 | null | null | null | null | null | null | 1.421771 | 0.338265 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364768,"numValue":1.4217706788267996,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364769,"numValue":0.3382653250563863,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364770,"numValue":3.283536500045092,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18464 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,464 | train | mutant | 476,011 | 358 | 477,363 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14N | G14N | 1 | 1 | 0 | 0 | 14 | G | N | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,485 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.555052 | 0.069934 | 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":12123652,"numValue":-0.555052152204198,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123653,"numValue":0.0699344384381835,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18465 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,465 | train | mutant | 476,012 | 358 | 477,364 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14H | G14H | 1 | 1 | 0 | 0 | 14 | G | H | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,629 | MegaScale | null | null | null | null | 4.177305 | null | null | null | null | null | null | 1.87128 | 0.875418 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364771,"numValue":1.8712803023957447,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364772,"numValue":0.8754182307903645,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364773,"numValue":4.177304794896544,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18466 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,466 | train | mutant | 476,012 | 358 | 477,364 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14H | G14H | 1 | 1 | 0 | 0 | 14 | G | H | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,480 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.509568 | 0.08171 | 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":12123642,"numValue":-0.50956767249678,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123643,"numValue":0.0817099551500306,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18467 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,467 | train | mutant | 476,013 | 358 | 477,365 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14D | G14D | 1 | 1 | 0 | 0 | 14 | G | D | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,630 | MegaScale | null | null | null | null | 1.248827 | null | null | null | null | null | null | 0.02443 | -1.129603 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364774,"numValue":0.024429629892017,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364775,"numValue":-1.1296031485721434,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364776,"numValue":1.248827362265839,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18468 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,468 | train | mutant | 476,013 | 358 | 477,365 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14D | G14D | 1 | 1 | 0 | 0 | 14 | G | D | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,064,418 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.665523 | 0.075232 | 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":12121518,"numValue":-0.665522933052943,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121519,"numValue":0.0752318783840419,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18469 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,469 | train | mutant | 476,014 | 358 | 477,366 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14R | G14R | 1 | 1 | 0 | 0 | 14 | G | R | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,631 | MegaScale | null | null | null | null | 4.429601 | null | null | null | null | null | null | 1.832167 | 1.022113 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364777,"numValue":1.8321673287095368,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364778,"numValue":1.0221127041085307,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364779,"numValue":4.429601269773425,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18470 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,470 | train | mutant | 476,014 | 358 | 477,366 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14R | G14R | 1 | 1 | 0 | 0 | 14 | G | R | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,488 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.239306 | 0.031113 | 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":12123658,"numValue":-0.239306355474296,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123659,"numValue":0.0311132364359403,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18472 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,472 | train | mutant | 476,015 | 358 | 477,367 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14K | G14K | 1 | 1 | 0 | 0 | 14 | G | K | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,482 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.253487 | 0.048253 | 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":12123646,"numValue":-0.253487000329307,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123647,"numValue":0.0482532260813708,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18473 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,473 | train | mutant | 476,016 | 358 | 477,368 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14T | G14T | 1 | 1 | 0 | 0 | 14 | G | T | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,633 | MegaScale | null | null | null | null | 3.197083 | null | null | null | null | null | null | 1.307647 | 0.181955 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364783,"numValue":1.307647083755526,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364784,"numValue":0.1819553928893093,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364785,"numValue":3.197083289390907,"references":[],"strValue":null,"typ... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18475 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,475 | train | mutant | 476,017 | 358 | 477,369 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14S | G14S | 1 | 1 | 0 | 0 | 14 | G | S | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,634 | MegaScale | null | null | null | null | 3.169327 | null | null | null | null | null | null | 1.258653 | 0.209761 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364786,"numValue":1.258653232549107,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364787,"numValue":0.2097612526101788,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364788,"numValue":3.169326940833769,"references":[],"strValue":null,"typ... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18476 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,476 | train | mutant | 476,017 | 358 | 477,369 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14S | G14S | 1 | 1 | 0 | 0 | 14 | G | S | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,489 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.528054 | 0.037519 | 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":12123660,"numValue":-0.528054338857181,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123661,"numValue":0.0375188214019542,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18478 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,478 | train | mutant | 476,018 | 358 | 477,370 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14A | G14A | 1 | 1 | 0 | 0 | 14 | G | A | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,064,416 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.564901 | 0.053053 | 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":12121514,"numValue":-0.564901198871706,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121515,"numValue":0.0530530247554682,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,479 | train | mutant | 476,019 | 358 | 477,371 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14M | G14M | 1 | 1 | 0 | 0 | 14 | G | M | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,636 | MegaScale | null | null | null | null | 3.688568 | null | null | null | null | null | null | 1.647528 | 0.589177 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364792,"numValue":1.6475281521059832,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364793,"numValue":0.5891768547597895,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364794,"numValue":3.688568026799883,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18480 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,480 | train | mutant | 476,019 | 358 | 477,371 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14M | G14M | 1 | 1 | 0 | 0 | 14 | G | M | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,484 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.500021 | 0.045425 | 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":12123650,"numValue":-0.500020945891946,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123651,"numValue":0.0454248253164746,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18481 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,481 | train | mutant | 476,020 | 358 | 477,372 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14L | G14L | 1 | 1 | 0 | 0 | 14 | G | L | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,637 | MegaScale | null | null | null | null | 3.242845 | null | null | null | null | null | null | 1.322587 | 0.212103 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364795,"numValue":1.3225873254753364,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364796,"numValue":0.2121034001763543,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364797,"numValue":3.242844625010035,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,482 | train | mutant | 476,020 | 358 | 477,372 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14L | G14L | 1 | 1 | 0 | 0 | 14 | G | L | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,483 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.634562 | 0.030134 | 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":12123648,"numValue":-0.634562083347722,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123649,"numValue":0.030133582042544,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18483 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,483 | train | mutant | 476,021 | 358 | 477,373 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14V | G14V | 1 | 1 | 0 | 0 | 14 | G | V | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,638 | MegaScale | null | null | null | null | 1.937305 | null | null | null | null | null | null | 0.374994 | -0.766572 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364798,"numValue":0.374994052863452,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364799,"numValue":-0.766571863769721,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364800,"numValue":1.937305359171365,"references":[],"strValue":null,"typ... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,484 | train | mutant | 476,021 | 358 | 477,373 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14V | G14V | 1 | 1 | 0 | 0 | 14 | G | V | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,491 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.94854 | 0.059103 | 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":12123664,"numValue":-0.948539776923491,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123665,"numValue":0.0591034250489438,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,485 | train | mutant | 476,022 | 358 | 477,374 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14I | G14I | 1 | 1 | 0 | 0 | 14 | G | I | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,639 | MegaScale | null | null | null | null | 2.034232 | null | null | null | null | null | null | 0.398134 | -0.594902 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364801,"numValue":0.3981342778623929,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364802,"numValue":-0.5949023915503692,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364803,"numValue":2.0342324070789464,"references":[],"strValue":null,"... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18486 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,486 | train | mutant | 476,022 | 358 | 477,374 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14I | G14I | 1 | 1 | 0 | 0 | 14 | G | I | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,481 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.824404 | 0.131137 | 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":12123644,"numValue":-0.824403503625173,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123645,"numValue":0.13113661732616,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18487 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,487 | train | mutant | 476,023 | 358 | 477,375 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14W | G14W | 1 | 1 | 0 | 0 | 14 | G | W | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,640 | MegaScale | null | null | null | null | 2.954194 | null | null | null | null | null | null | 0.881216 | 0.006653 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364804,"numValue":0.8812164026130641,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364805,"numValue":0.0066533785813065,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364806,"numValue":2.954194487819779,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18488 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,488 | train | mutant | 476,023 | 358 | 477,375 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14W | G14W | 1 | 1 | 0 | 0 | 14 | G | W | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,492 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.933742 | 0.05994 | 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":12123666,"numValue":-0.93374161159962,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123667,"numValue":0.0599395985491336,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,489 | train | mutant | 476,024 | 358 | 477,376 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14Y | G14Y | 1 | 1 | 0 | 0 | 14 | G | Y | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,641 | MegaScale | null | null | null | null | 2.828522 | null | null | null | null | null | null | 0.901637 | -0.08086 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364807,"numValue":0.9016373096170892,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364808,"numValue":-0.0808602719062648,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364809,"numValue":2.828521751002982,"references":[],"strValue":null,"t... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,490 | train | mutant | 476,024 | 358 | 477,376 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14Y | G14Y | 1 | 1 | 0 | 0 | 14 | G | Y | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,493 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.030744 | 0.15019 | 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":12123668,"numValue":-1.03074417779339,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123669,"numValue":0.150190141470946,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,491 | train | mutant | 476,025 | 358 | 477,377 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14F | G14F | 1 | 1 | 0 | 0 | 14 | G | F | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,642 | MegaScale | null | null | null | null | 2.966044 | null | null | null | null | null | null | 1.067865 | 0.082586 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364810,"numValue":1.0678650801172345,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364811,"numValue":0.0825860283533693,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364812,"numValue":2.9660440721677777,"references":[],"strValue":null,"t... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18492 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,492 | train | mutant | 476,025 | 358 | 477,377 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14F | G14F | 1 | 1 | 0 | 0 | 14 | G | F | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,064,420 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.725797 | 0.097405 | 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":12121522,"numValue":-0.725796868518619,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121523,"numValue":0.0974053897368074,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18493 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,493 | train | mutant | 476,026 | 358 | 477,378 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14P | G14P | 1 | 1 | 0 | 0 | 14 | G | P | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,643 | MegaScale | null | null | null | null | 0.625469 | null | null | null | null | null | null | -0.367471 | -1.587466 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364813,"numValue":-0.3674710980263008,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364814,"numValue":-1.587466338932411,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364815,"numValue":0.6254689711457653,"references":[],"strValue":null,"... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,494 | train | mutant | 476,026 | 358 | 477,378 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14P | G14P | 1 | 1 | 0 | 0 | 14 | G | P | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,065,486 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.925089 | 0.065351 | 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":12123654,"numValue":-0.925089332849114,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123655,"numValue":0.065350692192727,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,495 | train | mutant | 476,027 | 358 | 477,379 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14C | G14C | 1 | 1 | 0 | 0 | 14 | G | C | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,644 | MegaScale | null | null | null | null | 3.721491 | null | null | null | null | null | null | 1.51232 | 0.493927 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364816,"numValue":1.512319945996506,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364817,"numValue":0.493927342376966,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364818,"numValue":3.7214911066479455,"references":[],"strValue":null,"typ... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18496 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,496 | train | mutant | 476,027 | 358 | 477,379 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | G14C | G14C | 1 | 1 | 0 | 0 | 14 | G | C | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 5,064,417 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.522929 | 0.06474 | 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":12121516,"numValue":-0.522928698159761,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121517,"numValue":0.064740347915252,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18497 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,497 | train | mutant | 476,028 | 358 | 477,380 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insG14 | insG14 | 1 | 0 | 0 | 1 | 14 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,645 | MegaScale | null | null | null | null | 4.673203 | null | null | null | null | null | null | 1.833016 | 1.160813 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364819,"numValue":1.8330161915018637,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364820,"numValue":1.1608126934370322,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364821,"numValue":4.673203058419225,"references":[],"strValue":null,"ty... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,498 | train | mutant | 476,028 | 358 | 477,380 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insG14 | insG14 | 1 | 0 | 0 | 1 | 14 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,667 | MegaScale | null | null | null | null | 4.727195 | null | null | null | null | null | null | 1.843086 | 1.199486 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364885,"numValue":1.843086135536368,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364886,"numValue":1.199486121175778,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364887,"numValue":4.727195451419883,"references":[],"strValue":null,"type... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18499 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,499 | train | mutant | 476,029 | 358 | 477,381 | 67 | 68 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | insA14 | insA14 | 1 | 0 | 0 | 1 | 14 | - | A | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,646 | MegaScale | null | null | null | null | 2.469467 | null | null | null | null | null | null | 0.590021 | -0.311238 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364822,"numValue":0.5900209824034954,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364823,"numValue":-0.3112383287657896,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364824,"numValue":2.469467251406834,"references":[],"strValue":null,"t... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,500 | train | mutant | 476,030 | 358 | 477,382 | 67 | 66 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | delG14 | delG14 | 1 | 0 | 1 | 0 | 14 | G | - | 9 | CONSERVATION | 1CSP | 247 | null | 14 | A | T | true | true | 6.987289 | 21.5 | 501,647 | MegaScale | null | null | null | null | 1.114817 | null | null | null | null | null | null | -0.106145 | -1.270397 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364825,"numValue":-0.1061451750217915,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364826,"numValue":-1.2703966315477802,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364827,"numValue":1.1148171485442044,"references":[],"strValue":null,... | [{"id":20822,"numValue":9.0,"position":14,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,502 | train | mutant | 1,768 | 358 | 1,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15A | F15A | 1 | 1 | 0 | 0 | 15 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 3,371 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | null | 1CSP_A:F15A | 44.1 | -15.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:F15A",... | [{"datasets":[],"id":12427,"numValue":44.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12428,"numValue":-15.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12429,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18503 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,503 | train | mutant | 1,768 | 358 | 1,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15A | F15A | 1 | 1 | 0 | 0 | 15 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 7,107 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 0.35 M | 60 | 1CSP_A:F15A | null | null | null | 1.67 | 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|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":60.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type... | [{"datasets":["capriotti_S1615_map.csv"],"id":24935,"numValue":1.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24936,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,504 | train | mutant | 1,768 | 358 | 1,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15A | F15A | 1 | 1 | 0 | 0 | 15 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 7,875 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | 1CSP_A:F15A | null | null | 15.61 | -1.12 | null | -1.1 | -10.61 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 553 | ARTICLE | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | 1,999 | 10.1021/bi982487i | 10074340 | Biochemistry;38;2882-91 | 7 | Perl D|Reinstein J|Schindler T|Jacob M|Holtermann G|Schmid F X|Geeves M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":[],"id":26922,"numValue":-1.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26923,"numValue":-10.61,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26924,"numValue":15.61,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":26925,"numValue":-1.12,"referenc... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:18505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,505 | train | mutant | 1,768 | 358 | 1,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15A | F15A | 1 | 1 | 0 | 0 | 15 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 7,878 | ProTherm | 7 | CD | Thermal | Sodium cacodylate-HCl | 0.1 M | 45 | 1CSP_A:F15A | null | null | 14.44 | 0.96 | null | -0.05 | 29.16 | null | null | null | null | null | null | null | null | null | yes | DCP|DHVH|DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 553 | ARTICLE | Microsecond folding of the cold shock protein measured by a pressure-jump technique. | 1,999 | 10.1021/bi982487i | 10074340 | Biochemistry;38;2882-91 | 7 | Perl D|Reinstein J|Schindler T|Jacob M|Holtermann G|Schmid F X|Geeves M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","typ... | [{"datasets":[],"id":26937,"numValue":-0.05,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26938,"numValue":29.16,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26939,"numValue":14.44,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":2... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18506 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,506 | train | mutant | 1,768 | 358 | 1,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15A | F15A | 1 | 1 | 0 | 0 | 15 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 10,701 | ProTherm | 7 | CD | Urea | Potassium phosphate | 0.35 M | 25 | 1CSP_A:F15A | null | null | 1.22 | 2.27 | null | null | null | 1.55 | 0.78 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 300 | ARTICLE | Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. | 1,998 | 10.1002/(sici)1097-0134(19980301)30:4<401::aid-prot7>3.0.co;2-l | 9533624 | Proteins;30;401-6 | 6 | Perl D|Schindler T|Graumann P|Sieber V|Schmid F X|Marahiel M A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.35 M","type":"... | [{"datasets":[],"id":36742,"numValue":1.22,"references":[],"strValue":null,"type":"DG"},{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":36743,"numValue":2.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36744,"numValue":0.78,"references":[],"strValue":... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:18507 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,507 | train | mutant | 1,768 | 358 | 1,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15A | F15A | 1 | 1 | 0 | 0 | 15 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,657 | MegaScale | null | null | null | null | 3.456129 | null | null | null | null | null | null | 1.622576 | 0.529573 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364855,"numValue":1.6225757821099491,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364856,"numValue":0.5295729956338642,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364857,"numValue":3.4561289581735744,"references":[],"strValue":null,"t... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,508 | train | mutant | 1,768 | 358 | 1,981 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15A | F15A | 1 | 1 | 0 | 0 | 15 | F | A | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,064,422 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.355841 | 0.03835 | 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":12121526,"numValue":-0.355840956707755,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121527,"numValue":0.0383504438474371,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,509 | train | mutant | 476,031 | 358 | 477,383 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15Q | F15Q | 1 | 1 | 0 | 0 | 15 | F | Q | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,648 | MegaScale | null | null | null | null | 4.371127 | null | null | null | null | null | null | 1.976863 | 1.079878 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364828,"numValue":1.97686329305542,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364829,"numValue":1.0798783806761718,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364830,"numValue":4.371126908639711,"references":[],"strValue":null,"type... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,510 | train | mutant | 476,031 | 358 | 477,383 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15Q | F15Q | 1 | 1 | 0 | 0 | 15 | F | Q | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,473 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.200273 | 0.04134 | 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":12123628,"numValue":-0.200272781141558,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123629,"numValue":0.0413396894352908,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18513 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,513 | train | mutant | 476,033 | 358 | 477,385 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15N | F15N | 1 | 1 | 0 | 0 | 15 | F | N | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,650 | MegaScale | null | null | null | null | 3.471257 | null | null | null | null | null | null | 1.59912 | 0.348862 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364834,"numValue":1.5991197920402755,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364835,"numValue":0.3488619917469134,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364836,"numValue":3.471256796069882,"references":[],"strValue":null,"ty... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,514 | train | mutant | 476,033 | 358 | 477,385 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15N | F15N | 1 | 1 | 0 | 0 | 15 | F | N | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,471 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.411401 | 0.063388 | 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":12123624,"numValue":-0.411401238463429,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123625,"numValue":0.0633878505117146,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18515 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,515 | train | mutant | 476,034 | 358 | 477,386 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15H | F15H | 1 | 1 | 0 | 0 | 15 | F | H | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,651 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.561344 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364837,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364838,"numValue":1.5613435608812458,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364839,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:18516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,516 | train | mutant | 476,034 | 358 | 477,386 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15H | F15H | 1 | 1 | 0 | 0 | 15 | F | H | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,466 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.190525 | 0.075786 | 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":12123614,"numValue":-0.190524814503119,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123615,"numValue":0.0757859171598867,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18518 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,518 | train | mutant | 476,035 | 358 | 477,387 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15D | F15D | 1 | 1 | 0 | 0 | 15 | F | D | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,064,424 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.523123 | 0.058076 | 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":12121530,"numValue":-0.523122762001981,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121531,"numValue":0.0580755368358504,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,519 | train | mutant | 476,036 | 358 | 477,388 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15R | F15R | 1 | 1 | 0 | 0 | 15 | F | R | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,653 | MegaScale | null | null | null | null | 3.261803 | null | null | null | null | null | null | 1.239624 | 0.296025 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364843,"numValue":1.239623982296802,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364844,"numValue":0.2960253709285059,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364845,"numValue":3.2618033757957545,"references":[],"strValue":null,"ty... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,520 | train | mutant | 476,036 | 358 | 477,388 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15R | F15R | 1 | 1 | 0 | 0 | 15 | F | R | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,474 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.352004 | 0.030232 | 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":12123630,"numValue":-0.352004454390796,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123631,"numValue":0.0302319142649988,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18521 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,521 | train | mutant | 476,037 | 358 | 477,389 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15K | F15K | 1 | 1 | 0 | 0 | 15 | F | K | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,654 | MegaScale | null | null | null | null | 3.20983 | null | null | null | null | null | null | 1.298086 | 0.296268 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364846,"numValue":1.298086278953258,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364847,"numValue":0.2962678427240127,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364848,"numValue":3.2098298285404026,"references":[],"strValue":null,"ty... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,522 | train | mutant | 476,037 | 358 | 477,389 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15K | F15K | 1 | 1 | 0 | 0 | 15 | F | K | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,468 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.344762 | 0.041256 | 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":12123618,"numValue":-0.344762021239932,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123619,"numValue":0.041256347479283,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,523 | train | mutant | 476,038 | 358 | 477,390 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15T | F15T | 1 | 1 | 0 | 0 | 15 | F | T | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 501,655 | MegaScale | null | null | null | null | 4.019519 | null | null | null | null | null | null | 1.803623 | 0.831062 | null | null | null | null | null | TRYPSIN_ML|CHYMOTRYPSIN_ML|DG | 1909 | ARTICLE | Mega-scale experimental analysis of protein folding stability in biology and design. | 2,023 | 10.1038/s41586-023-06328-6 | 37468638 | Nature;620;434-444 | 1 | Tsuboyama Kotaro | [{"datasets":[],"id":2364849,"numValue":1.8036231009968768,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364850,"numValue":0.8310616364201167,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364851,"numValue":4.019518939395159,"references":[],"strValue":null,"ty... | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:18524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18,524 | train | mutant | 476,038 | 358 | 477,390 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | F15T | F15T | 1 | 1 | 0 | 0 | 15 | F | T | 5 | CONSERVATION | 1CSP | 247 | null | 15 | A | E | false | true | 55.974195 | 20.403636 | 5,065,476 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.186439 | 0.035862 | 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":12123634,"numValue":-0.186438678861939,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123635,"numValue":0.0358618572118239,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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