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:17858 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,858 | train | mutant | 7,447 | 358 | 8,130 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|A46K|S48R|E66L | E3R|A46K|S48R|E66L | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48|66 | A | E|L | false | false | 44.051961 | 34.28325 | 15,872 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | null | NaCl | 0-2 M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 70.8 | 17 | null | null | null | null | 47.8 | 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":58309,"numValue":70.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58310,"numValue":17.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58311,"numValue":47.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58312,"numValue":null,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,859 | train | mutant | 7,447 | 358 | 8,130 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|A46K|S48R|E66L | E3R|A46K|S48R|E66L | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48|66 | A | E|L | false | false | 44.051961 | 34.28325 | 16,517 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 70.8 | 17 | null | -2.81 | 48 | 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":60529,"numValue":70.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60530,"numValue":17.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60531,"numValue":48.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60532,"numValue":-2.81,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17860 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,860 | train | mutant | 7,447 | 358 | 8,130 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|A46K|S48R|E66L | E3R|A46K|S48R|E66L | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48|66 | A | E|L | false | false | 44.051961 | 34.28325 | 16,553 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 70.8 | 17 | null | -1.13 | 48 | 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":60744,"numValue":70.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60745,"numValue":17.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60746,"numValue":48.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60747,"numValue":-1.13,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17861 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,861 | train | mutant | 7,447 | 358 | 8,130 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|A46K|S48R|E66L | E3R|A46K|S48R|E66L | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48|66 | A | E|L | false | false | 44.051961 | 34.28325 | 16,588 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 70.8 | 24.3 | null | -1.68 | 48 | 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":60954,"numValue":70.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60955,"numValue":24.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60956,"numValue":48.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60957,"numValue":-1.68,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17862 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,862 | train | mutant | 7,447 | 358 | 8,130 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|A46K|S48R|E66L | E3R|A46K|S48R|E66L | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48|66 | A | E|L | false | false | 44.051961 | 34.28325 | 16,610 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | 70.8 | 17 | null | -1.68 | 48 | 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":61086,"numValue":70.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":61087,"numValue":17.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":61088,"numValue":48.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":61089,"numValue":-1.68,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17863 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,863 | train | mutant | 7,447 | 358 | 8,130 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|A46K|S48R|E66L | E3R|A46K|S48R|E66L | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|48|66 | A | E|L | false | false | 44.051961 | 34.28325 | 16,726 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1 M | 70 | 1CSP_A:E3R 1CSP_A:A46K 1CSP_A:S48R 1CSP_A:E66L | null | null | null | -2.8 | 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":61515,"numValue":-2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61516,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20856,"numValue":4.0,"position":48,"positionArray":null,"positionRange... | |||||||||||||
fireprotdb:17864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,864 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,938 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R 1CSP_A:V20Q | 58.7 | null | null | null | null | null | 45.17 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | 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 1CSP_... | [{"datasets":[],"id":58531,"numValue":58.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58532,"numValue":45.17,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58533,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,865 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,939 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R 1CSP_A:V20Q | 52.1 | null | null | null | null | null | 38 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | 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 1CSP_... | [{"datasets":[],"id":58534,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58535,"numValue":38.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58536,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,866 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,947 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:V20Q | 58.2 | null | null | null | null | null | 44.69 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58558,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58559,"numValue":44.69,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58560,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17867 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,867 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,948 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:V20Q | 51.6 | null | null | null | null | null | 37.52 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58561,"numValue":51.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58562,"numValue":37.52,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58563,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,868 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,959 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R 1CSP_A:V20Q | 57.5 | null | null | null | null | null | 44.22 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58594,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58595,"numValue":44.22,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58596,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17869 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,869 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,960 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R 1CSP_A:V20Q | 51 | null | null | null | null | null | 37.05 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58597,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58598,"numValue":37.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58599,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17870 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,870 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,968 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R 1CSP_A:V20Q | 56.9 | null | null | null | null | null | 43.74 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58621,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58622,"numValue":43.74,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58623,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17871 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,871 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,969 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R 1CSP_A:V20Q | 50.5 | null | null | null | null | null | 36.57 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58624,"numValue":50.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58625,"numValue":36.57,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58626,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17872 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,872 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,977 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R 1CSP_A:V20Q | 56.7 | null | null | null | null | null | 43.5 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58648,"numValue":56.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58649,"numValue":43.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58650,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17873 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,873 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,978 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R 1CSP_A:V20Q | 50.5 | null | null | null | null | null | 36.57 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58651,"numValue":50.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58652,"numValue":36.57,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58653,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17874 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,874 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,986 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20Q | 58.5 | null | null | null | null | null | 44.93 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58675,"numValue":58.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58676,"numValue":44.93,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58677,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17875 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,875 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,987 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20Q | 51.9 | null | null | null | null | null | 37.76 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58678,"numValue":51.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58679,"numValue":37.76,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58680,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,876 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,763 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3R 1CSP_A:V20Q | null | null | 0.48 | 1.67 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|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":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61624,"numValue":0.48,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61625,"numValue":1.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61626,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,877 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,765 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:V20Q | null | null | 0.43 | 1.63 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61630,"numValue":0.43,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61631,"numValue":1.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61632,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17878 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,878 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,766 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.1 M | 1CSP_A:E3R 1CSP_A:V20Q | null | null | 0.33 | 1.65 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61633,"numValue":0.33,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61634,"numValue":1.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61635,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17879 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,879 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,767 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.2 M | 1CSP_A:E3R 1CSP_A:V20Q | null | null | 0.24 | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61636,"numValue":0.24,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61637,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61638,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17880 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,880 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,768 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 0.5 M | 1CSP_A:E3R 1CSP_A:V20Q | null | null | 0.22 | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61639,"numValue":0.22,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61640,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61641,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17881 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,881 | train | mutant | 7,505 | 358 | 8,189 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20Q|E3R | V20Q|E3R | 2 | 2 | 0 | 0 | 20 | V | Q | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,770 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20Q | null | null | 0.45 | 1.74 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61645,"numValue":0.45,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61646,"numValue":1.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61647,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17882 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,882 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,940 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R 1CSP_A:V20E | 43 | null | null | null | null | null | 29.64 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | 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 1CSP_... | [{"datasets":[],"id":58537,"numValue":43.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58538,"numValue":29.64,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58539,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17883 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,883 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,941 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R 1CSP_A:V20E | 36 | null | null | null | null | null | 21.99 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | 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 1CSP_... | [{"datasets":[],"id":58540,"numValue":36.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58541,"numValue":21.99,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58542,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17884 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,884 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,949 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:V20E | 43 | null | null | null | null | null | 29.64 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58564,"numValue":43.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58565,"numValue":29.64,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58566,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,886 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,961 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R 1CSP_A:V20E | 42.4 | null | null | null | null | null | 29.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58600,"numValue":42.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58601,"numValue":29.16,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58602,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17887 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,887 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,962 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R 1CSP_A:V20E | 33.6 | null | null | null | null | null | 20.08 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58603,"numValue":33.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58604,"numValue":20.08,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58605,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17888 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,888 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,970 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R 1CSP_A:V20E | 42.7 | null | null | null | null | null | 29.4 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58627,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58628,"numValue":29.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58629,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17889 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,889 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,971 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R 1CSP_A:V20E | 37.1 | null | null | null | null | null | 22.94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58630,"numValue":37.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58631,"numValue":22.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58632,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,890 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,979 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R 1CSP_A:V20E | 42.9 | null | null | null | null | null | 29.64 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58654,"numValue":42.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58655,"numValue":29.64,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58656,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,891 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,980 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R 1CSP_A:V20E | 36 | null | null | null | null | null | 21.99 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58657,"numValue":36.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58658,"numValue":21.99,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58659,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,892 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,988 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20E | 45.1 | null | null | null | null | null | 31.31 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58681,"numValue":45.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58682,"numValue":31.31,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58683,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,893 | train | mutant | 7,506 | 358 | 8,190 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20E|E3R | V20E|E3R | 2 | 2 | 0 | 0 | 20 | V | E | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,989 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20E | 39.8 | null | null | null | null | null | 25.1 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58684,"numValue":39.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58685,"numValue":25.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58686,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17894 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,894 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,942 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R 1CSP_A:V20K | 55.7 | null | null | null | null | null | 40.15 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | 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 1CSP_... | [{"datasets":[],"id":58543,"numValue":55.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58544,"numValue":40.15,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58545,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17895 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,895 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,943 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | 1CSP_A:E3R 1CSP_A:V20K | 48.8 | null | null | null | null | null | 34.66 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | 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 1CSP_... | [{"datasets":[],"id":58546,"numValue":48.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58547,"numValue":34.66,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58548,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17896 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,896 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,951 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:V20K | 54.6 | null | null | null | null | null | 39.2 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58570,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58571,"numValue":39.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58572,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17897 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,897 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,952 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:V20K | 47.9 | null | null | null | null | null | 33.94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58573,"numValue":47.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58574,"numValue":33.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58575,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17898 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,898 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,963 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.1 M | 1CSP_A:E3R 1CSP_A:V20K | 53.4 | null | null | null | null | null | 38.24 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58606,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58607,"numValue":38.24,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58608,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17900 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,900 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,972 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.2 M | 1CSP_A:E3R 1CSP_A:V20K | 52.5 | null | null | null | null | null | 37.52 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58633,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58634,"numValue":37.52,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58635,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17902 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,902 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,981 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.5 M | 1CSP_A:E3R 1CSP_A:V20K | 52.8 | null | null | null | null | null | 37.76 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58660,"numValue":52.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58661,"numValue":37.76,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58662,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17904 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,904 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,990 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20K | 55 | null | null | null | null | null | 39.67 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58687,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58688,"numValue":39.67,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58689,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17905 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,905 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 15,991 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20K | 48.3 | null | null | null | null | null | 34.18 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58690,"numValue":48.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58691,"numValue":34.18,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58692,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17906 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,906 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,764 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | 1CSP_A:E3R 1CSP_A:V20K | null | null | 0.1 | 2.06 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|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":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61627,"numValue":0.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61628,"numValue":2.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61629,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:17907 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,907 | train | mutant | 7,507 | 358 | 8,191 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | V20K|E3R | V20K|E3R | 2 | 2 | 0 | 0 | 20 | V | K | 4 | CONSERVATION | 1CSP | 247 | null | 3|20 | A | E|L | false | false | 48.755479 | 36.823428 | 16,771 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | 55 | NaCl | 1.0 M | 1CSP_A:E3R 1CSP_A:V20K | null | null | 0 | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"... | [{"datasets":[],"id":61648,"numValue":0.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":61649,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61650,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20828,"numValue":2.0,"position":20,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:17908 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,908 | train | mutant | 7,511 | 358 | 8,195 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|F15A|F27A | E3R|F15A|F27A | 3 | 3 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|15|27 | A | E | true | true | 68.670768 | 20.366788 | 15,956 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:F15A 1CSP_A:F27A | 44 | null | null | null | null | null | 32.27 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58585,"numValue":44.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58586,"numValue":32.27,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58587,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20835,"numValue":9.0,"position":27,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17909 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,909 | train | mutant | 7,512 | 358 | 8,196 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|F15A|E19K|F27A | E3R|F15A|E19K|F27A | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|15|19|27 | A | E | true | true | 72.250719 | 26.344535 | 15,957 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:F15A 1CSP_A:E19K 1CSP_A:F27A | 39 | null | null | null | null | null | 27.72 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58588,"numValue":39.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58589,"numValue":27.72,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58590,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20827,"numValue":3.0,"position":19,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17910 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,910 | train | mutant | 7,513 | 358 | 8,197 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus 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|F15A|D25K|F27A | E3R|F15A|D25K|F27A | 4 | 4 | 0 | 0 | 3 | E | R | 4 | CONSERVATION | 1CSP | 247 | null | 3|15|25|27 | A | E|L | true | true | 66.470513 | 24.484466 | 15,958 | ProTherm | 7.5 | CD | Thermal | Sodium cacodylate | 50 mM | null | NaCl | 0.05 M | 1CSP_A:E3R 1CSP_A:F15A 1CSP_A:D25K 1CSP_A:F27A | 23 | null | null | null | null | null | 10.28 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 218 | ARTICLE | Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. | 2,007 | 10.1016/j.jmb.2006.11.061 | 17188709 | J Mol Biol;366;842-56 | 2 | Makhatadze George I|Gribenko Alexey V | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":58591,"numValue":23.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58592,"numValue":10.28,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":58593,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20823,"numValue":5.0,"position":15,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:17911 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,911 | train | mutant | 7,832 | 358 | 8,544 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K5A | E3L|K5A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|5 | A | E | false | false | 87.960711 | 33.037556 | 16,505 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3L 1CSP_A:K5A | 49.1 | -4.7 | null | 0.65 | 41.76 | 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":60457,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60458,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60459,"numValue":41.76,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60460,"numValue":0.65,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17912 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,912 | train | mutant | 7,832 | 358 | 8,544 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K5A | E3L|K5A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|5 | A | E | false | false | 87.960711 | 33.037556 | 16,541 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3L 1CSP_A:K5A | 49.1 | -4.7 | null | 0.36 | 41.76 | 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":60673,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60674,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60675,"numValue":41.76,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60676,"numValue":0.36,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17913 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,913 | train | mutant | 7,832 | 358 | 8,544 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K5A | E3L|K5A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|5 | A | E | false | false | 87.960711 | 33.037556 | 16,577 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3L 1CSP_A:K5A | 49.1 | -4.7 | null | 0.29 | 41.76 | 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":60888,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60889,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60890,"numValue":41.76,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60891,"numValue":0.29,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20813,"numValue":6.0,"position":5,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17914 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,914 | train | mutant | 7,833 | 358 | 8,545 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K7A | E3L|K7A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|7 | A | E | false | false | 79.401913 | 31.296445 | 16,506 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3L 1CSP_A:K7A | 51.3 | -2.5 | null | 0.29 | 43.44 | 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":60463,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60464,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60465,"numValue":43.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60466,"numValue":0.29,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20815,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17915 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,915 | train | mutant | 7,833 | 358 | 8,545 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K7A | E3L|K7A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|7 | A | E | false | false | 79.401913 | 31.296445 | 16,542 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3L 1CSP_A:K7A | 51.3 | -2.5 | null | 0.14 | 43.44 | 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":60679,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60680,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60681,"numValue":43.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60682,"numValue":0.14,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20815,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17916 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,916 | train | mutant | 7,833 | 358 | 8,545 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K7A | E3L|K7A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|7 | A | E | false | false | 79.401913 | 31.296445 | 16,578 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3L 1CSP_A:K7A | 51.3 | -2.5 | null | 0.14 | 43.44 | 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":60894,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60895,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60896,"numValue":43.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60897,"numValue":0.14,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20815,"numValue":9.0,"position":7,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17917 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,917 | train | mutant | 7,834 | 358 | 8,546 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|E12A | E3L|E12A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|12 | A | E|T | true | true | 128.756678 | 39.448667 | 16,507 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3L 1CSP_A:E12A | 60.2 | 6.4 | null | -1.08 | 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":60469,"numValue":60.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60470,"numValue":6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60471,"numValue":51.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60472,"numValue":-1.08,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20820,"numValue":3.0,"position":12,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17918 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,918 | train | mutant | 7,834 | 358 | 8,546 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|E12A | E3L|E12A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|12 | A | E|T | true | true | 128.756678 | 39.448667 | 16,543 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3L 1CSP_A:E12A | 60.2 | 6.4 | null | -0.77 | 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":60685,"numValue":60.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60686,"numValue":6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60687,"numValue":51.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60688,"numValue":-0.77,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20820,"numValue":3.0,"position":12,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17919 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,919 | train | mutant | 7,834 | 358 | 8,546 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|E12A | E3L|E12A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|12 | A | E|T | true | true | 128.756678 | 39.448667 | 16,579 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3L 1CSP_A:E12A | 60.2 | 6.4 | null | -0.31 | 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":60900,"numValue":60.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60901,"numValue":6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60902,"numValue":51.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60903,"numValue":-0.31,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20820,"numValue":3.0,"position":12,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17920 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,920 | train | mutant | 7,835 | 358 | 8,547 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K13A | E3L|K13A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|13 | A | E|T | true | true | 107.84994 | 38.098667 | 16,508 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3L 1CSP_A:K13A | 65.6 | 11.8 | null | -0.77 | 56.4 | 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":60475,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60476,"numValue":11.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60477,"numValue":56.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60478,"numValue":-0.77,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17921 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,921 | train | mutant | 7,835 | 358 | 8,547 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K13A | E3L|K13A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|13 | A | E|T | true | true | 107.84994 | 38.098667 | 16,544 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3L 1CSP_A:K13A | 65.6 | 11.8 | null | -0.46 | 56.4 | 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":60691,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60692,"numValue":11.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60693,"numValue":56.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60694,"numValue":-0.46,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17922 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,922 | train | mutant | 7,835 | 358 | 8,547 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|K13A | E3L|K13A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|13 | A | E|T | true | true | 107.84994 | 38.098667 | 16,580 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3L 1CSP_A:K13A | 65.6 | 11.8 | null | -0.31 | 56.4 | 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":60906,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60907,"numValue":11.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60908,"numValue":56.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60909,"numValue":-0.31,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20821,"numValue":9.0,"position":13,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17925 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,925 | train | mutant | 7,836 | 358 | 8,548 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|E19A | E3L|E19A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|19 | A | E | false | false | 80.491634 | 36.135889 | 16,581 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3L 1CSP_A:E19A | 61.9 | 8.1 | null | -0.26 | 48.24 | 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":60912,"numValue":61.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60913,"numValue":8.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60914,"numValue":48.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60915,"numValue":-0.26,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20827,"numValue":3.0,"position":19,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17926 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,926 | train | mutant | 7,837 | 358 | 8,549 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|D25A | E3L|D25A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|25 | A | E|L | false | false | 68.931221 | 32.41575 | 16,510 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3L 1CSP_A:D25A | 57.1 | 3.3 | null | -0.84 | 41.76 | 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":60487,"numValue":57.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60488,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60489,"numValue":41.76,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60490,"numValue":-0.84,"references":[... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17927 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,927 | train | mutant | 7,837 | 358 | 8,549 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3L|D25A | E3L|D25A | 2 | 2 | 0 | 0 | 3 | E | L | 4 | CONSERVATION | 1CSP | 247 | null | 3|25 | A | E|L | false | false | 68.931221 | 32.41575 | 16,546 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3L 1CSP_A:D25A | 57.1 | 3.3 | null | null | 41.76 | null | null | null | null | null | null | null | null | null | null | null | Unknown | 2.0 | TM|DTM|DH|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":60703,"numValue":57.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60704,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60705,"numValue":41.76,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60706,"numValue":2.0,"references":[],... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20833,"numValue":9.0,"position":25,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17928 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,928 | train | mutant | 7,838 | 358 | 8,550 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|T64R | E3V|T64R | 2 | 2 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|64 | A | E | false | false | 67.258716 | 29.259857 | 16,512 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3V 1CSP_A:T64R | 69.2 | 15.4 | null | -2.54 | 53.28 | 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":60499,"numValue":69.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60500,"numValue":15.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60501,"numValue":53.28,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60502,"numValue":-2.54,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17929 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,929 | train | mutant | 7,838 | 358 | 8,550 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|T64R | E3V|T64R | 2 | 2 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|64 | A | E | false | false | 67.258716 | 29.259857 | 16,548 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3V 1CSP_A:T64R | 69.2 | 15.4 | null | -1.51 | 53.28 | 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":60714,"numValue":69.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60715,"numValue":15.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60716,"numValue":53.28,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60717,"numValue":-1.51,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17930 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,930 | train | mutant | 7,838 | 358 | 8,550 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|T64R | E3V|T64R | 2 | 2 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|64 | A | E | false | false | 67.258716 | 29.259857 | 16,583 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3V 1CSP_A:T64R | 69.2 | 20.8 | null | -1.03 | 53.28 | 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":60924,"numValue":69.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60925,"numValue":20.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60926,"numValue":53.28,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60927,"numValue":-1.03,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17931 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,931 | train | mutant | 7,839 | 358 | 8,551 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|E66V | E3V|E66V | 2 | 2 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,513 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3V 1CSP_A:E66V | 73.2 | 19.4 | null | -3.17 | 55.2 | 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":60505,"numValue":73.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60506,"numValue":19.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60507,"numValue":55.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60508,"numValue":-3.17,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17932 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,932 | train | mutant | 7,839 | 358 | 8,551 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|E66V | E3V|E66V | 2 | 2 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,549 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3V 1CSP_A:E66V | 73.2 | 19.4 | null | -1.34 | 55.2 | 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":60720,"numValue":73.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60721,"numValue":19.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60722,"numValue":55.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60723,"numValue":-1.34,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17933 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,933 | train | mutant | 7,839 | 358 | 8,551 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|E66V | E3V|E66V | 2 | 2 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|66 | A | E|L | false | false | 61.892795 | 40.83 | 16,584 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3V 1CSP_A:E66V | 73.2 | 15.4 | null | -1.82 | 55.2 | 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":60930,"numValue":73.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60931,"numValue":15.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60932,"numValue":55.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60933,"numValue":-1.82,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:17934 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,934 | train | mutant | 7,840 | 358 | 8,552 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|T64R|E66V | E3V|T64R|E66V | 3 | 3 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|64|66 | A | E|L | false | false | 60.103441 | 37.395238 | 16,516 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3V 1CSP_A:T64R 1CSP_A:E66V | 78.1 | 24.3 | null | -3.96 | 60.24 | 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":60523,"numValue":78.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60524,"numValue":24.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60525,"numValue":60.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60526,"numValue":-3.96,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17935 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,935 | train | mutant | 7,840 | 358 | 8,552 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|T64R|E66V | E3V|T64R|E66V | 3 | 3 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|64|66 | A | E|L | false | false | 60.103441 | 37.395238 | 16,552 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3V 1CSP_A:T64R 1CSP_A:E66V | 78.1 | 24.3 | null | -1.8 | 60.24 | 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":60738,"numValue":78.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60739,"numValue":24.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60740,"numValue":60.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60741,"numValue":-1.8,"references":[... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20874,"numValue":2.0,"position":66,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17937 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,937 | train | mutant | 7,841 | 358 | 8,553 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|A46L|T64R|E66V|A67G | E3V|A46L|T64R|E66V|A67G | 5 | 5 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|64|66|67 | A | E|L | false | false | 70.286788 | 39.940076 | 16,518 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0M | 1CSP_A:E3V 1CSP_A:A46L 1CSP_A:T64R 1CSP_A:E66V 1CSP_A:A67G | 85.6 | 31.8 | null | -5.14 | 64.08 | 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":60535,"numValue":85.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60536,"numValue":31.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60537,"numValue":64.08,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60538,"numValue":-5.14,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17938 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,938 | train | mutant | 7,841 | 358 | 8,553 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|A46L|T64R|E66V|A67G | E3V|A46L|T64R|E66V|A67G | 5 | 5 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|64|66|67 | A | E|L | false | false | 70.286788 | 39.940076 | 16,554 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 0-2M | 1CSP_A:E3V 1CSP_A:A46L 1CSP_A:T64R 1CSP_A:E66V 1CSP_A:A67G | 85.6 | 31.8 | null | -1.94 | 64.08 | 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":60750,"numValue":85.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60751,"numValue":31.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60752,"numValue":64.08,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60753,"numValue":-1.94,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17939 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,939 | train | mutant | 7,841 | 358 | 8,553 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3V|A46L|T64R|E66V|A67G | E3V|A46L|T64R|E66V|A67G | 5 | 5 | 0 | 0 | 3 | E | V | 4 | CONSERVATION | 1CSP | 247 | null | 3|46|64|66|67 | A | E|L | false | false | 70.286788 | 39.940076 | 16,589 | ProTherm | 7 | CD | Thermal | Sodium cacodylate/HCl | 0.1M | null | NaCl | 2M | 1CSP_A:E3V 1CSP_A:A46L 1CSP_A:T64R 1CSP_A:E66V 1CSP_A:A67G | 85.6 | 17 | null | -3.19 | 64.08 | 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":60960,"numValue":85.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":60961,"numValue":17.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60962,"numValue":64.08,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":60963,"numValue":-3.19,"references":... | [{"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":null,"strValue":null,"type":"CONSERVATION"},{"id":20872,"numValue":3.0,"position":64,"positionArray":null,"positionRange... | ||||||||||
fireprotdb:17940 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,940 | train | mutant | 475,780 | 358 | 477,152 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3N | E3N | 1 | 1 | 0 | 0 | 3 | E | N | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,385 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.234923 | 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":2364039,"numValue":2.234922528772272,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364040,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364041,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17941 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,941 | train | mutant | 475,780 | 358 | 477,152 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3N | E3N | 1 | 1 | 0 | 0 | 3 | E | N | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,594 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.01219 | 0.070187 | 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":12123870,"numValue":-0.0121903251078438,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123871,"numValue":0.0701867705010448,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17942 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,942 | train | mutant | 475,781 | 358 | 477,153 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3H | E3H | 1 | 1 | 0 | 0 | 3 | E | H | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,386 | 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":2364042,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364043,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364044,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17943 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,943 | train | mutant | 475,781 | 358 | 477,153 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3H | E3H | 1 | 1 | 0 | 0 | 3 | E | H | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,589 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.120595 | 0.078934 | 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":12123860,"numValue":-0.120594976187618,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123861,"numValue":0.0789335051039588,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17944 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,944 | train | mutant | 475,782 | 358 | 477,154 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3D | E3D | 1 | 1 | 0 | 0 | 3 | E | D | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,387 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.192022 | 1.70007 | 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":2364045,"numValue":2.192021956037258,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364046,"numValue":1.7000698706598354,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364047,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17945 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,945 | train | mutant | 475,782 | 358 | 477,154 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3D | E3D | 1 | 1 | 0 | 0 | 3 | E | D | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,064,307 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.003511 | 0.111993 | 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":12121296,"numValue":0.003510813631059,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121297,"numValue":0.111992808106864,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17946 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,946 | train | mutant | 475,783 | 358 | 477,155 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3T | E3T | 1 | 1 | 0 | 0 | 3 | E | T | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,390 | 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":2364054,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364055,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364056,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17947 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,947 | train | mutant | 475,783 | 358 | 477,155 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3T | E3T | 1 | 1 | 0 | 0 | 3 | E | T | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,599 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.047632 | 0.043432 | 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":12123880,"numValue":-0.0476315103006253,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123881,"numValue":0.043431941767599,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17948 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,948 | train | mutant | 475,784 | 358 | 477,156 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3S | E3S | 1 | 1 | 0 | 0 | 3 | E | S | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,391 | 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":2364057,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364058,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364059,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17949 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,949 | train | mutant | 475,784 | 358 | 477,156 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3S | E3S | 1 | 1 | 0 | 0 | 3 | E | S | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,598 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.004244 | 0.037588 | 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":12123878,"numValue":0.00424437986144797,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123879,"numValue":0.0375883077884432,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17950 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,950 | train | mutant | 475,785 | 358 | 477,157 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3A | E3A | 1 | 1 | 0 | 0 | 3 | E | A | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,392 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.1842 | 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":2364060,"numValue":2.184200286563037,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364061,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364062,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17951 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,951 | train | mutant | 475,785 | 358 | 477,157 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3A | E3A | 1 | 1 | 0 | 0 | 3 | E | A | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,064,305 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.035934 | 0.032419 | 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":12121292,"numValue":-0.035934318344314,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121293,"numValue":0.0324186285832119,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17952 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,952 | train | mutant | 475,786 | 358 | 477,158 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3G | E3G | 1 | 1 | 0 | 0 | 3 | E | G | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,393 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 2.231264 | 1.698035 | 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":2364063,"numValue":2.231263873002741,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364064,"numValue":1.6980353202667726,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364065,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17953 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,953 | train | mutant | 475,786 | 358 | 477,158 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3G | E3G | 1 | 1 | 0 | 0 | 3 | E | G | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,588 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.07419 | 0.028502 | 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":12123858,"numValue":-0.0741895519192233,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123859,"numValue":0.028502249735999,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17954 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,954 | train | mutant | 475,787 | 358 | 477,159 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3M | E3M | 1 | 1 | 0 | 0 | 3 | E | M | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,394 | 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":2364066,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364067,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364068,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17957 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,957 | train | mutant | 475,788 | 358 | 477,160 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3I | E3I | 1 | 1 | 0 | 0 | 3 | E | I | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,590 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.02196 | 0.06635 | 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":12123862,"numValue":0.0219597589854657,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123863,"numValue":0.066349838839302,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17958 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,958 | train | mutant | 475,789 | 358 | 477,161 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3W | E3W | 1 | 1 | 0 | 0 | 3 | E | W | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,398 | 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":2364078,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364079,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364080,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17959 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,959 | train | mutant | 475,789 | 358 | 477,161 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3W | E3W | 1 | 1 | 0 | 0 | 3 | E | W | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,601 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.046391 | 0.031383 | 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":12123884,"numValue":-0.0463913172255029,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123885,"numValue":0.0313826257537071,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17963 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,963 | train | mutant | 475,791 | 358 | 477,163 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3F | E3F | 1 | 1 | 0 | 0 | 3 | E | F | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,587 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.051324 | 0.061135 | 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":12123856,"numValue":0.0513244887898998,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123857,"numValue":0.0611353789731336,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17964 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,964 | train | mutant | 475,792 | 358 | 477,164 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3P | E3P | 1 | 1 | 0 | 0 | 3 | E | P | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,401 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | null | 1.672701 | 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":2364087,"numValue":null,"references":[],"strValue":">2.25","type":"TRYPSIN_ML"},{"datasets":[],"id":2364088,"numValue":1.672700954576109,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364089,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17965 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,965 | train | mutant | 475,792 | 358 | 477,164 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3P | E3P | 1 | 1 | 0 | 0 | 3 | E | P | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,065,595 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.152555 | 0.035438 | 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":12123872,"numValue":-0.152555401884198,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12123873,"numValue":0.0354383269832218,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17966 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,966 | train | mutant | 475,793 | 358 | 477,165 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3C | E3C | 1 | 1 | 0 | 0 | 3 | E | C | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,402 | MegaScale | null | null | null | null | 4.991035 | null | null | null | null | null | null | 1.990362 | 1.158791 | 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":2364090,"numValue":1.990361715500313,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364091,"numValue":1.1587910434717508,"references":[],"strValue":null,"type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364092,"numValue":4.991035015833763,"references":[],"strValue":null,"typ... | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17967 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,967 | train | mutant | 475,793 | 358 | 477,165 | 67 | 67 | 36 | Cold shock protein CspB | Bacillus subtilis (strain 168) | 1 | 36|1483 | Cold shock protein CspB|1CSQ | Bacillus subtilis (strain 168) | 1 | P32081 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 1CSQ | E3C | E3C | 1 | 1 | 0 | 0 | 3 | E | C | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,064,306 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.049094 | 0.054527 | 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":12121294,"numValue":-0.0490943493135666,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121295,"numValue":0.0545267813929086,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||
fireprotdb:17970 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,970 | train | mutant | 475,796 | 358 | 477,168 | 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 | delE3 | delE3 | 1 | 0 | 1 | 0 | 3 | E | - | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 501,405 | MegaScale | null | null | null | null | null | >5 | null | null | null | null | null | null | 1.853338 | 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":2364099,"numValue":1.853337652542853,"references":[],"strValue":null,"type":"TRYPSIN_ML"},{"datasets":[],"id":2364100,"numValue":null,"references":[],"strValue":">1.75","type":"CHYMOTRYPSIN_ML"},{"datasets":[],"id":2364101,"numValue":null,"references":[],"strValue":">5","type":"DG"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||||
fireprotdb:17971 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17,971 | train | mutant | 475,796 | 358 | 477,168 | 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 | delE3 | delE3 | 1 | 0 | 1 | 0 | 3 | E | - | 4 | CONSERVATION | 1CSP | 247 | null | 3 | A | E | false | false | 77.992697 | 27.994 | 5,064,304 | Domainome FITNESS | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -1.088531 | 0.095706 | 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":12121290,"numValue":-1.08853055153079,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS"},{"datasets":[],"id":12121291,"numValue":0.0957057977431553,"references":[],"strValue":null,"type":"DOMAINOME_FITNESS_STD"}] | [{"id":20811,"numValue":4.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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