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:17628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,628 | train | mutant | 7,440 | 358 | 8,123 | 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 | M1R|E3K|E66K | M1R|E3K|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|66 | A | L|E | false | false | 88.531284 | 37.287917 | 16,569 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:E66K | 61.1 | 7.3 | null | -0.7 | 39.84 | 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":60840,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60841,"numValue":7.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60842,"numValue":39.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60843,"numValue":-0.7,"references":[]... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,630 | train | mutant | 7,441 | 358 | 8,124 | 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 | M1R|K65I|E66K | M1R|K65I|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|65|66 | A | L|E | false | false | 94.212486 | 43.315843 | 15,866 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:M1R 1CSP_A:K65I 1CSP_A:E66K | 75.7 | 21.9 | null | null | null | null | 55.45 | 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":58285,"numValue":75.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58286,"numValue":21.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58287,"numValue":55.45,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58288,"numValue":null,"references"... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,631 | train | mutant | 7,441 | 358 | 8,124 | 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 | M1R|K65I|E66K | M1R|K65I|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|65|66 | A | L|E | false | false | 94.212486 | 43.315843 | 16,498 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R 1CSP_A:K65I 1CSP_A:E66K | 75.7 | 21.9 | null | -3.58 | 55.68 | 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":60415,"numValue":75.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60416,"numValue":21.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60417,"numValue":55.68,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60418,"numValue":-3.58,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17632 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,632 | train | mutant | 7,441 | 358 | 8,124 | 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 | M1R|K65I|E66K | M1R|K65I|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|65|66 | A | L|E | false | false | 94.212486 | 43.315843 | 16,534 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R 1CSP_A:K65I 1CSP_A:E66K | 75.7 | 21.9 | null | -1.13 | 55.68 | 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":60631,"numValue":75.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60632,"numValue":21.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60633,"numValue":55.68,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60634,"numValue":-1.13,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,633 | train | mutant | 7,441 | 358 | 8,124 | 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 | M1R|K65I|E66K | M1R|K65I|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|65|66 | A | L|E | false | false | 94.212486 | 43.315843 | 16,570 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R 1CSP_A:K65I 1CSP_A:E66K | 75.7 | 21.9 | null | -2.45 | 55.68 | 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":60846,"numValue":75.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60847,"numValue":21.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60848,"numValue":55.68,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60849,"numValue":-2.45,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,634 | train | mutant | 7,441 | 358 | 8,124 | 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 | M1R|K65I|E66K | M1R|K65I|E66K | 3 | 3 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|65|66 | A | L|E | false | false | 94.212486 | 43.315843 | 16,720 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:M1R 1CSP_A:K65I 1CSP_A:E66K | null | null | null | -3.56 | 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":61503,"numValue":-3.56,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61504,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | |||||||||||||
fireprotdb:17636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,636 | train | mutant | 7,442 | 358 | 8,125 | 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 | M1R|E3K|K65I|E66K | M1R|E3K|K65I|E66K | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 16,500 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 74.7 | 20.9 | null | -3.38 | 51.36 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|DDG|STATE|REVERSIBILITY | ION|ION_CONC|PH|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":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0M","type":"ION_CONC"},{"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"... | [{"datasets":[],"id":60427,"numValue":74.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60428,"numValue":20.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60429,"numValue":51.36,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60430,"numValue":-3.38,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,637 | train | mutant | 7,442 | 358 | 8,125 | 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 | M1R|E3K|K65I|E66K | M1R|E3K|K65I|E66K | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 16,536 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 74.7 | 20.9 | null | -1.46 | 51.36 | 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":60643,"numValue":74.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60644,"numValue":20.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60645,"numValue":51.36,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60646,"numValue":-1.46,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,638 | train | mutant | 7,442 | 358 | 8,125 | 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 | M1R|E3K|K65I|E66K | M1R|E3K|K65I|E66K | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 16,572 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | 74.7 | 20.9 | null | -1.92 | 51.36 | 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":60858,"numValue":74.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60859,"numValue":20.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60860,"numValue":51.36,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60861,"numValue":-1.92,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,639 | train | mutant | 7,442 | 358 | 8,125 | 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 | M1R|E3K|K65I|E66K | M1R|E3K|K65I|E66K | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 16,721 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66K | null | null | null | -3.37 | 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":61505,"numValue":-3.37,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61506,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | |||||||||||||
fireprotdb:17640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,640 | train | mutant | 7,443 | 358 | 8,126 | 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 | M1R|E3K|K65I|E66L | M1R|E3K|K65I|E66L | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 15,868 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66L | 85 | 31.2 | null | null | null | null | 57.6 | 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":58293,"numValue":85.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58294,"numValue":31.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58295,"numValue":57.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58296,"numValue":null,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:17641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,641 | train | mutant | 7,443 | 358 | 8,126 | 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 | M1R|E3K|K65I|E66L | M1R|E3K|K65I|E66L | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 16,499 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66L | 85 | 31.2 | null | -4.82 | 57.84 | 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":60421,"numValue":85.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60422,"numValue":31.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60423,"numValue":57.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60424,"numValue":-4.82,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17643 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,643 | train | mutant | 7,443 | 358 | 8,126 | 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 | M1R|E3K|K65I|E66L | M1R|E3K|K65I|E66L | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 16,571 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66L | 85 | 31.2 | null | -3.46 | 57.84 | 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":60852,"numValue":85.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60853,"numValue":31.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60854,"numValue":57.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60855,"numValue":-3.46,"references":... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17644 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,644 | train | mutant | 7,443 | 358 | 8,126 | 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 | M1R|E3K|K65I|E66L | M1R|E3K|K65I|E66L | 4 | 4 | 0 | 0 | 1 | M | R | 9 | CONSERVATION | 1CSP | 247 | null | 1|3|65|66 | A | L|E | false | false | 90.157538 | 39.485382 | 16,722 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:M1R 1CSP_A:E3K 1CSP_A:K65I 1CSP_A:E66L | null | null | null | -4.8 | 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":61507,"numValue":-4.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61508,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20873,"numValue":5.0,"position":65,"positionArray":null,"positionRange"... | |||||||||||||
fireprotdb:17645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,645 | train | mutant | 475,738 | 358 | 477,110 | 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 | M1Q | M1Q | 1 | 1 | 0 | 0 | 1 | M | Q | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,340 | 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":2363904,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363905,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363906,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,646 | train | mutant | 475,738 | 358 | 477,110 | 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 | M1Q | M1Q | 1 | 1 | 0 | 0 | 1 | M | Q | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,065,615 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.208215 | 0.085115 | 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":12123912,"numValue":-0.208215046289808,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123913,"numValue":0.0851153953041825,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,647 | train | mutant | 475,739 | 358 | 477,111 | 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 | M1E | M1E | 1 | 1 | 0 | 0 | 1 | M | E | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,341 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.212379 | 1.490221 | 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":2363907,"numValue":2.212379086831687,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363908,"numValue":1.4902207650700603,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363909,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,648 | train | mutant | 475,739 | 358 | 477,111 | 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 | M1E | M1E | 1 | 1 | 0 | 0 | 1 | M | E | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,287 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.162895 | 0.051339 | 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":12121256,"numValue":-0.162895250974413,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121257,"numValue":0.0513392827844457,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17649 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,649 | train | mutant | 475,740 | 358 | 477,112 | 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 | M1N | M1N | 1 | 1 | 0 | 0 | 1 | M | N | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,342 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.221218 | 1.647286 | 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":2363910,"numValue":2.221218296924599,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363911,"numValue":1.6472861307172315,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363912,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17651 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,651 | train | mutant | 475,741 | 358 | 477,113 | 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 | M1H | M1H | 1 | 1 | 0 | 0 | 1 | M | H | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,343 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.112111 | 1.684992 | 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":2363913,"numValue":2.112110722539602,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363914,"numValue":1.6849922685691707,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363915,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17652 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,652 | train | mutant | 475,741 | 358 | 477,113 | 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 | M1H | M1H | 1 | 1 | 0 | 0 | 1 | M | H | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,290 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | DOMAINOME_FITNESS|DOMAINOME_FITNESS_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":12121262,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121263,"numValue":null,"references":[],"strValue":"NA","type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17653 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,653 | train | mutant | 475,742 | 358 | 477,114 | 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 | M1D | M1D | 1 | 1 | 0 | 0 | 1 | M | D | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,344 | MegaScale | null | null | null | null | 4.778397 | null | null | null | null | null | null | 2.051141 | 1.306332 | 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":2363916,"numValue":2.05114085649148,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363917,"numValue":1.3063315239930229,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363918,"numValue":4.778396863751382,"references":[],"strValue":null,"type... | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17654 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,654 | train | mutant | 475,742 | 358 | 477,114 | 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 | M1D | M1D | 1 | 1 | 0 | 0 | 1 | M | D | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,286 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.386273 | 0.213147 | 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":12121254,"numValue":-0.38627291497446,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121255,"numValue":0.213147113824761,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17655 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,655 | train | mutant | 475,743 | 358 | 477,115 | 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 | M1K | M1K | 1 | 1 | 0 | 0 | 1 | M | K | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,346 | 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":2363922,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363923,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363924,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,656 | train | mutant | 475,743 | 358 | 477,115 | 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 | M1K | M1K | 1 | 1 | 0 | 0 | 1 | M | K | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,292 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.082032 | 0.058617 | 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":12121266,"numValue":-0.0820318410678466,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121267,"numValue":0.0586167750036448,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,657 | train | mutant | 475,744 | 358 | 477,116 | 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 | M1T | M1T | 1 | 1 | 0 | 0 | 1 | M | T | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,347 | 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":2363925,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363926,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363927,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,659 | train | mutant | 475,745 | 358 | 477,117 | 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 | M1S | M1S | 1 | 1 | 0 | 0 | 1 | M | S | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,348 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.560262 | 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":2363928,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363929,"numValue":1.5602624635572626,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363930,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17660 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,660 | train | mutant | 475,745 | 358 | 477,117 | 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 | M1S | M1S | 1 | 1 | 0 | 0 | 1 | M | S | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,065,617 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.134589 | 0.046719 | 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":12123916,"numValue":-0.134589162736577,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123917,"numValue":0.0467189134289419,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17663 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,663 | train | mutant | 475,747 | 358 | 477,119 | 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 | M1G | M1G | 1 | 1 | 0 | 0 | 1 | M | G | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,350 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.596965 | 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":2363934,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363935,"numValue":1.596965430620315,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363936,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17664 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,664 | train | mutant | 475,747 | 358 | 477,119 | 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 | M1G | M1G | 1 | 1 | 0 | 0 | 1 | M | G | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,289 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.050628 | 0.065434 | 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":12121260,"numValue":-0.0506283368906593,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121261,"numValue":0.0654338624108213,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,665 | train | mutant | 475,748 | 358 | 477,120 | 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 | M1L | M1L | 1 | 1 | 0 | 0 | 1 | M | L | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,351 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.703327 | 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":2363937,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363938,"numValue":1.7033270596341463,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363939,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17666 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,666 | train | mutant | 475,748 | 358 | 477,120 | 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 | M1L | M1L | 1 | 1 | 0 | 0 | 1 | M | L | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,293 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.109071 | 0.036719 | 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":12121268,"numValue":-0.109071362193849,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121269,"numValue":0.0367190808734075,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17667 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,667 | train | mutant | 475,749 | 358 | 477,121 | 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 | M1V | M1V | 1 | 1 | 0 | 0 | 1 | M | V | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,352 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.215606 | 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":2363940,"numValue":2.2156057810062157,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363941,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363942,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,669 | train | mutant | 475,750 | 358 | 477,122 | 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 | M1I | M1I | 1 | 1 | 0 | 0 | 1 | M | I | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,353 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.17659 | 1.745095 | 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":2363943,"numValue":2.176589609721717,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363944,"numValue":1.745094697346712,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363945,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17670 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,670 | train | mutant | 475,750 | 358 | 477,122 | 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 | M1I | M1I | 1 | 1 | 0 | 0 | 1 | M | I | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,291 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.021261 | 0.083488 | 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":12121264,"numValue":0.0212605403377705,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121265,"numValue":0.0834882399090329,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,671 | train | mutant | 475,751 | 358 | 477,123 | 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 | M1W | M1W | 1 | 1 | 0 | 0 | 1 | M | W | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,354 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.082174 | 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":2363946,"numValue":2.0821737617085327,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363947,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363948,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17673 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,673 | train | mutant | 475,752 | 358 | 477,124 | 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 | M1Y | M1Y | 1 | 1 | 0 | 0 | 1 | M | Y | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,355 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.215184 | 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":2363949,"numValue":2.2151838623893494,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363950,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363951,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,674 | train | mutant | 475,752 | 358 | 477,124 | 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 | M1Y | M1Y | 1 | 1 | 0 | 0 | 1 | M | Y | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,065,621 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.0441 | 0.099714 | 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":12123924,"numValue":-0.0441004561297645,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123925,"numValue":0.0997142833134598,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,676 | train | mutant | 475,753 | 358 | 477,125 | 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 | M1F | M1F | 1 | 1 | 0 | 0 | 1 | M | F | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,288 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.062146 | 0.088116 | 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":12121258,"numValue":-0.06214643073721,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121259,"numValue":0.0881159633273313,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,677 | train | mutant | 475,754 | 358 | 477,126 | 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 | M1P | M1P | 1 | 1 | 0 | 0 | 1 | M | P | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,357 | 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":2363955,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363956,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363957,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17678 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,678 | train | mutant | 475,754 | 358 | 477,126 | 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 | M1P | M1P | 1 | 1 | 0 | 0 | 1 | M | P | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,065,614 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.304273 | 0.157811 | 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":12123910,"numValue":-0.304272968090544,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123911,"numValue":0.157811011381133,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,681 | train | mutant | 475,756 | 358 | 477,128 | 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 | insG1 | insG1 | 1 | 0 | 0 | 1 | 1 | - | G | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,359 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.981566 | 1.477517 | 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":2363961,"numValue":1.9815664613693704,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363962,"numValue":1.4775168503827334,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363963,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,683 | train | mutant | 475,758 | 358 | 477,130 | 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 | delM1 | delM1 | 1 | 0 | 1 | 0 | 1 | M | - | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 501,361 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.930114 | 1.508916 | 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":2363967,"numValue":1.930113771289608,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363968,"numValue":1.508916213665083,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363969,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,684 | train | mutant | 475,758 | 358 | 477,130 | 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 | delM1 | delM1 | 1 | 0 | 1 | 0 | 1 | M | - | 9 | CONSERVATION | 1CSP | 247 | null | 1 | A | L | false | false | 141.808263 | 30.20375 | 5,064,283 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.089082 | 0.140857 | 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":12121248,"numValue":-1.08908223933727,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121249,"numValue":0.140857412573288,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20809,"numValue":9.0,"position":1,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,685 | train | mutant | 2,904 | 358 | 3,293 | 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 | L2R | L2R | 1 | 1 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,332 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:L2R | 50.7 | -3.1 | null | 0.36 | 41.52 | 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":19449,"numValue":50.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19450,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19451,"numValue":41.52,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19452,"numValue":0.36,"references":[... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,686 | train | mutant | 2,904 | 358 | 3,293 | 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 | L2R | L2R | 1 | 1 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,349 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:L2R | 50.7 | -3.1 | null | -0.46 | 41.52 | 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":19551,"numValue":50.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19552,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19553,"numValue":41.52,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19554,"numValue":-0.46,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,687 | train | mutant | 2,904 | 358 | 3,293 | 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 | L2R | L2R | 1 | 1 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,366 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:L2R | 50.7 | -3.1 | null | 0.82 | 41.52 | 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":19653,"numValue":50.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19654,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19655,"numValue":41.52,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":19656,"numValue":0.82,"references":[... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17688 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,688 | train | mutant | 2,904 | 358 | 3,293 | 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 | L2R | L2R | 1 | 1 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,367 | MegaScale | null | null | null | null | 4.912495 | null | null | null | null | null | null | 2.142587 | 1.377536 | 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":2363985,"numValue":2.1425872195391467,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363986,"numValue":1.3775357942519126,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363987,"numValue":4.912495114405601,"references":[],"strValue":null,"ty... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,689 | train | mutant | 2,904 | 358 | 3,293 | 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 | L2R | L2R | 1 | 1 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,607 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.050376 | 0.032856 | 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":12123896,"numValue":-0.0503762501676744,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123897,"numValue":0.032855597303543,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,690 | train | mutant | 7,829 | 358 | 8,541 | 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 | L2R|E3V|A46L|T64R|E66V|A67G | L2R|E3V|A46L|T64R|E66V|A67G | 6 | 6 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|46|64|66|67 | A | E|L | false | false | 69.039825 | 37.886522 | 16,501 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:A46L 1CSP_A:T64R 1CSP_A:E66V 1CSP_A:A67G | 82.2 | 28.4 | null | -4.56 | 57.12 | 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":60433,"numValue":82.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60434,"numValue":28.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60435,"numValue":57.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60436,"numValue":-4.56,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,691 | train | mutant | 7,829 | 358 | 8,541 | 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 | L2R|E3V|A46L|T64R|E66V|A67G | L2R|E3V|A46L|T64R|E66V|A67G | 6 | 6 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|46|64|66|67 | A | E|L | false | false | 69.039825 | 37.886522 | 16,537 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:A46L 1CSP_A:T64R 1CSP_A:E66V 1CSP_A:A67G | 82.2 | 28.4 | null | -1.87 | 57.12 | 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":60649,"numValue":82.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60650,"numValue":28.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60651,"numValue":57.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60652,"numValue":-1.87,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,692 | train | mutant | 7,829 | 358 | 8,541 | 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 | L2R|E3V|A46L|T64R|E66V|A67G | L2R|E3V|A46L|T64R|E66V|A67G | 6 | 6 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|46|64|66|67 | A | E|L | false | false | 69.039825 | 37.886522 | 16,573 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:A46L 1CSP_A:T64R 1CSP_A:E66V 1CSP_A:A67G | 82.2 | 28.4 | null | -2.69 | 57.12 | 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":60864,"numValue":82.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60865,"numValue":28.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60866,"numValue":57.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60867,"numValue":-2.69,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20854,"numValue":2.0,"position":46,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,693 | train | mutant | 7,830 | 358 | 8,542 | 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 | L2R|E3V|E66V | L2R|E3V|E66V | 3 | 3 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|66 | A | E|L | false | false | 62.196867 | 36.42625 | 16,502 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:E66V | 70.1 | 16.3 | null | -2.69 | 51.12 | 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":60439,"numValue":70.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60440,"numValue":16.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60441,"numValue":51.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60442,"numValue":-2.69,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,694 | train | mutant | 7,830 | 358 | 8,542 | 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 | L2R|E3V|E66V | L2R|E3V|E66V | 3 | 3 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|66 | A | E|L | false | false | 62.196867 | 36.42625 | 16,538 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:E66V | 70.1 | 16.3 | null | -1.58 | 51.12 | 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":60655,"numValue":70.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60656,"numValue":16.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60657,"numValue":51.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60658,"numValue":-1.58,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,695 | train | mutant | 7,830 | 358 | 8,542 | 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 | L2R|E3V|E66V | L2R|E3V|E66V | 3 | 3 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|66 | A | E|L | false | false | 62.196867 | 36.42625 | 16,574 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:E66V | 70.1 | 16.3 | null | -1.1 | 51.12 | 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":60870,"numValue":70.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60871,"numValue":16.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60872,"numValue":51.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60873,"numValue":-1.1,"references":[... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,696 | train | mutant | 7,831 | 358 | 8,543 | 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 | L2R|E3V|T64R|E66V | L2R|E3V|T64R|E66V | 4 | 4 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|64|66 | A | E|L | false | false | 60.778834 | 34.951116 | 16,503 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:T64R 1CSP_A:E66V | 75.1 | 21.3 | null | -3.29 | 57.12 | 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":60445,"numValue":75.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60446,"numValue":21.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60447,"numValue":57.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60448,"numValue":-3.29,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,697 | train | mutant | 7,831 | 358 | 8,543 | 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 | L2R|E3V|T64R|E66V | L2R|E3V|T64R|E66V | 4 | 4 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|64|66 | A | E|L | false | false | 60.778834 | 34.951116 | 16,539 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:T64R 1CSP_A:E66V | 75.1 | 21.3 | null | -1.8 | 57.12 | 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":60661,"numValue":75.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60662,"numValue":21.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60663,"numValue":57.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60664,"numValue":-1.8,"references":[... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,698 | train | mutant | 7,831 | 358 | 8,543 | 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 | L2R|E3V|T64R|E66V | L2R|E3V|T64R|E66V | 4 | 4 | 0 | 0 | 2 | L | R | 4 | CONSERVATION | 1CSP | 247 | null | 2|3|64|66 | A | E|L | false | false | 60.778834 | 34.951116 | 16,575 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:L2R 1CSP_A:E3V 1CSP_A:T64R 1CSP_A:E66V | 75.1 | 21.3 | null | -1.49 | 57.12 | 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":60876,"numValue":75.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60877,"numValue":21.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60878,"numValue":57.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60879,"numValue":-1.49,"references":... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange"... | ||||||||||
fireprotdb:17699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,699 | train | mutant | 475,759 | 358 | 477,131 | 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 | L2Q | L2Q | 1 | 1 | 0 | 0 | 2 | L | Q | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,362 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.63775 | 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":2363970,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363971,"numValue":1.6377496760561838,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363972,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,700 | train | mutant | 475,759 | 358 | 477,131 | 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 | L2Q | L2Q | 1 | 1 | 0 | 0 | 2 | L | Q | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,606 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.106503 | 0.045863 | 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":12123894,"numValue":-0.106503267037796,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123895,"numValue":0.045863137272629,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,701 | train | mutant | 475,760 | 358 | 477,132 | 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 | L2E | L2E | 1 | 1 | 0 | 0 | 2 | L | E | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,363 | MegaScale | null | null | null | null | 4.780358 | null | null | null | null | null | null | 2.095812 | 1.288553 | 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":2363973,"numValue":2.095812259260824,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363974,"numValue":1.288552726239177,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363975,"numValue":4.780357717306991,"references":[],"strValue":null,"type... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17702 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,702 | train | mutant | 475,760 | 358 | 477,132 | 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 | L2E | L2E | 1 | 1 | 0 | 0 | 2 | L | E | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,064,298 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.09508 | 0.050226 | 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":12121278,"numValue":-0.0950802423933444,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121279,"numValue":0.0502263720371913,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,703 | train | mutant | 475,761 | 358 | 477,133 | 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 | L2N | L2N | 1 | 1 | 0 | 0 | 2 | L | N | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,364 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.537283 | 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":2363976,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363977,"numValue":1.537282942092734,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363978,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,704 | train | mutant | 475,761 | 358 | 477,133 | 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 | L2N | L2N | 1 | 1 | 0 | 0 | 2 | L | N | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,604 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.047582 | 0.087295 | 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":12123890,"numValue":-0.0475818289756574,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123891,"numValue":0.0872946880911349,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,705 | train | mutant | 475,762 | 358 | 477,134 | 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 | L2H | L2H | 1 | 1 | 0 | 0 | 2 | L | H | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,365 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.715848 | 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":2363979,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363980,"numValue":1.7158479307937573,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363981,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,707 | train | mutant | 475,763 | 358 | 477,135 | 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 | L2D | L2D | 1 | 1 | 0 | 0 | 2 | L | D | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,366 | MegaScale | null | null | null | null | 4.055767 | null | null | null | null | null | null | 1.816285 | 0.880544 | 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":2363982,"numValue":1.8162852678333417,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363983,"numValue":0.8805437267989149,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363984,"numValue":4.055766607163094,"references":[],"strValue":null,"ty... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,708 | train | mutant | 475,763 | 358 | 477,135 | 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 | L2D | L2D | 1 | 1 | 0 | 0 | 2 | L | D | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,064,297 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.345735 | 0.088751 | 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":12121276,"numValue":-0.345734793849795,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121277,"numValue":0.0887509029274138,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,709 | train | mutant | 475,764 | 358 | 477,136 | 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 | L2K | L2K | 1 | 1 | 0 | 0 | 2 | L | K | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,368 | 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":2363988,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363989,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363990,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17710 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,710 | train | mutant | 475,764 | 358 | 477,136 | 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 | L2K | L2K | 1 | 1 | 0 | 0 | 2 | L | K | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,064,303 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.021058 | 0.055509 | 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":12121288,"numValue":0.0210575215900624,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121289,"numValue":0.0555093675978276,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17711 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,711 | train | mutant | 475,765 | 358 | 477,137 | 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 | L2T | L2T | 1 | 1 | 0 | 0 | 2 | L | T | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,369 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.135167 | 1.6735 | 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":2363991,"numValue":2.135166553300129,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2363992,"numValue":1.6734996669629172,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363993,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,712 | train | mutant | 475,765 | 358 | 477,137 | 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 | L2T | L2T | 1 | 1 | 0 | 0 | 2 | L | T | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,609 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.009554 | 0.045944 | 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":12123900,"numValue":0.00955414813609483,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123901,"numValue":0.0459438847594439,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,713 | train | mutant | 475,766 | 358 | 477,138 | 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 | L2S | L2S | 1 | 1 | 0 | 0 | 2 | L | S | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,370 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.509928 | 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":2363994,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363995,"numValue":1.5099284552424994,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363996,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17714 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,714 | train | mutant | 475,766 | 358 | 477,138 | 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 | L2S | L2S | 1 | 1 | 0 | 0 | 2 | L | S | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,608 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.080724 | 0.03113 | 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":12123898,"numValue":-0.0807241795267184,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123899,"numValue":0.0311301464869201,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,715 | train | mutant | 475,767 | 358 | 477,139 | 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 | L2A | L2A | 1 | 1 | 0 | 0 | 2 | L | A | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,371 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.577421 | 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":2363997,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2363998,"numValue":1.577420923839872,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2363999,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,716 | train | mutant | 475,767 | 358 | 477,139 | 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 | L2A | L2A | 1 | 1 | 0 | 0 | 2 | L | A | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,064,295 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.06338 | 0.046621 | 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":12121272,"numValue":-0.063380490315423,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121273,"numValue":0.0466208940148295,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,717 | train | mutant | 475,768 | 358 | 477,140 | 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 | L2G | L2G | 1 | 1 | 0 | 0 | 2 | L | G | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,372 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.09834 | 1.6408 | 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":2364000,"numValue":2.0983395220224463,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364001,"numValue":1.6407997709130728,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364002,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,718 | train | mutant | 475,768 | 358 | 477,140 | 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 | L2G | L2G | 1 | 1 | 0 | 0 | 2 | L | G | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,064,300 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.192533 | 0.039893 | 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":12121282,"numValue":-0.192532921391325,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121283,"numValue":0.0398930919221662,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,719 | train | mutant | 475,769 | 358 | 477,141 | 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 | L2M | L2M | 1 | 1 | 0 | 0 | 2 | L | M | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,373 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.672896 | 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":2364003,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364004,"numValue":1.6728960377904332,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364005,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,720 | train | mutant | 475,769 | 358 | 477,141 | 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 | L2M | L2M | 1 | 1 | 0 | 0 | 2 | L | M | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,603 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.004613 | 0.052947 | 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":12123888,"numValue":0.0046130030257154,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123889,"numValue":0.0529465288486267,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,721 | train | mutant | 475,770 | 358 | 477,142 | 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 | L2V | L2V | 1 | 1 | 0 | 0 | 2 | L | V | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,374 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.217244 | 1.716452 | 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":2364006,"numValue":2.21724398388832,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364007,"numValue":1.7164524856059695,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364008,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,722 | train | mutant | 475,770 | 358 | 477,142 | 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 | L2V | L2V | 1 | 1 | 0 | 0 | 2 | L | V | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,610 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.012358 | 0.041891 | 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":12123902,"numValue":-0.0123583829231669,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123903,"numValue":0.0418908209336004,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,723 | train | mutant | 475,771 | 358 | 477,143 | 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 | L2I | L2I | 1 | 1 | 0 | 0 | 2 | L | I | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,375 | 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":2364009,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364010,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364011,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,724 | train | mutant | 475,771 | 358 | 477,143 | 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 | L2I | L2I | 1 | 1 | 0 | 0 | 2 | L | I | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,064,302 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.006513 | 0.078333 | 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":12121286,"numValue":-0.00651316036831144,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121287,"numValue":0.078333465101292,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,726 | train | mutant | 475,772 | 358 | 477,144 | 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 | L2W | L2W | 1 | 1 | 0 | 0 | 2 | L | W | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,611 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.018679 | 0.035925 | 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":12123904,"numValue":-0.0186789514885169,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123905,"numValue":0.0359247439556381,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,727 | train | mutant | 475,773 | 358 | 477,145 | 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 | L2Y | L2Y | 1 | 1 | 0 | 0 | 2 | L | Y | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,377 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.744416 | 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":2364015,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364016,"numValue":1.7444156190291031,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364017,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,728 | train | mutant | 475,773 | 358 | 477,145 | 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 | L2Y | L2Y | 1 | 1 | 0 | 0 | 2 | L | Y | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,612 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.028415 | 0.056397 | 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":12123906,"numValue":0.0284146511331361,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123907,"numValue":0.0563972342099716,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,729 | train | mutant | 475,774 | 358 | 477,146 | 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 | L2F | L2F | 1 | 1 | 0 | 0 | 2 | L | F | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,378 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.745603 | 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":2364018,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364019,"numValue":1.7456030476119755,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364020,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,731 | train | mutant | 475,775 | 358 | 477,147 | 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 | L2P | L2P | 1 | 1 | 0 | 0 | 2 | L | P | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,379 | MegaScale | null | null | null | null | 4.330681 | null | null | null | null | null | null | 1.996292 | 1.062888 | 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":2364021,"numValue":1.996291560864738,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364022,"numValue":1.0628875559889503,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364023,"numValue":4.330681244420871,"references":[],"strValue":null,"typ... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17732 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,732 | train | mutant | 475,775 | 358 | 477,147 | 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 | L2P | L2P | 1 | 1 | 0 | 0 | 2 | L | P | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,065,605 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.285665 | 0.041303 | 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":12123892,"numValue":-0.285665165166178,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123893,"numValue":0.0413025817789877,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,733 | train | mutant | 475,776 | 358 | 477,148 | 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 | L2C | L2C | 1 | 1 | 0 | 0 | 2 | L | C | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,380 | MegaScale | null | null | null | null | 4.534195 | null | null | null | null | null | null | 1.979393 | 1.039811 | 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":2364024,"numValue":1.9793925244431525,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364025,"numValue":1.0398107173273778,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364026,"numValue":4.534195462880318,"references":[],"strValue":null,"ty... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,734 | train | mutant | 475,776 | 358 | 477,148 | 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 | L2C | L2C | 1 | 1 | 0 | 0 | 2 | L | C | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 5,064,296 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.043798 | 0.050067 | 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":12121274,"numValue":-0.0437980747321211,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121275,"numValue":0.0500673059283376,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17735 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,735 | train | mutant | 475,777 | 358 | 477,149 | 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 | insG2 | insG2 | 1 | 0 | 0 | 1 | 2 | - | G | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,381 | MegaScale | null | null | null | null | 4.887436 | null | null | null | null | null | null | 1.802764 | 1.245517 | 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":2364027,"numValue":1.8027640762195676,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364028,"numValue":1.2455168334499285,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364029,"numValue":4.887436279578509,"references":[],"strValue":null,"ty... | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,736 | train | mutant | 475,778 | 358 | 477,150 | 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 | insA2 | insA2 | 1 | 0 | 0 | 1 | 2 | - | A | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,382 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.836827 | 1.382903 | 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":2364030,"numValue":1.8368266206729853,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364031,"numValue":1.382903053259767,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364032,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,737 | train | mutant | 475,779 | 358 | 477,151 | 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 | delL2 | delL2 | 1 | 0 | 1 | 0 | 2 | L | - | 4 | CONSERVATION | 1CSP | 247 | null | 2 | A | E | false | false | 62.805013 | 27.61875 | 501,383 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.91842 | 1.456666 | 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":2364033,"numValue":1.918419726452202,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364034,"numValue":1.4566664218830072,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364035,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20810,"numValue":4.0,"position":2,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,739 | train | mutant | 323 | 358 | 359 | 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 | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 568 | ProTherm | 7 | CD | Thermal | sodium cacodylate-HCl | 100 mM | null | 1CSP_A:E3R | 69.6 | 16 | null | null | null | null | 52.34 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 58 | ARTICLE | Electrostatic stabilization of a thermophilic cold shock protein. | 2,001 | 10.1006/jmbi.2001.5050 | 11800561 | J Mol Biol;313;343-57 | 2 | Perl D|Schmid F 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":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3R"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":2256,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":2257,"numValue":16.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.cs... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17740 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,740 | train | mutant | 323 | 358 | 359 | 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 | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,060 | ProTherm | 7.5 | DSC | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R | 68.6 | null | null | null | 48.28 | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|khan_protherm_data_mapped.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3R","ty... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_mapped.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7728,"numValue":68.6,"referenc... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,742 | train | mutant | 323 | 358 | 359 | 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 | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,071 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R | 72.3 | null | null | null | null | null | 50.43 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3R","typ... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":7761,"numValue":72.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":7762,"numValue":50.43,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":7763,"numValue":null,"reference... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,743 | train | mutant | 323 | 358 | 359 | 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 | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,072 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R | 66.7 | null | null | null | null | null | 45.41 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CSP_A:E3R","typ... | [{"datasets":["EASE-MM_S1676.csv","khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7764,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","khan_protherm_data_mapped.csv","M4... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:17744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,744 | train | mutant | 323 | 358 | 359 | 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 | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,115 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R | 70.2 | null | null | null | null | null | 50.19 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7893,"numValue":70.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7894,"numValue":50.19,"refer... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17745 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,745 | train | mutant | 323 | 358 | 359 | 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 | E3R | E3R | 1 | 1 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 2,116 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R | 71.6 | null | null | null | null | null | 49.95 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7896,"numValue":71.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D1... | [{"id":20811,"numValue":4.0,"position":3,"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.