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:14173 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,173 | train | mutant | 7,043 | 302 | 7,696 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|D59A | D55A|D59A | 2 | 2 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|59 | A | H | false | false | 82.438633 | 20.5825 | 15,438 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D8A 1BNI_A:D12A | null | null | 9.04 | 0.89 | null | null | null | 4.16 | 1.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":56685,"numValue":9.04,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56686,"numValue":0.89,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56687,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56688,"numValue":4.16,"references":[],... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14175 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,175 | train | mutant | 7,045 | 302 | 7,698 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|D59A|R157A | D55A|D59A|R157A | 3 | 3 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|59|157 | A | H|L | false | false | 79.512079 | 15.900152 | 15,240 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:D8A 1BNI_A:D12A 1BNI_A:R110A | null | null | 9 | -0.18 | null | null | null | 4.63 | 1.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":55933,"numValue":9.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55934,"numValue":-0.18,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55935,"numValue":1.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55936,"numValue":4.63,"references":[],... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRan... | |||||||||||||
fireprotdb:14176 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,176 | train | mutant | 7,045 | 302 | 7,698 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|D59A|R157A | D55A|D59A|R157A | 3 | 3 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|59|157 | A | H|L | false | false | 79.512079 | 15.900152 | 15,402 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D8A 1BNI_A:D12A 1BNI_A:R110A | null | null | null | -0.11 | null | null | null | 4.63 | null | null | null | null | null | null | null | null | yes | DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 745 | ARTICLE | Co-operative interactions during protein folding. | 1,992 | 10.1016/0022-2836(92)90557-z | 1569552 | J Mol Biol;224;733-40 | 2 | Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":56536,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56537,"numValue":4.63,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56538,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRan... | |||||||||||
fireprotdb:14177 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,177 | train | mutant | 7,045 | 302 | 7,698 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|D59A|R157A | D55A|D59A|R157A | 3 | 3 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|59|157 | A | H|L | false | false | 79.512079 | 15.900152 | 15,441 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D8A 1BNI_A:D12A 1BNI_A:R110A | null | null | 10.04 | -0.11 | null | null | null | 4.63 | 2.16 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":56700,"numValue":10.04,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56701,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56702,"numValue":2.16,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56703,"numValue":4.63,"references":[... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRan... | |||||||||||||
fireprotdb:14178 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,178 | train | mutant | 7,149 | 302 | 7,804 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|R157A | D55A|R157A | 2 | 2 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|157 | A | H|L | false | false | 80.132315 | 13.205227 | 15,400 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D8A 1BNI_A:R110A | null | null | null | 0.47 | null | null | null | 4.36 | null | null | null | null | null | null | null | null | yes | DDG|CM|REVERSIBILITY | METHOD|PH|EXP_TEMPERATURE|MEASURE|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 745 | ARTICLE | Co-operative interactions during protein folding. | 1,992 | 10.1016/0022-2836(92)90557-z | 1569552 | J Mol Biol;224;733-40 | 2 | Horovitz A|Fersht A R | [{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":56530,"numValue":0.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56531,"numValue":4.36,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56532,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14179 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,179 | train | mutant | 7,149 | 302 | 7,804 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D55A|R157A | D55A|R157A | 2 | 2 | 0 | 0 | 55 | D | A | 4 | CONSERVATION | 1BNI | 159 | null | 55|157 | A | H|L | false | false | 80.132315 | 13.205227 | 15,439 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D8A 1BNI_A:R110A | null | null | 9.46 | 0.47 | null | null | null | 4.36 | 1.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":56690,"numValue":9.46,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56691,"numValue":0.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56692,"numValue":1.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56693,"numValue":4.36,"references":[],... | [{"id":20369,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14180 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,180 | train | mutant | 3,696 | 302 | 4,147 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V57T | V57T | 1 | 1 | 0 | 0 | 57 | V | T | 8 | CONSERVATION | 1BNI | 159 | null | 57 | A | H | false | false | 0 | 16.035714 | 8,501 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:V10T | null | null | null | 2.48 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":28901,"numValue":2.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28902,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20371,"numValue":8.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14181 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,181 | train | mutant | 3,696 | 302 | 4,147 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V57T | V57T | 1 | 1 | 0 | 0 | 57 | V | T | 8 | CONSERVATION | 1BNI | 159 | null | 57 | A | H | false | false | 0 | 16.035714 | 8,653 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:V10T | null | null | null | 2.58 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 597 | ARTICLE | The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90564-z | 1569559 | J Mol Biol;224;819-35 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":29360,"numValue":2.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29361,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20371,"numValue":8.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14182 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,182 | train | mutant | 3,696 | 302 | 4,147 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V57T | V57T | 1 | 1 | 0 | 0 | 57 | V | T | 8 | CONSERVATION | 1BNI | 159 | null | 57 | A | H | false | false | 0 | 16.035714 | 9,815 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:V10T | null | null | 6.83 | 1.99 | null | null | null | 3.3 | 2.07 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33654,"numValue":6.83,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33655,"numValue":1.99,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33656,"numValue":2.07,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33657,"numValue":3.3,... | [{"id":20371,"numValue":8.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14183 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,183 | train | mutant | 3,697 | 302 | 4,148 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V57A | V57A | 1 | 1 | 0 | 0 | 57 | V | A | 8 | CONSERVATION | 1BNI | 159 | null | 57 | A | H | false | false | 0 | 16.035714 | 8,502 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:V10A | null | null | null | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":28903,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28904,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20371,"numValue":8.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14184 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,184 | train | mutant | 3,697 | 302 | 4,148 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V57A | V57A | 1 | 1 | 0 | 0 | 57 | V | A | 8 | CONSERVATION | 1BNI | 159 | null | 57 | A | H | false | false | 0 | 16.035714 | 8,654 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:V10A | null | null | null | 3.63 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 597 | ARTICLE | The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90564-z | 1569559 | J Mol Biol;224;819-35 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":29362,"numValue":3.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29363,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20371,"numValue":8.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14185 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,185 | train | mutant | 3,697 | 302 | 4,148 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V57A | V57A | 1 | 1 | 0 | 0 | 57 | V | A | 8 | CONSERVATION | 1BNI | 159 | null | 57 | A | H | false | false | 0 | 16.035714 | 9,816 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:V10A | null | null | 5.35 | 3.47 | null | null | null | 2.8 | 1.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33659,"numValue":5.35,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33660,"numValue":3.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33661,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33662,"numValue":2.8... | [{"id":20371,"numValue":8.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14186 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,186 | train | mutant | 282 | 302 | 314 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59G | D59G | 1 | 1 | 0 | 0 | 59 | D | G | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 497 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:D12G | 49.68 | -1.95 | null | null | 123.3 | null | 124.3 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08 mM,13.92 mM,","type":"BUFFER_CONC"},{"numValue":null,"strV... | [{"datasets":[],"id":2006,"numValue":49.68,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2007,"numValue":-1.95,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2008,"numValue":123.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14187 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,187 | train | mutant | 282 | 302 | 314 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59G | D59G | 1 | 1 | 0 | 0 | 59 | D | G | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 1,469 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:D12G | 49.95 | -2.3 | null | null | null | null | 128.7 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:D12G","type":"_PDB_CHAI... | [{"datasets":[],"id":5381,"numValue":49.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5382,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5383,"numValue":128.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5384,"numValue":null,"references":[]... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14188 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,188 | train | mutant | 282 | 302 | 314 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59G | D59G | 1 | 1 | 0 | 0 | 59 | D | G | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 8,780 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:D12G | null | null | 7.88 | 0.78 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":29671,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29672,"numValue":7.88,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":29673,"numValue":0.78,"references":[],"strValue":null,"type":"DDG"},... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14189 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,189 | train | mutant | 282 | 302 | 314 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59G | D59G | 1 | 1 | 0 | 0 | 59 | D | G | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 9,081 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D12G | null | null | 8.6 | 0.2 | null | null | null | 3.97 | 1.87 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30845,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30846,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30847,"numValue":1.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3084... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14190 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,190 | train | mutant | 282 | 302 | 314 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59G | D59G | 1 | 1 | 0 | 0 | 59 | D | G | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 9,127 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:D12G | null | null | 8.3 | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31070,"numValue":8.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":31071,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31072,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBI... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14191 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,191 | train | mutant | 843 | 302 | 949 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A | D59A | 1 | 1 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 1,470 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:D12A | 51.25 | -1 | null | null | null | null | 152.8 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|HotMuSiC_S1626.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:D12A","type":"_PDB_CHAI... | [{"datasets":[],"id":5385,"numValue":51.25,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5386,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S1676.csv","HotMuSiC_S1626.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.cs... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14192 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,192 | train | mutant | 843 | 302 | 949 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A | D59A | 1 | 1 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 9,128 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:D12A | null | null | 10.6 | -1.1 | 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 | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31073,"numValue":10.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":31074,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31075,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14193 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,193 | train | mutant | 843 | 302 | 949 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A | D59A | 1 | 1 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 9,817 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:D12A | null | null | 8.43 | 0.39 | null | null | null | 4.4 | 1.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33664,"numValue":8.43,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":33665,"numValue":0.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33666,"numValue":1.91,"references":[],"strValue":null,"type":"M"},{"datase... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14194 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,194 | train | mutant | 843 | 302 | 949 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A | D59A | 1 | 1 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 10,725 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 50 mM | 25 | 1BNI_A:D12A | null | null | 10.12 | -0.11 | null | null | null | 4.33 | 2.33 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 700 | ARTICLE | Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. | 1,990 | 10.1021/bi00492a006 | 2248951 | Biochemistry;29;9343-52 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":36859,"numValue":10.12,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":36860,"numValue":-0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36861,"numValue":2.33,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14195 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,195 | train | mutant | 843 | 302 | 949 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A | D59A | 1 | 1 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 11,104 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D12A | null | null | null | 0.34 | null | null | null | 4.42 | null | null | null | null | null | null | null | null | yes | DDG|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 745 | ARTICLE | Co-operative interactions during protein folding. | 1,992 | 10.1016/0022-2836(92)90557-z | 1569552 | J Mol Biol;224;733-40 | 2 | Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":38231,"numValue":0.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38232,"numValue":4.42,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38233,"numValue":null,"references":[],"str... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14196 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,196 | train | mutant | 843 | 302 | 949 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A | D59A | 1 | 1 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 11,337 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D12A | null | null | 9.59 | 0.34 | null | null | null | 4.42 | 2.12 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":39031,"numValue":9.59,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":39032,"numValue":0.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39033,"numValue":2.12,"references":[],"str... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14197 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,197 | train | mutant | 3,911 | 302 | 4,413 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59S | D59S | 1 | 1 | 0 | 0 | 59 | D | S | 3 | CONSERVATION | 1BNI | 159 | null | 59 | A | H | false | false | 78.271606 | 21.29 | 9,082 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D12S | null | null | 7.9 | 0.9 | null | null | null | 4.29 | 1.85 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30850,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30851,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30852,"numValue":1.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30853,"numValue":4.29,... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14198 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,198 | train | mutant | 7,046 | 302 | 7,699 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A|R157A | D59A|R157A | 2 | 2 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59|157 | A | H|L | false | false | 75.965289 | 13.912727 | 15,241 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:D12A 1BNI_A:R110A | null | null | 9.21 | -0.39 | null | null | null | 4.78 | 1.93 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":55938,"numValue":9.21,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55939,"numValue":-0.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55940,"numValue":1.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55941,"numValue":4.78,"references":[]... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14200 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,200 | train | mutant | 7,046 | 302 | 7,699 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A|R157A | D59A|R157A | 2 | 2 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59|157 | A | H|L | false | false | 75.965289 | 13.912727 | 15,440 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D12A 1BNI_A:R110A | null | null | 10.38 | -0.45 | null | null | null | 4.78 | 2.14 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":56695,"numValue":10.38,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56696,"numValue":-0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56697,"numValue":2.14,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56698,"numValue":4.78,"references":[... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14201 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,201 | train | mutant | 7,101 | 302 | 7,754 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D59A|T63R | D59A|T63R | 2 | 2 | 0 | 0 | 59 | D | A | 3 | CONSERVATION | 1BNI | 159 | null | 59|63 | A | H | false | false | 89.415177 | 28.647857 | 15,315 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 50 mM | 25 | 1BNI_A:D12A 1BNI_A:T16R | null | null | 9.88 | 0.13 | null | null | null | 4.4 | 2.24 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 700 | ARTICLE | Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. | 1,990 | 10.1021/bi00492a006 | 2248951 | Biochemistry;29;9343-52 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":56205,"numValue":9.88,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56206,"numValue":0.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56207,"numValue":2.24,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56208,"numValue":4.4,"references":[],"... | [{"id":20373,"numValue":3.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14202 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,202 | train | mutant | 844 | 302 | 950 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60G | Y60G | 1 | 1 | 0 | 0 | 60 | Y | G | 8 | CONSERVATION | 1BNI | 159 | null | 60 | A | H | false | false | 41.06995 | 20.284167 | 1,471 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:Y13G | 36.65 | -15.6 | null | null | null | null | 92.7 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|PoPMuSiC-2.0_S2648.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:Y13G","type":"_PDB_CHAI... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":5389,"numValue":36.65,"references":[],"st... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14203 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,203 | train | mutant | 844 | 302 | 950 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60G | Y60G | 1 | 1 | 0 | 0 | 60 | Y | G | 8 | CONSERVATION | 1BNI | 159 | null | 60 | A | H | false | false | 41.06995 | 20.284167 | 9,129 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:Y13G | null | null | 3.1 | 6.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31076,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31077,"numValue":6.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31078,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14204 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,204 | train | mutant | 3,702 | 302 | 4,153 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A | Y60A | 1 | 1 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60 | A | H | false | false | 41.06995 | 20.284167 | 8,508 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:Y13A | null | null | null | 3.71 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv"],"id":28915,"numValue":3.71,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28916,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14205 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,205 | train | mutant | 3,702 | 302 | 4,153 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A | Y60A | 1 | 1 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60 | A | H | false | false | 41.06995 | 20.284167 | 9,818 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:Y13A | null | null | 5.82 | 3 | null | null | null | 2.8 | 2.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33669,"numValue":5.82,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33670,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33671,"numValue":2.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33672,"numValue":2.8,"... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14206 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,206 | train | mutant | 3,702 | 302 | 4,153 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A | Y60A | 1 | 1 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60 | A | H | false | false | 41.06995 | 20.284167 | 10,301 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y13A | null | null | 6.46 | 3.69 | null | null | null | 2.86 | 2.26 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 671 | ARTICLE | Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. | 1,991 | 10.1016/0022-2836(91)90725-l | 2010920 | J Mol Biol;218;465-75 | 3 | Serrano L|Bycroft M|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":35314,"numValue":6.46,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35315,"numValue":3.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35316,"numValue":2.26,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35317,"numValue":2.86,"references":[],... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14207 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,207 | train | mutant | 3,702 | 302 | 4,153 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A | Y60A | 1 | 1 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60 | A | H | false | false | 41.06995 | 20.284167 | 11,101 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y13A | null | null | null | 3.71 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 744 | ARTICLE | COSMIC analysis of the major alpha-helix of barnase during folding. | 1,991 | 10.1016/0022-2836(91)90852-w | 2023260 | J Mol Biol;219;5-9 | 3 | Serrano L|Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv"],"id":38224,"numValue":3.71,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38225,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14208 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,208 | train | mutant | 4,347 | 302 | 4,857 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60F | Y60F | 1 | 1 | 0 | 0 | 60 | Y | F | 8 | CONSERVATION | 1BNI | 159 | null | 60 | A | H | false | false | 41.06995 | 20.284167 | 10,303 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y13F | null | null | 9.52 | 0.63 | null | null | null | 4.38 | 2.17 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 671 | ARTICLE | Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. | 1,991 | 10.1016/0022-2836(91)90725-l | 2010920 | J Mol Biol;218;465-75 | 3 | Serrano L|Bycroft M|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":35324,"numValue":9.52,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":35325,"numValue":0.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35326,"numValue":2.17,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14209 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,209 | train | mutant | 7,004 | 302 | 7,656 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A|Y64A | Y60A|Y64A | 2 | 2 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60|64 | A | H | false | false | 81.93835 | 29.125 | 15,145 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:Y13A 1BNI_A:Y17A | null | null | null | 5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":[],"id":55568,"numValue":5.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55569,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14210 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,210 | train | mutant | 7,004 | 302 | 7,656 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A|Y64A | Y60A|Y64A | 2 | 2 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60|64 | A | H | false | false | 81.93835 | 29.125 | 15,242 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:Y13A 1BNI_A:Y17A | null | null | 4.86 | 3.96 | null | null | null | 2.43 | 2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":55943,"numValue":4.86,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55944,"numValue":3.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55945,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55946,"numValue":2.43,"references":[],"... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14211 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,211 | train | mutant | 7,004 | 302 | 7,656 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A|Y64A | Y60A|Y64A | 2 | 2 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60|64 | A | H | false | false | 81.93835 | 29.125 | 15,284 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y13A 1BNI_A:Y17A | null | null | 5.39 | 4.76 | null | null | null | 2.43 | 2.22 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 671 | ARTICLE | Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. | 1,991 | 10.1016/0022-2836(91)90725-l | 2010920 | J Mol Biol;218;465-75 | 3 | Serrano L|Bycroft M|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":56060,"numValue":5.39,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56061,"numValue":4.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56062,"numValue":2.22,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56063,"numValue":2.43,"references":[],... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14212 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,212 | train | mutant | 7,004 | 302 | 7,656 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60A|Y64A | Y60A|Y64A | 2 | 2 | 0 | 0 | 60 | Y | A | 8 | CONSERVATION | 1BNI | 159 | null | 60|64 | A | H | false | false | 81.93835 | 29.125 | 15,397 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y13A 1BNI_A:Y17A | null | null | null | 4.64 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 744 | ARTICLE | COSMIC analysis of the major alpha-helix of barnase during folding. | 1,991 | 10.1016/0022-2836(91)90852-w | 2023260 | J Mol Biol;219;5-9 | 3 | Serrano L|Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":56523,"numValue":4.64,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56524,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14213 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,213 | train | mutant | 7,084 | 302 | 7,737 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y60F|Y64F | Y60F|Y64F | 2 | 2 | 0 | 0 | 60 | Y | F | 8 | CONSERVATION | 1BNI | 159 | null | 60|64 | A | H | false | false | 81.93835 | 29.125 | 15,285 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y13F 1BNI_A:Y17F | null | null | 8.92 | 1.23 | null | null | null | 4.29 | 2.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 671 | ARTICLE | Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. | 1,991 | 10.1016/0022-2836(91)90725-l | 2010920 | J Mol Biol;218;465-75 | 3 | Serrano L|Bycroft M|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":56065,"numValue":8.92,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56066,"numValue":1.23,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56067,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56068,"numValue":4.29,"references":[],... | [{"id":20374,"numValue":8.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14214 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,214 | train | mutant | 664 | 302 | 719 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L61A | L61A | 1 | 1 | 0 | 0 | 61 | L | A | 7 | CONSERVATION | 1BNI | 159 | null | 61 | A | H | true | false | 0 | 24.67625 | 1,092 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | null | 1BNI_A:L14A | 42 | -11.9 | null | null | null | null | 108 | null | null | null | null | null | null | null | null | null | yes (>85%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:L14A","type":... | [{"datasets":[],"id":4082,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4083,"numValue":-11.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4084,"numValue":108.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":20375,"numValue":7.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14215 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,215 | train | mutant | 664 | 302 | 719 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L61A | L61A | 1 | 1 | 0 | 0 | 61 | L | A | 7 | CONSERVATION | 1BNI | 159 | null | 61 | A | H | true | false | 0 | 24.67625 | 7,783 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 48 | 1BNI_A:L14A | null | null | null | 4.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes (>85%) | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":48.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":26691,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26692,"numValue":null,"references":[],"strValue":"yes (>85%)","type":"REVERSIBILITY"}] | [{"id":20375,"numValue":7.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14216 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,216 | train | mutant | 664 | 302 | 719 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L61A | L61A | 1 | 1 | 0 | 0 | 61 | L | A | 7 | CONSERVATION | 1BNI | 159 | null | 61 | A | H | true | false | 0 | 24.67625 | 8,503 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:L14A | null | null | null | 4.32 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":28905,"numValue":4.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28906,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20375,"numValue":7.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14217 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,217 | train | mutant | 664 | 302 | 719 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L61A | L61A | 1 | 1 | 0 | 0 | 61 | L | A | 7 | CONSERVATION | 1BNI | 159 | null | 61 | A | H | true | false | 0 | 24.67625 | 8,909 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:L14A | null | null | 4.77 | 4.65 | null | null | null | 2.29 | 2.08 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFFER... | [{"datasets":[],"id":30208,"numValue":4.77,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30209,"numValue":4.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30210,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30211,"numValue":2.29,"references":[],... | [{"id":20375,"numValue":7.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14218 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,218 | train | mutant | 664 | 302 | 719 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L61A | L61A | 1 | 1 | 0 | 0 | 61 | L | A | 7 | CONSERVATION | 1BNI | 159 | null | 61 | A | H | true | false | 0 | 24.67625 | 9,684 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:L14A | null | null | null | 4.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 651 | ARTICLE | Mapping the transition state and pathway of protein folding by protein engineering. | 1,989 | 10.1038/340122a0 | 2739734 | Nature;340;122-6 | 4 | Matouschek A|Serrano L|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv"],"id":33254,"numValue":4.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33255,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20375,"numValue":7.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14219 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,219 | train | mutant | 664 | 302 | 719 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L61A | L61A | 1 | 1 | 0 | 0 | 61 | L | A | 7 | CONSERVATION | 1BNI | 159 | null | 61 | A | H | true | false | 0 | 24.67625 | 9,819 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:L14A | null | null | 4.29 | 4.53 | null | null | null | 2.2 | 1.87 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33674,"numValue":4.29,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33675,"numValue":4.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33676,"numValue":1.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33677,"numValue":2.2... | [{"id":20375,"numValue":7.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14220 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,220 | train | mutant | 845 | 302 | 951 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q62G | Q62G | 1 | 1 | 0 | 0 | 62 | Q | G | 5 | CONSERVATION | 1BNI | 159 | null | 62 | A | H | false | false | 72.879075 | 32.424444 | 1,472 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:Q15G | 50.25 | -2 | null | null | null | null | 123 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:Q15G","type":"_PDB_CHAI... | [{"datasets":[],"id":5393,"numValue":50.25,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5394,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5395,"numValue":123.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5396,"numValue":null,"references":[]... | [{"id":20376,"numValue":5.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14221 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,221 | train | mutant | 845 | 302 | 951 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q62G | Q62G | 1 | 1 | 0 | 0 | 62 | Q | G | 5 | CONSERVATION | 1BNI | 159 | null | 62 | A | H | false | false | 72.879075 | 32.424444 | 9,130 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:Q15G | null | null | 7.9 | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31079,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31080,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31081,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20376,"numValue":5.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14222 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,222 | train | mutant | 846 | 302 | 952 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q62A | Q62A | 1 | 1 | 0 | 0 | 62 | Q | A | 5 | CONSERVATION | 1BNI | 159 | null | 62 | A | H | false | false | 72.879075 | 32.424444 | 1,473 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:Q15A | 51.35 | -0.9 | null | null | null | null | 136.7 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:Q15A","type":"_PDB_CHAI... | [{"datasets":[],"id":5397,"numValue":51.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5398,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.cs... | [{"id":20376,"numValue":5.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14223 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,223 | train | mutant | 846 | 302 | 952 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q62A | Q62A | 1 | 1 | 0 | 0 | 62 | Q | A | 5 | CONSERVATION | 1BNI | 159 | null | 62 | A | H | false | false | 72.879075 | 32.424444 | 9,131 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:Q15A | null | null | 9.3 | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31082,"numValue":9.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31083,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31084,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20376,"numValue":5.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14224 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,224 | train | mutant | 4,290 | 302 | 4,798 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q62I | Q62I | 1 | 1 | 0 | 0 | 62 | Q | I | 5 | CONSERVATION | 1BNI | 159 | null | 62 | A | H | false | false | 72.879075 | 32.424444 | 9,963 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Q15I | null | null | 10.2 | -1.38 | null | null | null | 5 | 2.02 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":34230,"numValue":10.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34231,"numValue":-1.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34232,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34233,"numValue":5.... | [{"id":20376,"numValue":5.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14225 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,225 | train | mutant | 7,050 | 302 | 7,703 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q62I|T63R|K66R | Q62I|T63R|K66R | 3 | 3 | 0 | 0 | 62 | Q | I | 5 | CONSERVATION | 1BNI | 159 | null | 62|63|66 | A | H|S | true | false | 79.939023 | 31.805608 | 15,247 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Q15I 1BNI_A:T16R 1BNI_A:K19R | null | null | 10.8 | -1.98 | null | null | null | 5.42 | 2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":55968,"numValue":10.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55969,"numValue":-1.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55970,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55971,"numValue":5.42,"references":[],... | [{"id":20376,"numValue":5.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20380,"numValue":3.0,"position":66,"positionArray":null,"positionRang... | |||||||||||||
fireprotdb:14226 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,226 | train | mutant | 7,051 | 302 | 7,704 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q62I|T63R|K66R|G112S|K113A|K155R | Q62I|T63R|K66R|G112S|K113A|K155R | 6 | 6 | 0 | 0 | 62 | Q | I | 5 | CONSERVATION | 1BNI | 159 | null | 62|63|66|112|113|155 | A | H|S|L|E | true | false | 89.507445 | 26.104934 | 15,248 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Q15I 1BNI_A:T16R 1BNI_A:K19R 1BNI_A:G65S 1BNI_A:K66A 1BNI_A:K108R | null | null | 11.8 | -2.98 | null | null | null | 6.34 | 1.86 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":55973,"numValue":11.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55974,"numValue":-2.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55975,"numValue":1.86,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55976,"numValue":6.34,"references":[]... | [{"id":20376,"numValue":5.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20380,"numValue":3.0,"position":66,"positionArray":null,"positionRang... | |||||||||||||
fireprotdb:14227 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,227 | train | mutant | 275 | 302 | 307 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63R | T63R | 1 | 1 | 0 | 0 | 63 | T | R | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 489 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:T16R | 52.96 | 1.33 | null | null | 126.3 | null | 129.7 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08 mM,13.92 mM,","type":"BUFFER_CONC"},{"numValue":null,"strV... | [{"datasets":[],"id":1966,"numValue":52.96,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1967,"numValue":1.33,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1968,"numValue":126.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14228 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,228 | train | mutant | 275 | 302 | 307 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63R | T63R | 1 | 1 | 0 | 0 | 63 | T | R | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 8,532 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T16R | null | null | null | -0.47 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":28963,"numValue":-0.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28964,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14229 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,229 | train | mutant | 275 | 302 | 307 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63R | T63R | 1 | 1 | 0 | 0 | 63 | T | R | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 8,772 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:T16R | null | null | 8.86 | -0.2 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":29639,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29640,"numValue":8.86,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S983.csv"],"id":29641,"numValue... | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14230 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,230 | train | mutant | 275 | 302 | 307 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63R | T63R | 1 | 1 | 0 | 0 | 63 | T | R | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 9,821 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T16R | null | null | 9.56 | -0.74 | null | null | null | 4.8 | 1.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33684,"numValue":9.56,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33685,"numValue":-0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33686,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33687,"numValue":4.8,"references":[],... | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14231 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,231 | train | mutant | 275 | 302 | 307 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63R | T63R | 1 | 1 | 0 | 0 | 63 | T | R | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 9,964 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:T16R | null | null | 9.6 | -0.78 | null | null | null | 4.8 | 1.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":34235,"numValue":9.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34236,"numValue":-0.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34237,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34238,"numValue":4.8,"references":[],"... | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14232 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,232 | train | mutant | 275 | 302 | 307 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63R | T63R | 1 | 1 | 0 | 0 | 63 | T | R | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 10,726 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 50 mM | 25 | 1BNI_A:T16R | null | null | 9.23 | 0.78 | null | null | null | 4.75 | 1.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 700 | ARTICLE | Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles. | 1,990 | 10.1021/bi00492a006 | 2248951 | Biochemistry;29;9343-52 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":36864,"numValue":9.23,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36865,"numValue":0.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36866,"numValue":1.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36867,"numValue":4.75,"references":[],... | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14234 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,234 | train | mutant | 3,704 | 302 | 4,155 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63S | T63S | 1 | 1 | 0 | 0 | 63 | T | S | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 8,531 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T16S | null | null | null | 1.68 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["SAAFEC_S1262.csv"],"id":28961,"numValue":1.68,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28962,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14235 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,235 | train | mutant | 3,704 | 302 | 4,155 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63S | T63S | 1 | 1 | 0 | 0 | 63 | T | S | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 9,682 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:T16S | null | null | null | 1.87 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 651 | ARTICLE | Mapping the transition state and pathway of protein folding by protein engineering. | 1,989 | 10.1038/340122a0 | 2739734 | Nature;340;122-6 | 4 | Matouschek A|Serrano L|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv"],"id":33250,"numValue":1.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33251,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14236 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,236 | train | mutant | 3,704 | 302 | 4,155 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63S | T63S | 1 | 1 | 0 | 0 | 63 | T | S | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 9,820 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T16S | null | null | 7.46 | 1.36 | null | null | null | 3.6 | 2.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33679,"numValue":7.46,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33680,"numValue":1.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33681,"numValue":2.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33682,"numValue":3.6,... | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14238 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,238 | train | mutant | 3,913 | 302 | 4,415 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63A | T63A | 1 | 1 | 0 | 0 | 63 | T | A | 3 | CONSERVATION | 1BNI | 159 | null | 63 | A | H | false | false | 100.558748 | 36.005714 | 9,084 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:T16A | null | null | 8.3 | 0.5 | null | null | null | 4.43 | 1.88 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30860,"numValue":8.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30861,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30862,"numValue":1.88,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3086... | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14239 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,239 | train | mutant | 7,005 | 302 | 7,657 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63S|Y64A | T63S|Y64A | 2 | 2 | 0 | 0 | 63 | T | S | 3 | CONSERVATION | 1BNI | 159 | null | 63|64 | A | H | false | false | 111.682749 | 36.985773 | 15,146 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T16S 1BNI_A:Y17A | null | null | null | 2.55 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":[],"id":55570,"numValue":2.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55571,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14240 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,240 | train | mutant | 7,005 | 302 | 7,657 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T63S|Y64A | T63S|Y64A | 2 | 2 | 0 | 0 | 63 | T | S | 3 | CONSERVATION | 1BNI | 159 | null | 63|64 | A | H | false | false | 111.682749 | 36.985773 | 15,398 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:T16S 1BNI_A:Y17A | null | null | null | 2.39 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 744 | ARTICLE | COSMIC analysis of the major alpha-helix of barnase during folding. | 1,991 | 10.1016/0022-2836(91)90852-w | 2023260 | J Mol Biol;219;5-9 | 3 | Serrano L|Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":56525,"numValue":2.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56526,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20377,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14242 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,242 | train | mutant | 847 | 302 | 953 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y64G | Y64G | 1 | 1 | 0 | 0 | 64 | Y | G | 5 | CONSERVATION | 1BNI | 159 | null | 64 | A | H | false | false | 122.806749 | 37.965833 | 1,474 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:Y17G | 41.95 | -10.3 | null | null | null | null | 117.4 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:Y17G","type":"_PDB_CHAI... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":5401,"numValue":41.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],... | [{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14243 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,243 | train | mutant | 847 | 302 | 953 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y64G | Y64G | 1 | 1 | 0 | 0 | 64 | Y | G | 5 | CONSERVATION | 1BNI | 159 | null | 64 | A | H | false | false | 122.806749 | 37.965833 | 9,085 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y17G | null | null | 4.8 | 4 | null | null | null | 2.5 | 1.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30865,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":30866,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30867,"numValue":1.91,"re... | [{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14245 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,245 | train | mutant | 3,703 | 302 | 4,154 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y64A | Y64A | 1 | 1 | 0 | 0 | 64 | Y | A | 5 | CONSERVATION | 1BNI | 159 | null | 64 | A | H | false | false | 122.806749 | 37.965833 | 8,509 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:Y17A | null | null | null | 2.43 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":[],"id":28917,"numValue":2.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28918,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14246 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,246 | train | mutant | 3,703 | 302 | 4,154 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y64A | Y64A | 1 | 1 | 0 | 0 | 64 | Y | A | 5 | CONSERVATION | 1BNI | 159 | null | 64 | A | H | false | false | 122.806749 | 37.965833 | 9,822 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:Y17A | null | null | 7.15 | 1.67 | null | null | null | 3.5 | 2.02 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33689,"numValue":7.15,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33690,"numValue":1.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33691,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33692,"numValue":3.5,"references":[],"... | [{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14248 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,248 | train | mutant | 3,703 | 302 | 4,154 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y64A | Y64A | 1 | 1 | 0 | 0 | 64 | Y | A | 5 | CONSERVATION | 1BNI | 159 | null | 64 | A | H | false | false | 122.806749 | 37.965833 | 11,102 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y17A | null | null | null | 2.26 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 744 | ARTICLE | COSMIC analysis of the major alpha-helix of barnase during folding. | 1,991 | 10.1016/0022-2836(91)90852-w | 2023260 | J Mol Biol;219;5-9 | 3 | Serrano L|Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv"],"id":38226,"numValue":2.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38227,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14249 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,249 | train | mutant | 3,914 | 302 | 4,416 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y64S | Y64S | 1 | 1 | 0 | 0 | 64 | Y | S | 5 | CONSERVATION | 1BNI | 159 | null | 64 | A | H | false | false | 122.806749 | 37.965833 | 9,086 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y17S | null | null | 6.8 | 2 | null | null | null | 3.25 | 2.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30870,"numValue":6.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30871,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30872,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30873,"numValue":3.25,... | [{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14250 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,250 | train | mutant | 4,348 | 302 | 4,858 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y64F | Y64F | 1 | 1 | 0 | 0 | 64 | Y | F | 5 | CONSERVATION | 1BNI | 159 | null | 64 | A | H | false | false | 122.806749 | 37.965833 | 10,304 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Y17F | null | null | 9.57 | 0.58 | null | null | null | 4.43 | 2.16 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 671 | ARTICLE | Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. | 1,991 | 10.1016/0022-2836(91)90725-l | 2010920 | J Mol Biol;218;465-75 | 3 | Serrano L|Bycroft M|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":35329,"numValue":9.57,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":35330,"numValue":0.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35331,"numValue":2.16,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35... | [{"id":20378,"numValue":5.0,"position":64,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14251 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,251 | train | mutant | 3,692 | 302 | 4,143 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65Q | H65Q | 1 | 1 | 0 | 0 | 65 | H | Q | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 8,493 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:H18Q | null | null | null | 1.44 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["SAAFEC_S1262.csv"],"id":28885,"numValue":1.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28886,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14252 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,252 | train | mutant | 3,692 | 302 | 4,143 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65Q | H65Q | 1 | 1 | 0 | 0 | 65 | H | Q | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,681 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:H18Q | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 651 | ARTICLE | Mapping the transition state and pathway of protein folding by protein engineering. | 1,989 | 10.1038/340122a0 | 2739734 | Nature;340;122-6 | 4 | Matouschek A|Serrano L|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33248,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33249,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14253 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,253 | train | mutant | 3,915 | 302 | 4,417 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65G | H65G | 1 | 1 | 0 | 0 | 65 | H | G | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,087 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18G | null | null | 8.1 | 0.7 | null | null | null | 4.21 | 1.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30875,"numValue":8.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":30876,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30877,"numValue":1.91,"references":[],"strValue":null,"type":"M"},{"datasets... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14254 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,254 | train | mutant | 3,915 | 302 | 4,417 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65G | H65G | 1 | 1 | 0 | 0 | 65 | H | G | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 10,033 | ProTherm | 5.8 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:H18G | null | null | 10.02 | 0.98 | null | null | null | 5.12 | 1.85 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34472,"numValue":10.02,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":34473,"numValue":0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34474,"numValue":1.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34475,"numVa... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14255 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,255 | train | mutant | 3,915 | 302 | 4,417 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65G | H65G | 1 | 1 | 0 | 0 | 65 | H | G | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 10,037 | ProTherm | 9 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:H18G | null | null | 9.92 | -0.51 | null | null | null | 5.06 | 2.07 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34492,"numValue":9.92,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34493,"numValue":-0.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34494,"numValue":2.07,"references":[],"strValue":null,"type":... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14256 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,256 | train | mutant | 3,915 | 302 | 4,417 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65G | H65G | 1 | 1 | 0 | 0 | 65 | H | G | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 10,814 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1 M | 25 | 1BNI_A:H18G | null | null | 8.01 | 0.89 | 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 | 719 | ARTICLE | Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase. | 1,995 | 10.1021/bi00020a027 | 7756312 | Biochemistry;34;6805-14 | 2 | Fersht A R|Matthews J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1 M","type":"BUFFER_CO... | [{"datasets":[],"id":37216,"numValue":8.01,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37217,"numValue":0.89,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37218,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14257 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,257 | train | mutant | 3,916 | 302 | 4,418 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65A | H65A | 1 | 1 | 0 | 0 | 65 | H | A | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,088 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18A | null | null | 6.9 | 1.9 | null | null | null | 3.62 | 1.91 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30880,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":30881,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30882,"nu... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,258 | train | mutant | 3,916 | 302 | 4,418 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65A | H65A | 1 | 1 | 0 | 0 | 65 | H | A | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 10,813 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1 M | 25 | 1BNI_A:H18A | null | null | 6.75 | 2.15 | 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 | 719 | ARTICLE | Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase. | 1,995 | 10.1021/bi00020a027 | 7756312 | Biochemistry;34;6805-14 | 2 | Fersht A R|Matthews J M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1 M","type":"BUFFER_CO... | [{"datasets":[],"id":37213,"numValue":6.75,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37214,"numValue":2.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37215,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,259 | train | mutant | 3,917 | 302 | 4,419 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65S | H65S | 1 | 1 | 0 | 0 | 65 | H | S | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,089 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18S | null | null | 6.7 | 2.1 | null | null | null | 3.4 | 1.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30885,"numValue":6.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30886,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30887,"numValue":1.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30888,"numValue":3.4,"... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14260 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,260 | train | mutant | 3,918 | 302 | 4,420 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65N | H65N | 1 | 1 | 0 | 0 | 65 | H | N | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,090 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18N | null | null | 7 | 1.8 | null | null | null | 3.71 | 1.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30890,"numValue":7.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30891,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30892,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30893,"numValue":3.71,... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,261 | train | mutant | 3,919 | 302 | 4,421 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65D | H65D | 1 | 1 | 0 | 0 | 65 | H | D | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,091 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18D | null | null | 6.6 | 2.2 | null | null | null | 3.26 | 2.04 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30895,"numValue":6.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30896,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30897,"numValue":2.04,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30898,"numValue":3.26,... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,262 | train | mutant | 3,920 | 302 | 4,422 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65K | H65K | 1 | 1 | 0 | 0 | 65 | H | K | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,092 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18K | null | null | 7.9 | 0.9 | null | null | null | 3.96 | 1.99 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30900,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30901,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30902,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30903,"numValue":3.96,... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14263 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,263 | train | mutant | 3,920 | 302 | 4,422 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65K | H65K | 1 | 1 | 0 | 0 | 65 | H | K | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,965 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:H18K | null | null | 7.9 | 0.92 | null | null | null | 3.9 | 2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":34240,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34241,"numValue":0.92,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34242,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34243,"numValue":3.9,"... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14264 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,264 | train | mutant | 3,921 | 302 | 4,423 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65R | H65R | 1 | 1 | 0 | 0 | 65 | H | R | 3 | CONSERVATION | 1BNI | 159 | null | 65 | A | S | true | false | 104.073268 | 34.247001 | 9,093 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18R | null | null | 7.8 | 1 | null | null | null | 3.97 | 1.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":30905,"numValue":7.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30906,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30907,"numValue":1.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30908,"numValue":3.97,... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,265 | train | mutant | 7,008 | 302 | 7,661 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65A|W141L | H65A|W141L | 2 | 2 | 0 | 0 | 65 | H | A | 3 | CONSERVATION | 1BNI | 159 | null | 65|141 | A | S|L | true | false | 83.372859 | 28.914215 | 15,191 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18A 1BNI_A:W94L | null | null | 6.5 | 2.3 | null | null | null | 3.36 | 1.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":55688,"numValue":6.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55689,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55690,"numValue":1.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55691,"numValue":3.36,"references":[],"s... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14266 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,266 | train | mutant | 7,009 | 302 | 7,662 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65S|W141L | H65S|W141L | 2 | 2 | 0 | 0 | 65 | H | S | 3 | CONSERVATION | 1BNI | 159 | null | 65|141 | A | S|L | true | false | 83.372859 | 28.914215 | 15,192 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18S 1BNI_A:W94L | null | null | 6 | 2.8 | null | null | null | 3.24 | 1.86 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":55693,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55694,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55695,"numValue":1.86,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55696,"numValue":3.24,"references":[],"s... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,268 | train | mutant | 7,011 | 302 | 7,664 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65K|W141L | H65K|W141L | 2 | 2 | 0 | 0 | 65 | H | K | 3 | CONSERVATION | 1BNI | 159 | null | 65|141 | A | S|L | true | false | 83.372859 | 28.914215 | 15,194 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18K 1BNI_A:W94L | null | null | 6.1 | 2.7 | null | null | null | 3.37 | 1.8 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":55703,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55704,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55705,"numValue":1.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55706,"numValue":3.37,"references":[],"st... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,269 | train | mutant | 7,012 | 302 | 7,665 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65R|W141L | H65R|W141L | 2 | 2 | 0 | 0 | 65 | H | R | 3 | CONSERVATION | 1BNI | 159 | null | 65|141 | A | S|L | true | false | 83.372859 | 28.914215 | 15,195 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:H18R 1BNI_A:W94L | null | null | 7.2 | 1.6 | null | null | null | 3.48 | 2.06 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 620 | ARTICLE | Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. | 1,992 | 10.1016/0022-2836(92)90906-z | 1404368 | J Mol Biol;227;544-59 | 4 | Serrano L|Sancho J|Fersht A R|Hirshberg M | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":[],"id":55708,"numValue":7.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55709,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55710,"numValue":2.06,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55711,"numValue":3.48,"references":[],"s... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14271 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,271 | train | mutant | 7,083 | 302 | 7,736 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65G|W141L | H65G|W141L | 2 | 2 | 0 | 0 | 65 | H | G | 3 | CONSERVATION | 1BNI | 159 | null | 65|141 | A | S|L | true | false | 83.372859 | 28.914215 | 15,281 | ProTherm | 9 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:H18G 1BNI_A:W94L | null | null | 9.72 | -0.31 | null | null | null | 4.96 | 1.8 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":56045,"numValue":9.72,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56046,"numValue":-0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56047,"numValue":1.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56048,"numValue":4.96,"references":[],... | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14272 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,272 | train | mutant | 7,083 | 302 | 7,736 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65G|W141L | H65G|W141L | 2 | 2 | 0 | 0 | 65 | H | G | 3 | CONSERVATION | 1BNI | 159 | null | 65|141 | A | S|L | true | false | 83.372859 | 28.914215 | 15,320 | ProTherm | 5.9 | NMR | Urea | MES | 30 mM | 25 | NaCl | 1 M | 1BNI_A:H18G 1BNI_A:W94L | null | null | 8.11 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":5.9,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":56228,"numValue":8.11,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56229,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,273 | train | mutant | 7,083 | 302 | 7,736 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H65G|W141L | H65G|W141L | 2 | 2 | 0 | 0 | 65 | H | G | 3 | CONSERVATION | 1BNI | 159 | null | 65|141 | A | S|L | true | false | 83.372859 | 28.914215 | 15,322 | ProTherm | 8.9 | NMR | Urea | Tris | 30 mM | 25 | NaCl | 1 M | 1BNI_A:H18G 1BNI_A:W94L | null | null | 8.38 | -0.33 | 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 | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":8.9,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":56233,"numValue":8.38,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56234,"numValue":-0.33,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56235,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20379,"numValue":3.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,274 | train | mutant | 4,291 | 302 | 4,799 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K66R | K66R | 1 | 1 | 0 | 0 | 66 | K | R | 3 | CONSERVATION | 1BNI | 159 | null | 66 | A | S | true | false | 66.379247 | 26.986667 | 9,966 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:K19R | null | null | 9.7 | -0.88 | null | null | null | 4.6 | 2.08 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":34245,"numValue":9.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34246,"numValue":-0.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34247,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34248,"numValue":4.6... | [{"id":20380,"numValue":3.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,275 | train | mutant | 281 | 302 | 313 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D69M | D69M | 1 | 1 | 0 | 0 | 69 | D | M | 3 | CONSERVATION | 1BNI | 159 | null | 69 | A | T | true | false | 136.7539 | 27.2875 | 496 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:D22M | 50.06 | -1.57 | null | null | 128.8 | null | 128.4 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08 mM,13.92 mM,","type":"BUFFER_CONC"},{"numValue":null,"strV... | [{"datasets":[],"id":2001,"numValue":50.06,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2002,"numValue":-1.57,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2003,"numValue":128.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20383,"numValue":3.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,276 | train | mutant | 281 | 302 | 313 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D69M | D69M | 1 | 1 | 0 | 0 | 69 | D | M | 3 | CONSERVATION | 1BNI | 159 | null | 69 | A | T | true | false | 136.7539 | 27.2875 | 8,779 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:D22M | null | null | 8.39 | 0.27 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":29667,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29668,"numValue":8.39,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":29669,"numValue":0.27,"references... | [{"id":20383,"numValue":3.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,279 | train | mutant | 3,707 | 302 | 4,158 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N70A | N70A | 1 | 1 | 0 | 0 | 70 | N | A | 7 | CONSERVATION | 1BNI | 159 | null | 70 | A | T | false | false | 14.593535 | 19.94875 | 9,823 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:N23A | null | null | 6.62 | 2.2 | null | null | null | 3.4 | 1.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33694,"numValue":6.62,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":33695,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33696,"numValue":1.94,"references":[],"strV... | [{"id":20384,"numValue":7.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14280 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,280 | train | mutant | 4,254 | 302 | 4,761 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y71F | Y71F | 1 | 1 | 0 | 0 | 71 | Y | F | 8 | CONSERVATION | 1BNI | 159 | null | 71 | A | E | true | false | 18.334664 | 14.4025 | 9,824 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:Y24F | null | null | 8.91 | -0.09 | null | null | null | 4.5 | 1.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":33699,"numValue":8.91,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":33700,"numValue":-0.09,"references":[],"strValue":null,"type"... | [{"id":20385,"numValue":8.0,"position":71,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,281 | train | mutant | 3,708 | 302 | 4,159 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I72V | I72V | 1 | 1 | 0 | 0 | 72 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 72 | A | E | false | false | 18.811932 | 13.1975 | 8,514 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:I25V | null | null | null | 1.12 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":28927,"numValue":1.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28928,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20386,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,282 | train | mutant | 3,708 | 302 | 4,159 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I72V | I72V | 1 | 1 | 0 | 0 | 72 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 72 | A | E | false | false | 18.811932 | 13.1975 | 8,656 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I25V | null | null | null | 1.18 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 597 | ARTICLE | The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90564-z | 1569559 | J Mol Biol;224;819-35 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":29366,"numValue":1.18,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29367,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20386,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,283 | train | mutant | 3,708 | 302 | 4,159 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I72V | I72V | 1 | 1 | 0 | 0 | 72 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 72 | A | E | false | false | 18.811932 | 13.1975 | 9,825 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I25V | null | null | 7.99 | 0.83 | null | null | null | 4 | 2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33704,"numValue":7.99,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33705,"numValue":0.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33706,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33707,"numValue":4.0,"... | [{"id":20386,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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