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:20289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,289 | train | mutant | 7,432 | 358 | 8,115 | 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 | E43S|A46K|S48K | E43S|A46K|S48K | 3 | 3 | 0 | 0 | 43 | E | S | 7 | CONSERVATION | 1CSP | 247 | null | 43|46|48 | A | T|E | false | false | 62.631063 | 32.584333 | 16,711 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:E43S 1CSP_A:A46K 1CSP_A:S48K | null | null | null | -2.61 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"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":61485,"numValue":-2.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61486,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRang... | |||||||||||||
fireprotdb:20290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,290 | train | mutant | 7,433 | 358 | 8,116 | 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 | E43S|A46K|S48R | E43S|A46K|S48R | 3 | 3 | 0 | 0 | 43 | E | S | 7 | CONSERVATION | 1CSP | 247 | null | 43|46|48 | A | T|E | false | false | 62.631063 | 32.584333 | 15,858 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:E43S 1CSP_A:A46K 1CSP_A:S48R | 69.9 | 16.1 | null | null | null | null | 52.58 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"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","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type"... | [{"datasets":[],"id":58253,"numValue":69.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58254,"numValue":16.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58255,"numValue":52.58,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58256,"numValue":null,"references"... | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:20291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,291 | train | mutant | 7,433 | 358 | 8,116 | 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 | E43S|A46K|S48R | E43S|A46K|S48R | 3 | 3 | 0 | 0 | 43 | E | S | 7 | CONSERVATION | 1CSP | 247 | null | 43|46|48 | A | T|E | false | false | 62.631063 | 32.584333 | 16,523 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E43S 1CSP_A:A46K 1CSP_A:S48R | 69.9 | 16.1 | null | -2.71 | 52.8 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60565,"numValue":69.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60566,"numValue":16.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60567,"numValue":52.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60568,"numValue":-2.71,"references":[... | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRang... | ||||||||||
fireprotdb:20292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,292 | train | mutant | 7,433 | 358 | 8,116 | 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 | E43S|A46K|S48R | E43S|A46K|S48R | 3 | 3 | 0 | 0 | 43 | E | S | 7 | CONSERVATION | 1CSP | 247 | null | 43|46|48 | A | T|E | false | false | 62.631063 | 32.584333 | 16,559 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E43S 1CSP_A:A46K 1CSP_A:S48R | 69.9 | 16.1 | null | -1.58 | 52.8 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60780,"numValue":69.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60781,"numValue":16.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60782,"numValue":52.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60783,"numValue":-1.58,"references":[... | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRang... | ||||||||||
fireprotdb:20293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,293 | train | mutant | 7,433 | 358 | 8,116 | 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 | E43S|A46K|S48R | E43S|A46K|S48R | 3 | 3 | 0 | 0 | 43 | E | S | 7 | CONSERVATION | 1CSP | 247 | null | 43|46|48 | A | T|E | false | false | 62.631063 | 32.584333 | 16,594 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E43S 1CSP_A:A46K 1CSP_A:S48R | 69.9 | 15.6 | null | -1.13 | 52.8 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":60990,"numValue":69.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60991,"numValue":15.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60992,"numValue":52.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60993,"numValue":-1.13,"references":[... | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRang... | ||||||||||
fireprotdb:20294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,294 | train | mutant | 7,433 | 358 | 8,116 | 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 | E43S|A46K|S48R | E43S|A46K|S48R | 3 | 3 | 0 | 0 | 43 | E | S | 7 | CONSERVATION | 1CSP | 247 | null | 43|46|48 | A | T|E | false | false | 62.631063 | 32.584333 | 16,604 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E43S 1CSP_A:A46K 1CSP_A:S48R | 69.9 | 16.1 | null | -1.13 | 52.8 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate/HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.1M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":61050,"numValue":69.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61051,"numValue":16.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61052,"numValue":52.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61053,"numValue":-1.13,"references":[... | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRang... | ||||||||||
fireprotdb:20295 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,295 | train | mutant | 7,433 | 358 | 8,116 | 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 | E43S|A46K|S48R | E43S|A46K|S48R | 3 | 3 | 0 | 0 | 43 | E | S | 7 | CONSERVATION | 1CSP | 247 | null | 43|46|48 | A | T|E | false | false | 62.631063 | 32.584333 | 16,712 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:E43S 1CSP_A:A46K 1CSP_A:S48R | null | null | null | -2.7 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 186 | ARTICLE | Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions. | 2,005 | 10.1016/j.jmb.2005.02.014 | 15784264 | J Mol Biol;347;1063-76 | 3 | Wunderlich Michael|Martin Andreas|Schmid Franz X | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":70.0,"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":61487,"numValue":-2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61488,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRang... | |||||||||||||
fireprotdb:20296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,296 | train | mutant | 476,622 | 358 | 477,974 | 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 | E43N | E43N | 1 | 1 | 0 | 0 | 43 | E | N | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,265 | 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":2366678,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366679,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366680,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,297 | train | mutant | 476,622 | 358 | 477,974 | 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 | E43N | E43N | 1 | 1 | 0 | 0 | 43 | E | N | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,140 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.043207 | 0.096015 | 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":12122962,"numValue":0.043206805630035,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122963,"numValue":0.0960154780021213,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,298 | train | mutant | 476,623 | 358 | 477,975 | 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 | E43H | E43H | 1 | 1 | 0 | 0 | 43 | E | H | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,266 | 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":2366681,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366682,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366683,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,299 | train | mutant | 476,623 | 358 | 477,975 | 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 | E43H | E43H | 1 | 1 | 0 | 0 | 43 | E | H | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,135 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.008478 | 0.117904 | 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":12122952,"numValue":0.00847771942845868,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122953,"numValue":0.117903597743683,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,300 | train | mutant | 476,624 | 358 | 477,976 | 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 | E43D | E43D | 1 | 1 | 0 | 0 | 43 | E | D | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,267 | 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":2366684,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366685,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366686,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20301 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,301 | train | mutant | 476,624 | 358 | 477,976 | 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 | E43D | E43D | 1 | 1 | 0 | 0 | 43 | E | D | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,064,653 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.061536 | 0.102821 | 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":12121988,"numValue":-0.0615361477947041,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121989,"numValue":0.102820715493268,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,302 | train | mutant | 476,625 | 358 | 477,977 | 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 | E43R | E43R | 1 | 1 | 0 | 0 | 43 | E | R | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,268 | 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":2366687,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366688,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366689,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,303 | train | mutant | 476,625 | 358 | 477,977 | 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 | E43R | E43R | 1 | 1 | 0 | 0 | 43 | E | R | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,143 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.065922 | 0.049324 | 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":12122968,"numValue":0.0659222114347642,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122969,"numValue":0.0493237850324643,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,304 | train | mutant | 476,626 | 358 | 477,978 | 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 | E43T | E43T | 1 | 1 | 0 | 0 | 43 | E | T | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,270 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.243922 | 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":2366693,"numValue":2.2439218342983343,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366694,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366695,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,305 | train | mutant | 476,626 | 358 | 477,978 | 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 | E43T | E43T | 1 | 1 | 0 | 0 | 43 | E | T | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,145 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.085291 | 0.062755 | 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":12122972,"numValue":0.0852911813256118,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122973,"numValue":0.0627553643103959,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,306 | train | mutant | 476,627 | 358 | 477,979 | 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 | E43A | E43A | 1 | 1 | 0 | 0 | 43 | E | A | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,272 | 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":2366699,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366700,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366701,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,307 | train | mutant | 476,627 | 358 | 477,979 | 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 | E43A | E43A | 1 | 1 | 0 | 0 | 43 | E | A | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,064,651 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.006968 | 0.052429 | 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":12121984,"numValue":0.00696765248931344,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121985,"numValue":0.0524293830566932,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20308 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,308 | train | mutant | 476,628 | 358 | 477,980 | 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 | E43G | E43G | 1 | 1 | 0 | 0 | 43 | E | G | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,273 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.201687 | 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":2366702,"numValue":2.201687477140991,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366703,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366704,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,309 | train | mutant | 476,628 | 358 | 477,980 | 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 | E43G | E43G | 1 | 1 | 0 | 0 | 43 | E | G | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,134 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.013959 | 0.041035 | 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":12122950,"numValue":0.0139592256165744,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122951,"numValue":0.041034535697044,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,310 | train | mutant | 476,629 | 358 | 477,981 | 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 | E43M | E43M | 1 | 1 | 0 | 0 | 43 | E | M | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,274 | 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":2366705,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366706,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366707,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,311 | train | mutant | 476,629 | 358 | 477,981 | 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 | E43M | E43M | 1 | 1 | 0 | 0 | 43 | E | M | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,139 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.013649 | 0.046284 | 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":12122960,"numValue":-0.0136488706729482,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122961,"numValue":0.0462840178305662,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,312 | train | mutant | 476,630 | 358 | 477,982 | 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 | E43L | E43L | 1 | 1 | 0 | 0 | 43 | E | L | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,275 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.236204 | 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":2366708,"numValue":2.2362040366376084,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366709,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366710,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,313 | train | mutant | 476,630 | 358 | 477,982 | 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 | E43L | E43L | 1 | 1 | 0 | 0 | 43 | E | L | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,138 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.074917 | 0.032935 | 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":12122958,"numValue":-0.0749169846527026,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122959,"numValue":0.0329351732924483,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20314 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,314 | train | mutant | 476,631 | 358 | 477,983 | 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 | E43V | E43V | 1 | 1 | 0 | 0 | 43 | E | V | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,276 | 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":2366711,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366712,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366713,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,315 | train | mutant | 476,631 | 358 | 477,983 | 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 | E43V | E43V | 1 | 1 | 0 | 0 | 43 | E | V | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,146 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.029591 | 0.047852 | 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":12122974,"numValue":0.0295910558403986,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122975,"numValue":0.0478519113785752,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,317 | train | mutant | 476,632 | 358 | 477,984 | 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 | E43I | E43I | 1 | 1 | 0 | 0 | 43 | E | I | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,136 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.025315 | 0.058584 | 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":12122954,"numValue":-0.0253147817950206,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122955,"numValue":0.0585842122685517,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,318 | train | mutant | 476,633 | 358 | 477,985 | 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 | E43W | E43W | 1 | 1 | 0 | 0 | 43 | E | W | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,278 | 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":2366717,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366718,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366719,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,319 | train | mutant | 476,633 | 358 | 477,985 | 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 | E43W | E43W | 1 | 1 | 0 | 0 | 43 | E | W | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,147 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.160118 | 0.041728 | 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":12122976,"numValue":-0.160118003573743,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122977,"numValue":0.0417277373842709,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,320 | train | mutant | 476,634 | 358 | 477,986 | 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 | E43Y | E43Y | 1 | 1 | 0 | 0 | 43 | E | Y | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,279 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.724706 | 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":2366720,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366721,"numValue":1.7247062017509371,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366722,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,321 | train | mutant | 476,634 | 358 | 477,986 | 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 | E43Y | E43Y | 1 | 1 | 0 | 0 | 43 | E | Y | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,148 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.020678 | 0.084815 | 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":12122978,"numValue":-0.0206778581313578,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122979,"numValue":0.08481497662555,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,323 | train | mutant | 476,635 | 358 | 477,987 | 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 | E43F | E43F | 1 | 1 | 0 | 0 | 43 | E | F | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,065,133 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.105557 | 0.065896 | 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":12122948,"numValue":-0.105556868464644,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122949,"numValue":0.0658957147281147,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,324 | train | mutant | 476,636 | 358 | 477,988 | 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 | E43P | E43P | 1 | 1 | 0 | 0 | 43 | E | P | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,281 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.17154 | 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":2366726,"numValue":2.171540296639251,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366727,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366728,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,327 | train | mutant | 476,637 | 358 | 477,989 | 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 | E43C | E43C | 1 | 1 | 0 | 0 | 43 | E | C | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 5,064,652 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.045577 | 0.100432 | 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":12121986,"numValue":0.0455767888359072,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121987,"numValue":0.100432086456791,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20329 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,329 | train | mutant | 476,639 | 358 | 477,991 | 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 | insA43 | insA43 | 1 | 0 | 0 | 1 | 43 | - | A | 7 | CONSERVATION | 1CSP | 247 | null | 43 | A | T | false | false | 135.470932 | 42.28 | 502,284 | MegaScale | null | null | null | null | 2.810526 | null | null | null | null | null | null | 0.879421 | -0.12154 | 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":2366735,"numValue":0.8794214031313614,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366736,"numValue":-0.1215404156358248,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366737,"numValue":2.810525674203416,"references":[],"strValue":null,"t... | [{"id":20851,"numValue":7.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20330 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,330 | train | mutant | 476,640 | 358 | 477,992 | 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 | G44Q | G44Q | 1 | 1 | 0 | 0 | 44 | G | Q | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,286 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.406637 | 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":2366741,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366742,"numValue":1.4066368883490132,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366743,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,331 | train | mutant | 476,640 | 358 | 477,992 | 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 | G44Q | G44Q | 1 | 1 | 0 | 0 | 44 | G | Q | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,126 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.13381 | 0.040451 | 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":12122934,"numValue":-0.133810208629057,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122935,"numValue":0.0404506206577525,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20332 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,332 | train | mutant | 476,641 | 358 | 477,993 | 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 | G44E | G44E | 1 | 1 | 0 | 0 | 44 | G | E | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,287 | MegaScale | null | null | null | null | 4.34076 | null | null | null | null | null | null | 1.996667 | 0.99668 | 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":2366744,"numValue":1.9966674668977944,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366745,"numValue":0.9966801487976356,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366746,"numValue":4.340760141340795,"references":[],"strValue":null,"ty... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,334 | train | mutant | 476,642 | 358 | 477,994 | 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 | G44N | G44N | 1 | 1 | 0 | 0 | 44 | G | N | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,288 | MegaScale | null | null | null | null | 4.952446 | null | null | null | null | null | null | 2.146392 | 1.345825 | 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":2366747,"numValue":2.146391562468088,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366748,"numValue":1.3458247887146455,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366749,"numValue":4.952445633013643,"references":[],"strValue":null,"typ... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20335 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,335 | train | mutant | 476,642 | 358 | 477,994 | 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 | G44N | G44N | 1 | 1 | 0 | 0 | 44 | G | N | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,124 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.002211 | 0.073628 | 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":12122930,"numValue":-0.00221051228622223,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122931,"numValue":0.0736279076072106,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,336 | train | mutant | 476,643 | 358 | 477,995 | 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 | G44H | G44H | 1 | 1 | 0 | 0 | 44 | G | H | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,289 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.150812 | 1.571027 | 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":2366750,"numValue":2.150811948141291,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366751,"numValue":1.571027335861501,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366752,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20337 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,337 | train | mutant | 476,643 | 358 | 477,995 | 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 | G44H | G44H | 1 | 1 | 0 | 0 | 44 | G | H | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,119 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.137626 | 0.05035 | 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":12122920,"numValue":-0.137626470406215,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122921,"numValue":0.0503495326551362,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,338 | train | mutant | 476,644 | 358 | 477,996 | 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 | G44D | G44D | 1 | 1 | 0 | 0 | 44 | G | D | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,290 | MegaScale | null | null | null | null | 4.83984 | null | null | null | null | null | null | 2.124504 | 1.30022 | 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":2366753,"numValue":2.1245040265684807,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366754,"numValue":1.300220088412777,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366755,"numValue":4.839839808587739,"references":[],"strValue":null,"typ... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,339 | train | mutant | 476,644 | 358 | 477,996 | 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 | G44D | G44D | 1 | 1 | 0 | 0 | 44 | G | D | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,064,657 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.084924 | 0.054178 | 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":12121996,"numValue":-0.0849237848607264,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121997,"numValue":0.0541784785039027,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,340 | train | mutant | 476,645 | 358 | 477,997 | 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 | G44R | G44R | 1 | 1 | 0 | 0 | 44 | G | R | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,291 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.158061 | 1.455882 | 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":2366756,"numValue":2.158060889272321,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366757,"numValue":1.455881694221093,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366758,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,341 | train | mutant | 476,645 | 358 | 477,997 | 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 | G44R | G44R | 1 | 1 | 0 | 0 | 44 | G | R | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,127 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.143704 | 0.030639 | 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":12122936,"numValue":-0.143704152493944,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122937,"numValue":0.0306385651101058,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,342 | train | mutant | 476,646 | 358 | 477,998 | 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 | G44K | G44K | 1 | 1 | 0 | 0 | 44 | G | K | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,292 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.501783 | 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":2366759,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366760,"numValue":1.501783119702497,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366761,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20344 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,344 | train | mutant | 476,647 | 358 | 477,999 | 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 | G44T | G44T | 1 | 1 | 0 | 0 | 44 | G | T | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,293 | MegaScale | null | null | null | null | 4.527354 | null | null | null | null | null | null | 1.983655 | 1.11998 | 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":2366762,"numValue":1.983655192709322,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366763,"numValue":1.119979546007274,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366764,"numValue":4.527353589407063,"references":[],"strValue":null,"type... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20345 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,345 | train | mutant | 476,647 | 358 | 477,999 | 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 | G44T | G44T | 1 | 1 | 0 | 0 | 44 | G | T | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,129 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.411204 | 0.046563 | 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":12122940,"numValue":-0.411204353212631,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122941,"numValue":0.0465626073936975,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20346 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,346 | train | mutant | 476,648 | 358 | 478,000 | 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 | G44S | G44S | 1 | 1 | 0 | 0 | 44 | G | S | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,294 | MegaScale | null | null | null | null | 4.802867 | null | null | null | null | null | null | null | 1.303333 | 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":2366765,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366766,"numValue":1.30333295345129,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366767,"numValue":4.802867453963721,"references":[],"strValue":null,"type":"DG"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20348 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,348 | train | mutant | 476,649 | 358 | 478,001 | 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 | G44A | G44A | 1 | 1 | 0 | 0 | 44 | G | A | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,295 | MegaScale | null | null | null | null | 4.90348 | null | null | null | null | null | null | 2.182476 | 1.319215 | 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":2366768,"numValue":2.182476118026381,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366769,"numValue":1.319214628370222,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366770,"numValue":4.903480367965848,"references":[],"strValue":null,"type... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,349 | train | mutant | 476,649 | 358 | 478,001 | 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 | G44A | G44A | 1 | 1 | 0 | 0 | 44 | G | A | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,064,655 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.194942 | 0.044653 | 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":12121992,"numValue":-0.194942158977418,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121993,"numValue":0.0446526793905242,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,350 | train | mutant | 476,650 | 358 | 478,002 | 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 | G44M | G44M | 1 | 1 | 0 | 0 | 44 | G | M | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,296 | MegaScale | null | null | null | null | 4.739614 | null | null | null | null | null | null | 2.061618 | 1.293079 | 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":2366771,"numValue":2.061618251910088,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366772,"numValue":1.293078759446136,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366773,"numValue":4.739613966572192,"references":[],"strValue":null,"type... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,351 | train | mutant | 476,650 | 358 | 478,002 | 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 | G44M | G44M | 1 | 1 | 0 | 0 | 44 | G | M | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,123 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.307086 | 0.04949 | 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":12122928,"numValue":-0.30708640312298,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122929,"numValue":0.0494897819928259,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20352 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,352 | train | mutant | 476,651 | 358 | 478,003 | 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 | G44L | G44L | 1 | 1 | 0 | 0 | 44 | G | L | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,297 | MegaScale | null | null | null | null | 4.454698 | null | null | null | null | null | null | 2.041622 | 1.061686 | 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":2366774,"numValue":2.041622258858561,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366775,"numValue":1.0616858558001103,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366776,"numValue":4.454698021465639,"references":[],"strValue":null,"typ... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20354 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,354 | train | mutant | 476,652 | 358 | 478,004 | 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 | G44V | G44V | 1 | 1 | 0 | 0 | 44 | G | V | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,298 | MegaScale | null | null | null | null | 3.060106 | null | null | null | null | null | null | 1.185193 | 0.163196 | 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":2366777,"numValue":1.185193185764705,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366778,"numValue":0.1631963206305682,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366779,"numValue":3.060106388028536,"references":[],"strValue":null,"typ... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,355 | train | mutant | 476,652 | 358 | 478,004 | 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 | G44V | G44V | 1 | 1 | 0 | 0 | 44 | G | V | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,130 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.009742 | 0.076172 | 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":12122942,"numValue":-1.00974232382128,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122943,"numValue":0.076171714115501,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20356 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,356 | train | mutant | 476,653 | 358 | 478,005 | 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 | G44I | G44I | 1 | 1 | 0 | 0 | 44 | G | I | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,299 | MegaScale | null | null | null | null | 2.614263 | null | null | null | null | null | null | 1.083094 | -0.235723 | 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":2366780,"numValue":1.0830938400066703,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366781,"numValue":-0.2357230702604884,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366782,"numValue":2.614263383574396,"references":[],"strValue":null,"t... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,357 | train | mutant | 476,653 | 358 | 478,005 | 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 | G44I | G44I | 1 | 1 | 0 | 0 | 44 | G | I | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,120 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.04707 | 0.139837 | 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":12122922,"numValue":-1.04707031986738,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122923,"numValue":0.13983679868753,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20358 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,358 | train | mutant | 476,654 | 358 | 478,006 | 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 | G44W | G44W | 1 | 1 | 0 | 0 | 44 | G | W | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,300 | MegaScale | null | null | null | null | 4.968111 | null | null | null | null | null | null | 2.05239 | 1.353483 | 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":2366783,"numValue":2.0523900164665587,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366784,"numValue":1.3534828406021937,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366785,"numValue":4.96811062613569,"references":[],"strValue":null,"typ... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20359 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,359 | train | mutant | 476,654 | 358 | 478,006 | 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 | G44W | G44W | 1 | 1 | 0 | 0 | 44 | G | W | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,131 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.642772 | 0.053648 | 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":12122944,"numValue":-0.642771584956323,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122945,"numValue":0.0536479432882155,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20360 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,360 | train | mutant | 476,655 | 358 | 478,007 | 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 | G44Y | G44Y | 1 | 1 | 0 | 0 | 44 | G | Y | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,301 | MegaScale | null | null | null | null | 4.926712 | null | null | null | null | null | null | 2.233014 | 1.270458 | 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":2366786,"numValue":2.23301378624308,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366787,"numValue":1.2704576002299308,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366788,"numValue":4.926711651961819,"references":[],"strValue":null,"type... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20361 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,361 | train | mutant | 476,655 | 358 | 478,007 | 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 | G44Y | G44Y | 1 | 1 | 0 | 0 | 44 | G | Y | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,132 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.575751 | 0.068039 | 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":12122946,"numValue":-0.575751293569832,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122947,"numValue":0.0680388198833004,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,362 | train | mutant | 476,656 | 358 | 478,008 | 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 | G44F | G44F | 1 | 1 | 0 | 0 | 44 | G | F | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,302 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.225823 | 1.348643 | 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":2366789,"numValue":2.225823418455054,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366790,"numValue":1.348642796520905,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366791,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,363 | train | mutant | 476,656 | 358 | 478,008 | 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 | G44F | G44F | 1 | 1 | 0 | 0 | 44 | G | F | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,064,659 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.601556 | 0.050292 | 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":12122000,"numValue":-0.601555528418239,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122001,"numValue":0.0502917060462725,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,364 | train | mutant | 476,657 | 358 | 478,009 | 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 | G44P | G44P | 1 | 1 | 0 | 0 | 44 | G | P | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,303 | MegaScale | null | null | null | null | 3.124036 | null | null | null | null | null | null | 1.30458 | 0.151901 | 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":2366792,"numValue":1.3045798245191518,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366793,"numValue":0.1519007474386376,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366794,"numValue":3.124036062030288,"references":[],"strValue":null,"ty... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20365 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,365 | train | mutant | 476,657 | 358 | 478,009 | 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 | G44P | G44P | 1 | 1 | 0 | 0 | 44 | G | P | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,065,125 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.803725 | 0.06138 | 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":12122932,"numValue":-0.803725154814062,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122933,"numValue":0.0613798662934475,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20366 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,366 | train | mutant | 476,658 | 358 | 478,010 | 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 | G44C | G44C | 1 | 1 | 0 | 0 | 44 | G | C | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,304 | MegaScale | null | null | null | null | 4.501585 | null | null | null | null | null | null | 2.006947 | 1.022206 | 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":2366795,"numValue":2.006946719630692,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366796,"numValue":1.0222063205817382,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366797,"numValue":4.5015845221526,"references":[],"strValue":null,"type"... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20367 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,367 | train | mutant | 476,658 | 358 | 478,010 | 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 | G44C | G44C | 1 | 1 | 0 | 0 | 44 | G | C | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,064,656 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.307767 | 0.054335 | 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":12121994,"numValue":-0.307767221279947,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121995,"numValue":0.0543347661386564,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20368 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,368 | train | mutant | 476,659 | 358 | 478,011 | 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 | insG44 | insG44 | 1 | 0 | 0 | 1 | 44 | - | G | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,305 | MegaScale | null | null | null | null | 2.624181 | null | null | null | null | null | null | 0.798669 | -0.18027 | 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":2366798,"numValue":0.7986689641468852,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366799,"numValue":-0.1802697078380702,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366800,"numValue":2.624180795269411,"references":[],"strValue":null,"t... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20369 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,369 | train | mutant | 476,659 | 358 | 478,011 | 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 | insG44 | insG44 | 1 | 0 | 0 | 1 | 44 | - | G | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,327 | MegaScale | null | null | null | null | 2.666445 | null | null | null | null | null | null | 0.807319 | -0.179106 | 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":2366864,"numValue":0.8073189387796618,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366865,"numValue":-0.1791059985528723,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366866,"numValue":2.6664452687901,"references":[],"strValue":null,"typ... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20370 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,370 | train | mutant | 476,660 | 358 | 478,012 | 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 | insA44 | insA44 | 1 | 0 | 0 | 1 | 44 | - | A | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,306 | MegaScale | null | null | null | null | 3.459466 | null | null | null | null | null | null | 1.224805 | 0.409714 | 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":2366801,"numValue":1.2248051175937709,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366802,"numValue":0.4097138873746476,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366803,"numValue":3.4594663344323724,"references":[],"strValue":null,"t... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20371 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,371 | train | mutant | 476,661 | 358 | 478,013 | 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 | delG44 | delG44 | 1 | 0 | 1 | 0 | 44 | G | - | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 502,307 | MegaScale | null | null | null | null | 1.376768 | null | null | null | null | null | null | 0.057617 | -1.077427 | 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":2366804,"numValue":0.0576173823872707,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366805,"numValue":-1.0774269188284733,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366806,"numValue":1.3767676275467242,"references":[],"strValue":null,"... | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20372 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,372 | train | mutant | 476,661 | 358 | 478,013 | 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 | delG44 | delG44 | 1 | 0 | 1 | 0 | 44 | G | - | 6 | CONSERVATION | 1CSP | 247 | null | 44 | A | T | false | false | 36.416157 | 27.8475 | 5,064,654 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.009229 | 0.081648 | 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":12121990,"numValue":-1.00922895012995,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121991,"numValue":0.081647638821429,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20852,"numValue":6.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20373 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,373 | train | mutant | 476,662 | 358 | 478,014 | 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 | Q45E | Q45E | 1 | 1 | 0 | 0 | 45 | Q | E | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,308 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.120909 | 1.628304 | 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":2366807,"numValue":2.1209091306204826,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366808,"numValue":1.628303731044883,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366809,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20374 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,374 | train | mutant | 476,662 | 358 | 478,014 | 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 | Q45E | Q45E | 1 | 1 | 0 | 0 | 45 | Q | E | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,664 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.009244 | 0.068153 | 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":12122010,"numValue":-0.00924440654215946,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122011,"numValue":0.0681527802558809,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20375 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,375 | train | mutant | 476,663 | 358 | 478,015 | 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 | Q45N | Q45N | 1 | 1 | 0 | 0 | 45 | Q | N | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,309 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.198714 | 1.527766 | 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":2366810,"numValue":2.1987139402260647,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366811,"numValue":1.5277655813629478,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366812,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20376 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,376 | train | mutant | 476,663 | 358 | 478,015 | 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 | Q45N | Q45N | 1 | 1 | 0 | 0 | 45 | Q | N | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,672 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.048474 | 0.087692 | 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":12122026,"numValue":-0.0484742527760054,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122027,"numValue":0.0876920160209393,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20377 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,377 | train | mutant | 476,664 | 358 | 478,016 | 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 | Q45H | Q45H | 1 | 1 | 0 | 0 | 45 | Q | H | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,310 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.220811 | 1.548229 | 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":2366813,"numValue":2.2208109802525,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366814,"numValue":1.5482292802887088,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366815,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20378 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,378 | train | mutant | 476,664 | 358 | 478,016 | 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 | Q45H | Q45H | 1 | 1 | 0 | 0 | 45 | Q | H | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,667 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.164797 | 0.111174 | 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":12122016,"numValue":-0.164796635016391,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122017,"numValue":0.111173740929555,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20379 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,379 | train | mutant | 476,665 | 358 | 478,017 | 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 | Q45D | Q45D | 1 | 1 | 0 | 0 | 45 | Q | D | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,311 | 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":2366816,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366817,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366818,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20380 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,380 | train | mutant | 476,665 | 358 | 478,017 | 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 | Q45D | Q45D | 1 | 1 | 0 | 0 | 45 | Q | D | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,663 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.120753 | 0.090519 | 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":12122008,"numValue":-0.120753220407886,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122009,"numValue":0.0905190674165153,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20381 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,381 | train | mutant | 476,666 | 358 | 478,018 | 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 | Q45R | Q45R | 1 | 1 | 0 | 0 | 45 | Q | R | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,312 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.242919 | 1.367984 | 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":2366819,"numValue":2.2429187892441025,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366820,"numValue":1.3679838167939715,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366821,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20382 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,382 | train | mutant | 476,666 | 358 | 478,018 | 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 | Q45R | Q45R | 1 | 1 | 0 | 0 | 45 | Q | R | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,065,113 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.17123 | 0.03426 | 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":12122908,"numValue":-0.171230059924878,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122909,"numValue":0.034260437969707,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20383 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,383 | train | mutant | 476,667 | 358 | 478,019 | 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 | Q45K | Q45K | 1 | 1 | 0 | 0 | 45 | Q | K | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,313 | MegaScale | null | null | null | null | 4.85616 | null | null | null | null | null | null | 2.133055 | 1.274207 | 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":2366822,"numValue":2.133055322667742,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366823,"numValue":1.2742068352435152,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366824,"numValue":4.856159792628066,"references":[],"strValue":null,"typ... | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20384 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,384 | train | mutant | 476,667 | 358 | 478,019 | 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 | Q45K | Q45K | 1 | 1 | 0 | 0 | 45 | Q | K | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,669 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.172173 | 0.058581 | 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":12122020,"numValue":-0.172172778399885,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122021,"numValue":0.0585811087191155,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20385 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,385 | train | mutant | 476,668 | 358 | 478,020 | 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 | Q45T | Q45T | 1 | 1 | 0 | 0 | 45 | Q | T | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,314 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.582521 | 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":2366825,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366826,"numValue":1.5825212025624005,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366827,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20386 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,386 | train | mutant | 476,668 | 358 | 478,020 | 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 | Q45T | Q45T | 1 | 1 | 0 | 0 | 45 | Q | T | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,065,115 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.066153 | 0.069078 | 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":12122912,"numValue":-0.0661528309185654,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122913,"numValue":0.0690783862745097,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20387 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,387 | train | mutant | 476,669 | 358 | 478,021 | 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 | Q45S | Q45S | 1 | 1 | 0 | 0 | 45 | Q | S | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,315 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.235052 | 1.582841 | 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":2366828,"numValue":2.2350521507087544,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366829,"numValue":1.582841040300044,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366830,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20388 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,388 | train | mutant | 476,669 | 358 | 478,021 | 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 | Q45S | Q45S | 1 | 1 | 0 | 0 | 45 | Q | S | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,065,114 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.07889 | 0.045301 | 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":12122910,"numValue":-0.078889650601055,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122911,"numValue":0.045301376424175,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20389 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,389 | train | mutant | 476,670 | 358 | 478,022 | 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 | Q45A | Q45A | 1 | 1 | 0 | 0 | 45 | Q | A | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,316 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.677271 | 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":2366831,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366832,"numValue":1.6772710039858123,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366833,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20390 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,390 | train | mutant | 476,670 | 358 | 478,022 | 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 | Q45A | Q45A | 1 | 1 | 0 | 0 | 45 | Q | A | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,661 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.040739 | 0.057159 | 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":12122004,"numValue":-0.040738686473609,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122005,"numValue":0.0571585054459013,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20391 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,391 | train | mutant | 476,671 | 358 | 478,023 | 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 | Q45G | Q45G | 1 | 1 | 0 | 0 | 45 | Q | G | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,317 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.396691 | 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":2366834,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366835,"numValue":1.3966912131394364,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366836,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20392 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,392 | train | mutant | 476,671 | 358 | 478,023 | 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 | Q45G | Q45G | 1 | 1 | 0 | 0 | 45 | Q | G | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,666 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.148529 | 0.039089 | 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":12122014,"numValue":-0.148529374512732,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122015,"numValue":0.0390894811570695,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20393 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,393 | train | mutant | 476,672 | 358 | 478,024 | 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 | Q45M | Q45M | 1 | 1 | 0 | 0 | 45 | Q | M | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,318 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.206044 | 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":2366837,"numValue":2.20604359152062,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2366838,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366839,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20394 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,394 | train | mutant | 476,672 | 358 | 478,024 | 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 | Q45M | Q45M | 1 | 1 | 0 | 0 | 45 | Q | M | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,671 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.066237 | 0.058688 | 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":12122024,"numValue":-0.0662374731759179,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122025,"numValue":0.0586878560993303,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20395 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,395 | train | mutant | 476,673 | 358 | 478,025 | 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 | Q45L | Q45L | 1 | 1 | 0 | 0 | 45 | Q | L | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,319 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.579412 | 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":2366840,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366841,"numValue":1.5794119437128002,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366842,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:20396 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,396 | train | mutant | 476,673 | 358 | 478,025 | 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 | Q45L | Q45L | 1 | 1 | 0 | 0 | 45 | Q | L | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 5,064,670 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.253704 | 0.035371 | 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":12122022,"numValue":-0.253704126119908,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12122023,"numValue":0.035371410531938,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:20397 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20,397 | train | mutant | 476,674 | 358 | 478,026 | 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 | Q45V | Q45V | 1 | 1 | 0 | 0 | 45 | Q | V | 7 | CONSERVATION | 1CSP | 247 | null | 45 | A | L | false | false | 39.317331 | 33.077778 | 502,320 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.581857 | 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":2366843,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2366844,"numValue":1.5818567765173612,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2366845,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20853,"numValue":7.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.