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:14284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,284 | train | mutant | 4,255 | 302 | 4,762 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I72A | I72A | 1 | 1 | 0 | 0 | 72 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 72 | A | E | false | false | 18.811932 | 13.1975 | 9,826 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I25A | null | null | 5.14 | 3.68 | null | null | null | 2.7 | 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|_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":33709,"numValue":5.14,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33710,"numValue":3.68,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33711,"numValue":1.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33712,"numValue":2.7... | [{"id":20386,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,285 | train | mutant | 276 | 302 | 308 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73G | T73G | 1 | 1 | 0 | 0 | 73 | T | G | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 490 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:T26G | 47.57 | -4.06 | null | null | 111.9 | null | 118.5 | 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":1971,"numValue":47.57,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1972,"numValue":-4.06,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1973,"numValue":111.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,286 | train | mutant | 276 | 302 | 308 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73G | T73G | 1 | 1 | 0 | 0 | 73 | T | G | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 8,516 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T26G | null | null | null | 1.42 | 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":28931,"numValue":1.42,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28932,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,287 | train | mutant | 276 | 302 | 308 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73G | T73G | 1 | 1 | 0 | 0 | 73 | T | G | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 8,773 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:T26G | null | null | 6.58 | 2.08 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.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":29643,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29644,"numValue":6.58,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29645,"numValue":2.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29646,"numVa... | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,288 | train | mutant | 276 | 302 | 308 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73G | T73G | 1 | 1 | 0 | 0 | 73 | T | G | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,646 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T26G | null | null | null | 1.58 | 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|_PDB_CHAIN_MUTATION | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | 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":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":33111,"numValue":1.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33112,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,289 | train | mutant | 276 | 302 | 308 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73G | T73G | 1 | 1 | 0 | 0 | 73 | T | G | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,827 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T26G | null | null | 7.81 | 1.01 | null | null | null | 3.8 | 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":33714,"numValue":7.81,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33715,"numValue":1.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33716,"numValue":2.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33717,"numValue":3.8,... | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,290 | train | mutant | 3,709 | 302 | 4,160 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73A | T73A | 1 | 1 | 0 | 0 | 73 | T | A | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 8,515 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T26A | null | null | null | 1.93 | 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":28929,"numValue":1.93,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28930,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,291 | train | mutant | 3,709 | 302 | 4,160 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73A | T73A | 1 | 1 | 0 | 0 | 73 | T | A | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,645 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T26A | null | null | null | 2.11 | 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 | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | 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":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":33109,"numValue":2.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33110,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,292 | train | mutant | 3,709 | 302 | 4,160 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73A | T73A | 1 | 1 | 0 | 0 | 73 | T | A | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,680 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:T26A | null | null | null | 2.14 | 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":33246,"numValue":2.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33247,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,293 | train | mutant | 3,709 | 302 | 4,160 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73A | T73A | 1 | 1 | 0 | 0 | 73 | T | A | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,828 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T26A | null | null | 7.15 | 1.67 | null | null | null | 3.5 | 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":33719,"numValue":7.15,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33720,"numValue":1.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33721,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33722,"numValue":3.5,"references":[],"s... | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,294 | train | mutant | 3,922 | 302 | 4,424 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73D | T73D | 1 | 1 | 0 | 0 | 73 | T | D | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,094 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:T26D | null | null | 8.8 | 0 | null | null | null | 4.53 | 1.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv|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":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30910,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30911,"numValue":0.0,"r... | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,296 | train | mutant | 4,215 | 302 | 4,720 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73V | T73V | 1 | 1 | 0 | 0 | 73 | T | V | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,644 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T26V | null | null | null | 2.31 | 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 | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | 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":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":33107,"numValue":2.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33108,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,297 | train | mutant | 4,216 | 302 | 4,721 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73N | T73N | 1 | 1 | 0 | 0 | 73 | T | N | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,647 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T26N | null | null | null | 1.29 | 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 | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | 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":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33113,"numValue":1.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33114,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,298 | train | mutant | 4,217 | 302 | 4,722 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73Q | T73Q | 1 | 1 | 0 | 0 | 73 | T | Q | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,648 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T26Q | null | null | null | 1.72 | 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 | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | 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":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33115,"numValue":1.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33116,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,299 | train | mutant | 4,218 | 302 | 4,723 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73E | T73E | 1 | 1 | 0 | 0 | 73 | T | E | 9 | CONSERVATION | 1BNI | 159 | null | 73 | A | L | true | false | 37.605251 | 13.372857 | 9,649 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:T26E | null | null | null | 0.05 | 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 | 647 | ARTICLE | Capping and alpha-helix stability. | 1,989 | 10.1038/342296a0 | 2812029 | Nature;342;296-9 | 2 | 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":"19.3 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":33117,"numValue":0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33118,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,300 | train | mutant | 7,105 | 302 | 7,758 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73H|D101N | T73H|D101N | 2 | 2 | 0 | 0 | 73 | T | H | 9 | CONSERVATION | 1BNI | 159 | null | 73|101 | A | L|E | true | false | 33.33083 | 14.263303 | 15,321 | ProTherm | 4.4 | NMR | Urea | Sodium acetate | 30 mM | 25 | NaCl | 1 M | 1BNI_A:T26H 1BNI_A:D54N | null | null | 2.39 | 5.74 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":4.4,"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFE... | [{"datasets":[],"id":56230,"numValue":2.39,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56231,"numValue":5.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56232,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14301 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,301 | train | mutant | 7,105 | 302 | 7,758 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T73H|D101N | T73H|D101N | 2 | 2 | 0 | 0 | 73 | T | H | 9 | CONSERVATION | 1BNI | 159 | null | 73|101 | A | L|E | true | false | 33.33083 | 14.263303 | 15,323 | ProTherm | 8.9 | NMR | Urea | Tris | 30 mM | 25 | NaCl | 1 M | 1BNI_A:T26H 1BNI_A:D54N | null | null | 3.78 | 4.27 | 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":56236,"numValue":3.78,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56237,"numValue":4.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56238,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20387,"numValue":9.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,302 | train | mutant | 3,923 | 302 | 4,425 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K74G | K74G | 1 | 1 | 0 | 0 | 74 | K | G | 9 | CONSERVATION | 1BNI | 159 | null | 74 | A | H | false | false | 63.260027 | 17.217778 | 9,095 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:K27G | null | null | 9 | -0.2 | null | null | null | 4.29 | 2.11 | 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":30915,"numValue":9.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30916,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30917,"numValue":2.11,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30918,"numValue":4.29,"references":[],"... | [{"id":20388,"numValue":9.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,303 | train | mutant | 3,923 | 302 | 4,425 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K74G | K74G | 1 | 1 | 0 | 0 | 74 | K | G | 9 | CONSERVATION | 1BNI | 159 | null | 74 | A | H | false | false | 63.260027 | 17.217778 | 9,829 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:K27G | null | null | 8.44 | 0.38 | null | null | null | 4.3 | 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":33724,"numValue":8.44,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":33725,"numValue":0.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33726,"numValue":1.94,"references":[],"str... | [{"id":20388,"numValue":9.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,304 | train | mutant | 4,574 | 302 | 5,094 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K74A | K74A | 1 | 1 | 0 | 0 | 74 | K | A | 9 | CONSERVATION | 1BNI | 159 | null | 74 | A | H | false | false | 63.260027 | 17.217778 | 10,756 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:K27A | null | null | 9.19 | -0.36 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 706 | ARTICLE | Effect of active site residues in barnase on activity and stability. | 1,992 | 10.1016/0022-2836(92)90387-y | 1602471 | J Mol Biol;225;585-9 | 3 | Serrano L|Fersht A R|Meiering E 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":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":36998,"numValue":9.19,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":36999,"numValue":-0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37000,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20388,"numValue":9.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,305 | train | mutant | 4,574 | 302 | 5,094 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K74A | K74A | 1 | 1 | 0 | 0 | 74 | K | A | 9 | CONSERVATION | 1BNI | 159 | null | 74 | A | H | false | false | 63.260027 | 17.217778 | 10,815 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1 M | 25 | 1BNI_A:K27A | null | null | 9.43 | -0.53 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | SAAFEC_S1262.csv | 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":37219,"numValue":9.43,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":37220,"numValue":-0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37221,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20388,"numValue":9.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,306 | train | mutant | 3,924 | 302 | 4,426 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S75G | S75G | 1 | 1 | 0 | 0 | 75 | S | G | 2 | CONSERVATION | 1BNI | 159 | null | 75 | A | H | false | false | 77.045494 | 13.698333 | 9,096 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:S28G | null | null | 8.3 | 0.5 | null | null | null | 4.34 | 1.88 | 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|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":30920,"numValue":8.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30921,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30922,"... | [{"id":20389,"numValue":2.0,"position":75,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,307 | train | mutant | 3,925 | 302 | 4,427 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S75A | S75A | 1 | 1 | 0 | 0 | 75 | S | A | 2 | CONSERVATION | 1BNI | 159 | null | 75 | A | H | false | false | 77.045494 | 13.698333 | 9,097 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:S28A | null | null | 9.4 | -0.6 | null | null | null | 4.78 | 1.98 | 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":30925,"numValue":9.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":30926,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30927,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":309... | [{"id":20389,"numValue":2.0,"position":75,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14308 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,308 | train | mutant | 4,178 | 302 | 4,683 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S75E | S75E | 1 | 1 | 0 | 0 | 75 | S | E | 2 | CONSERVATION | 1BNI | 159 | null | 75 | A | H | false | false | 77.045494 | 13.698333 | 9,546 | ProTherm | 6.3 | Fluorescence | Urea | MES | 10 mM | 25 | 1BNI_A:S28E | null | null | 9.44 | -0.61 | null | null | null | 4.74 | 1.99 | 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 | 643 | ARTICLE | Surface electrostatic interactions contribute little of stability of barnase. | 1,991 | 10.1016/0022-2836(91)90117-o | 1870131 | J Mol Biol;220;779-88 | 3 | Bycroft M|Fersht A R|Sali D | [{"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":"10 mM","type":"BUFFER_... | [{"datasets":[],"id":32671,"numValue":9.44,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":32672,"numValue":-0.61,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":32673,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3... | [{"id":20389,"numValue":2.0,"position":75,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,309 | train | mutant | 3,710 | 302 | 4,161 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E76G | E76G | 1 | 1 | 0 | 0 | 76 | E | G | 6 | CONSERVATION | 1BNI | 159 | null | 76 | A | H | true | false | 85.739848 | 17.75 | 8,517 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:E29G | null | null | null | 1.76 | 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_S983.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_S983.csv"],"id":28933,"numValue":1.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28934,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20390,"numValue":6.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,310 | train | mutant | 3,710 | 302 | 4,161 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E76G | E76G | 1 | 1 | 0 | 0 | 76 | E | G | 6 | CONSERVATION | 1BNI | 159 | null | 76 | A | H | true | false | 85.739848 | 17.75 | 8,657 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:E29G | null | null | null | 1.9 | 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|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","SAAFEC_S1262.csv"],"id":29368,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29369,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20390,"numValue":6.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,311 | train | mutant | 3,710 | 302 | 4,161 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E76G | E76G | 1 | 1 | 0 | 0 | 76 | E | G | 6 | CONSERVATION | 1BNI | 159 | null | 76 | A | H | true | false | 85.739848 | 17.75 | 9,098 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:E29G | null | null | 6.6 | 2.2 | null | null | null | 3.64 | 1.81 | 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":30930,"numValue":6.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30931,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30932,"numValue":1.81,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30933,"numValue":3.64,"references":[],"s... | [{"id":20390,"numValue":6.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,312 | train | mutant | 3,710 | 302 | 4,161 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E76G | E76G | 1 | 1 | 0 | 0 | 76 | E | G | 6 | CONSERVATION | 1BNI | 159 | null | 76 | A | H | true | false | 85.739848 | 17.75 | 9,830 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:E29G | null | null | 6.77 | 2.05 | null | null | null | 3.6 | 1.84 | 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":33729,"numValue":6.77,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33730,"numValue":2.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33731,"numValue":1.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33732,"numValue":3.6... | [{"id":20390,"numValue":6.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,313 | train | mutant | 3,926 | 302 | 4,428 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E76A | E76A | 1 | 1 | 0 | 0 | 76 | E | A | 6 | CONSERVATION | 1BNI | 159 | null | 76 | A | H | true | false | 85.739848 | 17.75 | 9,099 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:E29A | null | null | 7.6 | 1.2 | null | null | null | 3.93 | 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|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":30935,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":30936,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30937,"numValue":1.94,"re... | [{"id":20390,"numValue":6.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,315 | train | mutant | 3,927 | 302 | 4,429 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E76S | E76S | 1 | 1 | 0 | 0 | 76 | E | S | 6 | CONSERVATION | 1BNI | 159 | null | 76 | A | H | true | false | 85.739848 | 17.75 | 9,100 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:E29S | null | null | 7.6 | 1.2 | null | null | null | 3.94 | 1.93 | 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":30940,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":30941,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30942,"numValue":1.93,"re... | [{"id":20390,"numValue":6.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,317 | train | mutant | 3,928 | 302 | 4,430 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q78G | Q78G | 1 | 1 | 0 | 0 | 78 | Q | G | 3 | CONSERVATION | 1BNI | 159 | null | 78 | A | H | false | false | 103.748188 | 17.838889 | 9,101 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Q31G | null | null | 7.7 | 1.1 | null | null | null | 4.07 | 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":30945,"numValue":7.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30946,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30947,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30948,"numValue":4.07,... | [{"id":20392,"numValue":3.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,318 | train | mutant | 3,929 | 302 | 4,431 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q78S | Q78S | 1 | 1 | 0 | 0 | 78 | Q | S | 3 | CONSERVATION | 1BNI | 159 | null | 78 | A | H | false | false | 103.748188 | 17.838889 | 9,102 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Q31S | null | null | 9.1 | -0.3 | null | null | null | 4.44 | 2.05 | 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|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":30950,"numValue":9.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":30951,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"dataset... | [{"id":20392,"numValue":3.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,319 | train | mutant | 3,929 | 302 | 4,431 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q78S | Q78S | 1 | 1 | 0 | 0 | 78 | Q | S | 3 | CONSERVATION | 1BNI | 159 | null | 78 | A | H | false | false | 103.748188 | 17.838889 | 9,831 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:Q31S | null | null | 8.89 | -0.07 | null | null | null | 4.4 | 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":33734,"numValue":8.89,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33735,"numValue":-0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33736,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33737,"numValue":4.4,"references":[],"... | [{"id":20392,"numValue":3.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,320 | train | mutant | 3,929 | 302 | 4,431 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q78S | Q78S | 1 | 1 | 0 | 0 | 78 | Q | S | 3 | CONSERVATION | 1BNI | 159 | null | 78 | A | H | false | false | 103.748188 | 17.838889 | 9,968 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Q31S | null | null | 9.1 | -0.28 | null | null | null | 4.4 | 2.05 | 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|SAAFEC_S1262.csv|SAAFEC_S983.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":34255,"numValue":9.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34256,"numValue":-0.28,"references":[],"strValue":null,"typ... | [{"id":20392,"numValue":3.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,321 | train | mutant | 3,930 | 302 | 4,432 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q78A | Q78A | 1 | 1 | 0 | 0 | 78 | Q | A | 3 | CONSERVATION | 1BNI | 159 | null | 78 | A | H | false | false | 103.748188 | 17.838889 | 9,103 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:Q31A | null | null | 8.5 | 0.3 | null | null | null | 4.62 | 1.83 | 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":30955,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30956,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30957,"numValue":1.83,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30958,"numValue":4.62,"references":[],"s... | [{"id":20392,"numValue":3.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,323 | train | mutant | 3,947 | 302 | 4,449 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79R | A79R | 1 | 1 | 0 | 0 | 79 | A | R | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,142 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32R | null | null | 8.63 | 0.2 | null | null | null | 4.5 | 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|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31115,"numValue":8.63,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31116,"numValue":0.2,"references":[],"strValue":null,"type... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,324 | train | mutant | 3,948 | 302 | 4,450 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79K | A79K | 1 | 1 | 0 | 0 | 79 | A | K | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,143 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32K | null | null | 8.73 | 0.1 | null | null | null | 4.5 | 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|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31120,"numValue":8.73,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31121,"numValue":0.1,"references":[],"strValue":null,"type... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,325 | train | mutant | 3,949 | 302 | 4,451 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79M | A79M | 1 | 1 | 0 | 0 | 79 | A | M | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,144 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32M | null | null | 8.75 | 0.08 | null | null | null | 4.4 | 1.97 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31125,"numValue":8.75,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31126,"numValue":0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31127,"numValue":1.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,326 | train | mutant | 3,950 | 302 | 4,452 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79L | A79L | 1 | 1 | 0 | 0 | 79 | A | L | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,145 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32L | null | null | 8.91 | -0.08 | null | null | null | 4.4 | 2.02 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31130,"numValue":8.91,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31131,"numValue":-0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31132,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,327 | train | mutant | 3,951 | 302 | 4,453 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79S | A79S | 1 | 1 | 0 | 0 | 79 | A | S | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,146 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32S | null | null | 8.67 | 0.16 | null | null | null | 4.3 | 1.98 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31135,"numValue":8.67,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31136,"numValue":0.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31137,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,328 | train | mutant | 3,952 | 302 | 4,454 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79Q | A79Q | 1 | 1 | 0 | 0 | 79 | A | Q | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,147 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32Q | null | null | 8.48 | 0.35 | null | null | null | 4.3 | 1.95 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31140,"numValue":8.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31141,"numValue":0.35,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31142,"numValue":1.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14329 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,329 | train | mutant | 3,953 | 302 | 4,455 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79E | A79E | 1 | 1 | 0 | 0 | 79 | A | E | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,148 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32E | null | null | 8.96 | -0.13 | null | null | null | 4.3 | 2.08 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31145,"numValue":8.96,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31146,"numValue":-0.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31147,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14330 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,330 | train | mutant | 3,954 | 302 | 4,456 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79N | A79N | 1 | 1 | 0 | 0 | 79 | A | N | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,149 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32N | null | null | 8.5 | 0.33 | null | null | null | 4.2 | 2 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31150,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31151,"numValue":0.33,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31152,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3115... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,331 | train | mutant | 3,955 | 302 | 4,457 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79F | A79F | 1 | 1 | 0 | 0 | 79 | A | F | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,150 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32F | null | null | 8.4 | 0.43 | null | null | null | 4.2 | 1.98 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31155,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31156,"numValue":0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31157,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":311... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14332 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,332 | train | mutant | 3,956 | 302 | 4,458 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79D | A79D | 1 | 1 | 0 | 0 | 79 | A | D | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,151 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32D | null | null | 8.42 | 0.41 | null | null | null | 4.2 | 1.99 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31160,"numValue":8.42,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31161,"numValue":0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31162,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,333 | train | mutant | 3,957 | 302 | 4,459 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79H | A79H | 1 | 1 | 0 | 0 | 79 | A | H | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,152 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32H | null | null | 8.13 | 0.7 | null | null | null | 4.1 | 1.94 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31165,"numValue":8.13,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":31166,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31167,"numValue":1.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31168,"numValue":4.1,... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,336 | train | mutant | 3,960 | 302 | 4,462 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79Y | A79Y | 1 | 1 | 0 | 0 | 79 | A | Y | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,155 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32Y | null | null | 8.13 | 0.7 | null | null | null | 4.1 | 1.95 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31180,"numValue":8.13,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":31181,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31182,"numValue":1.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31183,"numValue":4.1,... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14337 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,337 | train | mutant | 3,961 | 302 | 4,463 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79V | A79V | 1 | 1 | 0 | 0 | 79 | A | V | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,156 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32V | null | null | 8.49 | 0.34 | null | null | null | 4.1 | 2.05 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31185,"numValue":8.49,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":31186,"numValue":0.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31187,"numValue":2.05,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,338 | train | mutant | 3,962 | 302 | 4,464 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79G | A79G | 1 | 1 | 0 | 0 | 79 | A | G | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,157 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32G | null | null | 8.18 | 0.65 | null | null | null | 4.1 | 1.98 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31190,"numValue":8.18,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":31191,"numValue":0.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31192,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31193,"numValue":4.1,... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,339 | train | mutant | 3,962 | 302 | 4,464 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79G | A79G | 1 | 1 | 0 | 0 | 79 | A | G | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 10,817 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1 M | 25 | 1BNI_A:A32G | null | null | 7.99 | 0.91 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|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 | 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":37225,"numValue":7.99,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":37226,"numValue":0.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37227,"numValue":null,"references":[],"str... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,340 | train | mutant | 3,963 | 302 | 4,465 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79W | A79W | 1 | 1 | 0 | 0 | 79 | A | W | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,158 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32W | null | null | 7.69 | 1.14 | null | null | null | 4 | 1.88 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31195,"numValue":7.69,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":31196,"numValue":1.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31197,"numValue":1.88,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31198,"numValue":4.0... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,341 | train | mutant | 3,964 | 302 | 4,466 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79C | A79C | 1 | 1 | 0 | 0 | 79 | A | C | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,159 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32C | null | null | 6.98 | 1.85 | null | null | null | 4 | 1.71 | 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 | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31200,"numValue":6.98,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":31201,"numValue":1.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31202,"numValue":1.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31203,"numValue":4.0... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,342 | train | mutant | 3,965 | 302 | 4,467 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A79P | A79P | 1 | 1 | 0 | 0 | 79 | A | P | 1 | CONSERVATION | 1BNI | 159 | null | 79 | A | H | false | false | 89.380682 | 10.118 | 9,160 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A32P | null | null | 4.71 | 4.12 | null | null | null | 2.4 | 1.89 | 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|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 624 | ARTICLE | Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. | 1,992 | 10.1016/0022-2836(92)90907-2 | 1404369 | J Mol Biol;227;560-8 | 3 | Horovitz A|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":31205,"numValue":4.71,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":31206,"numValue":4.12,"references":[],"strValue":null,"type":"DDG"},{"datase... | [{"id":20393,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14343 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,343 | train | mutant | 3,711 | 302 | 4,162 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L80Q | L80Q | 1 | 1 | 0 | 0 | 80 | L | Q | 4 | CONSERVATION | 1BNI | 159 | null | 80 | A | T | false | false | 95.152213 | 11.4675 | 8,518 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:L33Q | null | null | null | 1.3 | 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|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","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":28935,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28936,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY... | [{"id":20394,"numValue":4.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14345 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,345 | train | mutant | 3,931 | 302 | 4,433 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81A | G81A | 1 | 1 | 0 | 0 | 81 | G | A | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 9,104 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:G34A | null | null | 6.1 | 2.7 | null | null | null | 2.97 | 2.06 | 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":30960,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30961,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30962,"numValue":2.06,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30963,"numValue":2.97,... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14346 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,346 | train | mutant | 3,932 | 302 | 4,434 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81S | G81S | 1 | 1 | 0 | 0 | 81 | G | S | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 9,105 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:G34S | null | null | 5.9 | 2.9 | null | null | null | 2.93 | 2.03 | 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":30965,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30966,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30967,"numValue":2.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30968,"numValue":2.93,... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14347 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,347 | train | mutant | 3,933 | 302 | 4,435 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81N | G81N | 1 | 1 | 0 | 0 | 81 | G | N | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 9,106 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:G34N | null | null | 6.1 | 2.7 | null | null | null | 3.16 | 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|potapov_with_uniprot_mapping.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":30970,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":30971,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14348 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,348 | train | mutant | 3,934 | 302 | 4,436 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81D | G81D | 1 | 1 | 0 | 0 | 81 | G | D | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 9,107 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:G34D | null | null | 5.6 | 3.2 | null | null | null | 2.83 | 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":30975,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30976,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30977,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30978,"numValue":2.83,... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,349 | train | mutant | 3,935 | 302 | 4,437 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81H | G81H | 1 | 1 | 0 | 0 | 81 | G | H | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 9,108 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:G34H | null | null | 6.5 | 2.3 | null | null | null | 3.21 | 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|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":30980,"numValue":6.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30981,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30982,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30983,"numValue":3.21,... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,350 | train | mutant | 3,935 | 302 | 4,437 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81H | G81H | 1 | 1 | 0 | 0 | 81 | G | H | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 10,765 | ProTherm | 4.4 | NMR | Urea | Sodium acetate | 30 mM | 25 | NaCl | 1 M | 1BNI_A:G34H | null | null | 5.53 | 2.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|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 | 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":4.4,"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFE... | [{"datasets":[],"id":37024,"numValue":5.53,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":37025,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37026,"numValue":null,"references":[],"strV... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,351 | train | mutant | 3,935 | 302 | 4,437 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81H | G81H | 1 | 1 | 0 | 0 | 81 | G | H | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 10,769 | ProTherm | 8.9 | NMR | Urea | Tris | 30 mM | 25 | NaCl | 1 M | 1BNI_A:G34H | null | null | 4.9 | 3.15 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv | 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":37036,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":37037,"numValue":3.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37038,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14352 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,352 | train | mutant | 3,936 | 302 | 4,438 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81K | G81K | 1 | 1 | 0 | 0 | 81 | G | K | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 9,109 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:G34K | null | null | 6.1 | 2.7 | null | null | null | 2.97 | 2.06 | 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":30985,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30986,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30987,"numValue":2.06,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30988,"numValue":2.97,... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14354 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,354 | train | mutant | 3,938 | 302 | 4,440 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G81T | G81T | 1 | 1 | 0 | 0 | 81 | G | T | 9 | CONSERVATION | 1BNI | 159 | null | 81 | A | T | false | false | 35.55793 | 7.8725 | 9,111 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:G34T | null | null | 5.6 | 3.2 | null | null | null | 2.84 | 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":30995,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30996,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30997,"numValue":1.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30998,"numValue":2.84,... | [{"id":20395,"numValue":9.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,355 | train | mutant | 3,712 | 302 | 4,163 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V83T | V83T | 1 | 1 | 0 | 0 | 83 | V | T | 2 | CONSERVATION | 1BNI | 159 | null | 83 | A | L | false | true | 66.647988 | 9.408571 | 8,519 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:V36T | null | null | null | 1.15 | 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":28937,"numValue":1.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28938,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20397,"numValue":2.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,357 | train | mutant | 3,712 | 302 | 4,163 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V83T | V83T | 1 | 1 | 0 | 0 | 83 | V | T | 2 | CONSERVATION | 1BNI | 159 | null | 83 | A | L | false | true | 66.647988 | 9.408571 | 9,835 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:V36T | null | null | 7.77 | 1.05 | null | null | null | 3.9 | 1.95 | 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|_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":33754,"numValue":7.77,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":33755,"numValue":1.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33756,"numValue":1.95,"... | [{"id":20397,"numValue":2.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14359 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,359 | train | mutant | 3,713 | 302 | 4,164 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V83A | V83A | 1 | 1 | 0 | 0 | 83 | V | A | 2 | CONSERVATION | 1BNI | 159 | null | 83 | A | L | false | true | 66.647988 | 9.408571 | 8,659 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:V36A | null | null | null | 1.34 | 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|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","SAAFEC_S1262.csv"],"id":29372,"numValue":1.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29373,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20397,"numValue":2.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14360 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,360 | train | mutant | 3,713 | 302 | 4,164 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V83A | V83A | 1 | 1 | 0 | 0 | 83 | V | A | 2 | CONSERVATION | 1BNI | 159 | null | 83 | A | L | false | true | 66.647988 | 9.408571 | 9,834 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:V36A | null | null | 7.14 | 1.68 | null | null | null | 3.9 | 1.83 | 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":33749,"numValue":7.14,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33750,"numValue":1.68,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33751,"numValue":1.83,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33752,"numValue":3.9,"references":[],"... | [{"id":20397,"numValue":2.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,362 | train | mutant | 3,714 | 302 | 4,165 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N88D | N88D | 1 | 1 | 0 | 0 | 88 | N | D | 8 | CONSERVATION | 1BNI | 159 | null | 88 | A | L | false | true | 28.827366 | 9.72 | 8,660 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:N41D | null | null | null | 2.51 | 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|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","SAAFEC_S1262.csv"],"id":29374,"numValue":2.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29375,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20402,"numValue":8.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,363 | train | mutant | 3,714 | 302 | 4,165 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N88D | N88D | 1 | 1 | 0 | 0 | 88 | N | D | 8 | CONSERVATION | 1BNI | 159 | null | 88 | A | L | false | true | 28.827366 | 9.72 | 9,836 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:N41D | null | null | 6.2 | 2.62 | null | null | null | 3.2 | 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":33759,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33760,"numValue":2.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33761,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33762,"numValue":3.2,... | [{"id":20402,"numValue":8.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,364 | train | mutant | 7,113 | 302 | 7,766 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A90C|S127C | A90C|S127C | 2 | 2 | 0 | 0 | 90 | A | C | 4 | CONSERVATION | 1BNI | 159 | null | 90|127 | A | H|S | false | false | 51.163115 | 10.858 | 15,333 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:A43C 1BNI_A:S80C | null | null | 10 | -1.21 | null | null | null | 5.77 | 1.73 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 926 | ARTICLE | Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. | 1,993 | 10.1021/bi00067a022 | 8476861 | Biochemistry;32;4322-9 | 2 | Clarke J|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":"450 mM","type":"BUFFER... | [{"datasets":[],"id":56277,"numValue":10.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56278,"numValue":-1.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56279,"numValue":1.73,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56280,"numValue":5.77,"references":[]... | [{"id":20404,"numValue":4.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20441,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14365 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,365 | train | mutant | 7,113 | 302 | 7,766 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A90C|S127C | A90C|S127C | 2 | 2 | 0 | 0 | 90 | A | C | 4 | CONSERVATION | 1BNI | 159 | null | 90|127 | A | H|S | false | false | 51.163115 | 10.858 | 16,823 | ProTherm | 7.6 | Hydrogen exchange | GdnHCl | Imidazole | 50 mM | 37 | HCl | 27.5 mM | 1BNI_A:A43C 1BNI_A:S80C | null | null | null | -1.9 | null | null | null | null | 4.91 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 574 | ARTICLE | The kinetic pathway of folding of barnase. | 2,003 | 10.1016/j.jmb.2003.08.024 | 14516751 | J Mol Biol;333;169-86 | 4 | Fersht Alan R|Khan Faaizah|Chuang Jessica I|Gianni Stefano | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":37.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Hydrogen exchange","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Imidazole","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":61780,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61781,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":61782,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20404,"numValue":4.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20441,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14366 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,366 | train | mutant | 7,113 | 302 | 7,766 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A90C|S127C | A90C|S127C | 2 | 2 | 0 | 0 | 90 | A | C | 4 | CONSERVATION | 1BNI | 159 | null | 90|127 | A | H|S | false | false | 51.163115 | 10.858 | 16,824 | ProTherm | 7.9 | Hydrogen exchange | GdnHCl | Tris | 50 mM | 37 | HCl | 27.5 mM | 1BNI_A:A43C 1BNI_A:S80C | null | null | null | -1.8 | null | null | null | null | 4.91 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 574 | ARTICLE | The kinetic pathway of folding of barnase. | 2,003 | 10.1016/j.jmb.2003.08.024 | 14516751 | J Mol Biol;333;169-86 | 4 | Fersht Alan R|Khan Faaizah|Chuang Jessica I|Gianni Stefano | [{"numValue":7.9,"strValue":null,"type":"PH"},{"numValue":37.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Hydrogen exchange","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":61783,"numValue":-1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61784,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":61785,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20404,"numValue":4.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20441,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14367 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,367 | train | mutant | 7,113 | 302 | 7,766 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | A90C|S127C | A90C|S127C | 2 | 2 | 0 | 0 | 90 | A | C | 4 | CONSERVATION | 1BNI | 159 | null | 90|127 | A | H|S | false | false | 51.163115 | 10.858 | 16,927 | ProTherm | 7.5 | Hydrogen exchange | GdnHCl | Imidazole | 50 mM | 25 | HCl | 27.5 mM | 1BNI_A:A43C 1BNI_A:S80C | null | null | null | -1.9 | null | null | null | null | 4.91 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 574 | ARTICLE | The kinetic pathway of folding of barnase. | 2,003 | 10.1016/j.jmb.2003.08.024 | 14516751 | J Mol Biol;333;169-86 | 4 | Fersht Alan R|Khan Faaizah|Chuang Jessica I|Gianni Stefano | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Hydrogen exchange","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Imidazole","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","t... | [{"datasets":[],"id":62201,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":62202,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62203,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20404,"numValue":4.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20441,"numValue":7.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14368 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,368 | train | mutant | 4,293 | 302 | 4,801 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D91E | D91E | 1 | 1 | 0 | 0 | 91 | D | E | 3 | CONSERVATION | 1BNI | 159 | null | 91 | A | H | false | false | 114.581448 | 14.39375 | 9,969 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D44E | null | null | 8.5 | 0.32 | null | null | null | 4.6 | 1.84 | 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 | 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":34260,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34261,"numValue":0.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34262,"numValue":1.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":342... | [{"id":20405,"numValue":3.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14369 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,369 | train | mutant | 3,715 | 302 | 4,166 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V92T | V92T | 1 | 1 | 0 | 0 | 92 | V | T | 8 | CONSERVATION | 1BNI | 159 | null | 92 | A | H | false | false | 41.83123 | 8.412857 | 8,522 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:V45T | null | null | null | 2.32 | 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":28943,"numValue":2.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28944,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20406,"numValue":8.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14370 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,370 | train | mutant | 3,715 | 302 | 4,166 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V92T | V92T | 1 | 1 | 0 | 0 | 92 | V | T | 8 | CONSERVATION | 1BNI | 159 | null | 92 | A | H | false | false | 41.83123 | 8.412857 | 8,661 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:V45T | null | null | null | 2.44 | 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":29376,"numValue":2.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29377,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20406,"numValue":8.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14371 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,371 | train | mutant | 3,715 | 302 | 4,166 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V92T | V92T | 1 | 1 | 0 | 0 | 92 | V | T | 8 | CONSERVATION | 1BNI | 159 | null | 92 | A | H | false | false | 41.83123 | 8.412857 | 9,838 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:V45T | null | null | 6.6 | 2.22 | null | null | null | 3.3 | 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":33769,"numValue":6.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33770,"numValue":2.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33771,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33772,"numValue":3.3,"references":[],"s... | [{"id":20406,"numValue":8.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14372 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,372 | train | mutant | 3,716 | 302 | 4,167 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 8 | CONSERVATION | 1BNI | 159 | null | 92 | A | H | false | false | 41.83123 | 8.412857 | 8,523 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:V45A | null | null | null | 1.72 | 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":28945,"numValue":1.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28946,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20406,"numValue":8.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14373 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,373 | train | mutant | 3,716 | 302 | 4,167 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 8 | CONSERVATION | 1BNI | 159 | null | 92 | A | H | false | false | 41.83123 | 8.412857 | 8,662 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:V45A | null | null | null | 1.83 | 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":29378,"numValue":1.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29379,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20406,"numValue":8.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14374 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,374 | train | mutant | 3,716 | 302 | 4,167 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | V92A | V92A | 1 | 1 | 0 | 0 | 92 | V | A | 8 | CONSERVATION | 1BNI | 159 | null | 92 | A | H | false | false | 41.83123 | 8.412857 | 9,837 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:V45A | null | null | 7.65 | 1.17 | null | null | null | 3.6 | 2.08 | 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":33764,"numValue":7.65,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33765,"numValue":1.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33766,"numValue":2.08,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33767,"numValue":3.6,"references":[],"... | [{"id":20406,"numValue":8.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14375 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,375 | train | mutant | 274 | 302 | 306 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I98V | I98V | 1 | 1 | 0 | 0 | 98 | I | V | 9 | CONSERVATION | 1BNI | 159 | null | 98 | A | E | true | false | 0.502539 | 9.83875 | 488 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:I51V | 46.95 | -4.53 | null | null | 117.6 | null | 114.5 | 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":1961,"numValue":46.95,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1962,"numValue":-4.53,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1963,"numValue":117.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14376 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,376 | train | mutant | 274 | 302 | 306 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I98V | I98V | 1 | 1 | 0 | 0 | 98 | I | V | 9 | CONSERVATION | 1BNI | 159 | null | 98 | A | E | true | false | 0.502539 | 9.83875 | 8,524 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:I51V | null | null | null | 1.8 | 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":28947,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28948,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14377 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,377 | train | mutant | 274 | 302 | 306 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I98V | I98V | 1 | 1 | 0 | 0 | 98 | I | V | 9 | CONSERVATION | 1BNI | 159 | null | 98 | A | E | true | false | 0.502539 | 9.83875 | 8,663 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I51V | null | null | null | 1.85 | 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":29380,"numValue":1.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29381,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14378 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,378 | train | mutant | 274 | 302 | 306 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I98V | I98V | 1 | 1 | 0 | 0 | 98 | I | V | 9 | CONSERVATION | 1BNI | 159 | null | 98 | A | E | true | false | 0.502539 | 9.83875 | 8,771 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:I51V | null | null | 6.83 | 1.86 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.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":29635,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29636,"numValue":6.83,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29637,"numValue":1.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29638,"numVa... | [{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14379 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,379 | train | mutant | 274 | 302 | 306 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I98V | I98V | 1 | 1 | 0 | 0 | 98 | I | V | 9 | CONSERVATION | 1BNI | 159 | null | 98 | A | E | true | false | 0.502539 | 9.83875 | 9,839 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I51V | null | null | 7.69 | 1.13 | null | null | null | 3.6 | 2.11 | 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":33774,"numValue":7.69,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33775,"numValue":1.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33776,"numValue":2.11,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33777,"numValue":3.6,"references":[],"... | [{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14380 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,380 | train | mutant | 4,256 | 302 | 4,763 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I98A | I98A | 1 | 1 | 0 | 0 | 98 | I | A | 9 | CONSERVATION | 1BNI | 159 | null | 98 | A | E | true | false | 0.502539 | 9.83875 | 9,840 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I51A | null | null | 4.1 | 4.72 | null | null | null | 2.1 | 1.9 | 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|_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":33779,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":33780,"numValue":4.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33781,"numValue":1.9,"re... | [{"id":20412,"numValue":9.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14382 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,382 | train | mutant | 1,950 | 302 | 2,179 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G99A | G99A | 1 | 1 | 0 | 0 | 99 | G | A | 9 | CONSERVATION | 1BNI | 159 | null | 99 | A | E | true | false | 2.104778 | 10.515 | 7,316 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | 54.1 | 1BNI_A:G52A | null | null | null | 5.3 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":54.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25534,"numValue":5.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25535,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20413,"numValue":9.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14383 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,383 | train | mutant | 1,952 | 302 | 2,181 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G99V | G99V | 1 | 1 | 0 | 0 | 99 | G | V | 9 | CONSERVATION | 1BNI | 159 | null | 99 | A | E | true | false | 2.104778 | 10.515 | 3,766 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | null | 1BNI_A:G52V | 33 | -21.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","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:G52V","type":"_PDB_CHA... | [{"datasets":[],"id":13905,"numValue":33.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":13906,"numValue":-21.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":13907,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}... | [{"id":20413,"numValue":9.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14384 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,384 | train | mutant | 1,952 | 302 | 2,181 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G99V | G99V | 1 | 1 | 0 | 0 | 99 | G | V | 9 | CONSERVATION | 1BNI | 159 | null | 99 | A | E | true | false | 2.104778 | 10.515 | 7,318 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | 54.1 | 1BNI_A:G52V | null | null | null | 8.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":54.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25538,"numValue":8.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25539,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20413,"numValue":9.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14385 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,385 | train | mutant | 1,949 | 302 | 2,178 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G100A | G100A | 1 | 1 | 0 | 0 | 100 | G | A | 9 | CONSERVATION | 1BNI | 159 | null | 100 | A | E | true | false | 17.824802 | 12.2425 | 3,763 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | null | 1BNI_A:G53A | 45.5 | -8.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","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:G53A","type":"_PDB_CHA... | [{"datasets":[],"id":13896,"numValue":45.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":13897,"numValue":-8.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":13898,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20414,"numValue":9.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14386 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,386 | train | mutant | 1,949 | 302 | 2,178 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G100A | G100A | 1 | 1 | 0 | 0 | 100 | G | A | 9 | CONSERVATION | 1BNI | 159 | null | 100 | A | E | true | false | 17.824802 | 12.2425 | 7,315 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | 54.1 | 1BNI_A:G53A | null | null | null | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":54.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25532,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25533,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20414,"numValue":9.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14387 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,387 | train | mutant | 1,951 | 302 | 2,180 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G100V | G100V | 1 | 1 | 0 | 0 | 100 | G | V | 9 | CONSERVATION | 1BNI | 159 | null | 100 | A | E | true | false | 17.824802 | 12.2425 | 3,765 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | null | 1BNI_A:G53V | 34.5 | -19.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","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:G53V","type":"_PDB_CHA... | [{"datasets":[],"id":13902,"numValue":34.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":13903,"numValue":-19.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":13904,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}... | [{"id":20414,"numValue":9.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14388 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,388 | train | mutant | 1,951 | 302 | 2,180 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G100V | G100V | 1 | 1 | 0 | 0 | 100 | G | V | 9 | CONSERVATION | 1BNI | 159 | null | 100 | A | E | true | false | 17.824802 | 12.2425 | 7,317 | ProTherm | 6.3 | DSC | Thermal | MES | 50 mM | 54.1 | 1BNI_A:G53V | null | null | null | 7.8 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | 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 | 347 | ARTICLE | An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. | 1,999 | 10.1006/jmbi.1999.2569 | 10064710 | J Mol Biol;286;1471-85 | 3 | Fersht A R|Axe D D|Foster N W | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":54.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25536,"numValue":7.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25537,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20414,"numValue":9.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14389 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,389 | train | mutant | 280 | 302 | 312 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101N | D101N | 1 | 1 | 0 | 0 | 101 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 494 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:D54N | 44.57 | -7.06 | null | null | 116.6 | null | 113.3 | 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":1991,"numValue":44.57,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1992,"numValue":-7.06,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1993,"numValue":116.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14390 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,390 | train | mutant | 280 | 302 | 312 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101N | D101N | 1 | 1 | 0 | 0 | 101 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 495 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:D54N | 44.14 | -7.49 | null | null | 115 | null | 115.6 | 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":1996,"numValue":44.14,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1997,"numValue":-7.49,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1998,"numValue":115.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14392 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,392 | train | mutant | 280 | 302 | 312 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101N | D101N | 1 | 1 | 0 | 0 | 101 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 8,664 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D54N | null | null | null | 2.42 | 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":29382,"numValue":2.42,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29383,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14393 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,393 | train | mutant | 280 | 302 | 312 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101N | D101N | 1 | 1 | 0 | 0 | 101 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 8,777 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:D54N | null | null | 6.2 | 2.46 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.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":29659,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29660,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29661,"numValue":2.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29662,"numVal... | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14394 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,394 | train | mutant | 280 | 302 | 312 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101N | D101N | 1 | 1 | 0 | 0 | 101 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 8,778 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:D54N | null | null | 6 | 2.66 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.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":29663,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29664,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29665,"numValue":2.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29666,"numVal... | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14395 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,395 | train | mutant | 280 | 302 | 312 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101N | D101N | 1 | 1 | 0 | 0 | 101 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 9,842 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:D54N | null | null | 7.04 | 1.78 | null | null | null | 3.3 | 2.11 | 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":33789,"numValue":7.04,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33790,"numValue":1.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33791,"numValue":2.11,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33792,"numValue":3.3,"references":[],"... | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14396 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,396 | train | mutant | 280 | 302 | 312 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101N | D101N | 1 | 1 | 0 | 0 | 101 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 10,762 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:D54N | null | null | 8.16 | 2.67 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 706 | ARTICLE | Effect of active site residues in barnase on activity and stability. | 1,992 | 10.1016/0022-2836(92)90387-y | 1602471 | J Mol Biol;225;585-9 | 3 | Serrano L|Fersht A R|Meiering E 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":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":37016,"numValue":8.16,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37017,"numValue":2.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37018,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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