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:14397 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,397 | 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 | 10,767 | ProTherm | 4.4 | NMR | Urea | Sodium acetate | 30 mM | 25 | NaCl | 1 M | 1BNI_A:D54N | null | null | 5.48 | 2.65 | 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":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":37030,"numValue":5.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":37031,"numValue":2.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37032,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14398 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,398 | 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 | 10,771 | ProTherm | 8.9 | NMR | Urea | Tris | 30 mM | 25 | NaCl | 1 M | 1BNI_A:D54N | null | null | 5.73 | 2.32 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.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":37042,"numValue":5.73,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":37043,"numValue":2.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37044,"numValue":null,"references":[],"strValue"... | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14399 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,399 | 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 | 10,810 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 25 | 1BNI_A:D54N | null | null | 7.6 | 2.6 | 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|_PDB_CHAIN_MUTATION | 718 | ARTICLE | pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds. | 1,995 | 10.1021/bi00029a018 | 7626612 | Biochemistry;34;9424-33 | 3 | Oliveberg M|Fersht A R|Arcus V L | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":37204,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":37205,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37206,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14401 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,401 | train | mutant | 3,717 | 302 | 4,168 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101A | D101A | 1 | 1 | 0 | 0 | 101 | D | A | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 8,665 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:D54A | null | null | null | 3.1 | 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":29384,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29385,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14402 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,402 | train | mutant | 3,717 | 302 | 4,168 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101A | D101A | 1 | 1 | 0 | 0 | 101 | D | A | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 9,841 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:D54A | null | null | 5.96 | 2.86 | null | null | null | 3 | 1.95 | 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":33784,"numValue":5.96,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33785,"numValue":2.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33786,"numValue":1.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33787,"numValue":3.0,"references":[],"... | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14403 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,403 | train | mutant | 3,717 | 302 | 4,168 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D101A | D101A | 1 | 1 | 0 | 0 | 101 | D | A | 9 | CONSERVATION | 1BNI | 159 | null | 101 | A | E | false | false | 29.056408 | 15.15375 | 10,809 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 25 | 1BNI_A:D54A | null | null | 6.9 | 3.3 | 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|_PDB_CHAIN_MUTATION | 718 | ARTICLE | pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds. | 1,995 | 10.1021/bi00029a018 | 7626612 | Biochemistry;34;9424-33 | 3 | Oliveberg M|Fersht A R|Arcus V L | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":37201,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":37202,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37203,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20415,"numValue":9.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14405 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,405 | train | mutant | 848 | 302 | 954 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I102G | I102G | 1 | 1 | 0 | 0 | 102 | I | G | 4 | CONSERVATION | 1BNI | 159 | null | 102 | A | E | false | false | 95.025684 | 19.54125 | 9,133 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:I55G | null | null | 6.4 | 3.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31088,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31089,"numValue":3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31090,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20416,"numValue":4.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14406 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,406 | train | mutant | 3,698 | 302 | 4,149 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I102V | I102V | 1 | 1 | 0 | 0 | 102 | I | V | 4 | CONSERVATION | 1BNI | 159 | null | 102 | A | E | false | false | 95.025684 | 19.54125 | 8,504 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:I55V | null | null | null | 0.3 | 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|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":28907,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28908,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20416,"numValue":4.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14407 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,407 | train | mutant | 3,698 | 302 | 4,149 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I102V | I102V | 1 | 1 | 0 | 0 | 102 | I | V | 4 | CONSERVATION | 1BNI | 159 | null | 102 | A | E | false | false | 95.025684 | 19.54125 | 9,843 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I55V | null | null | 8.19 | 0.63 | null | null | null | 4.4 | 1.85 | 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":33794,"numValue":8.19,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33795,"numValue":0.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33796,"numValue":1.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33797,"numValue":4.4,"references":[],"... | [{"id":20416,"numValue":4.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14408 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,408 | train | mutant | 3,698 | 302 | 4,149 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I102V | I102V | 1 | 1 | 0 | 0 | 102 | I | V | 4 | CONSERVATION | 1BNI | 159 | null | 102 | A | E | false | false | 95.025684 | 19.54125 | 9,970 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:I55V | null | null | 8.5 | 0.32 | null | null | null | 4.4 | 1.93 | 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":34265,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34266,"numValue":0.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34267,"numValue":1.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":342... | [{"id":20416,"numValue":4.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14409 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,409 | train | mutant | 3,785 | 302 | 4,241 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I102T | I102T | 1 | 1 | 0 | 0 | 102 | I | T | 4 | CONSERVATION | 1BNI | 159 | null | 102 | A | E | false | false | 95.025684 | 19.54125 | 8,666 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I55T | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S983.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":["SAAFEC_S983.csv"],"id":29386,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29387,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20416,"numValue":4.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14410 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,410 | train | mutant | 3,785 | 302 | 4,241 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I102T | I102T | 1 | 1 | 0 | 0 | 102 | I | T | 4 | CONSERVATION | 1BNI | 159 | null | 102 | A | E | false | false | 95.025684 | 19.54125 | 9,845 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I55T | null | null | 7.58 | 1.24 | null | null | null | 4.1 | 1.84 | 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":33804,"numValue":7.58,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33805,"numValue":1.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33806,"numValue":1.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33807,"numValue":4.1,"references":[],"... | [{"id":20416,"numValue":4.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14411 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,411 | train | mutant | 3,786 | 302 | 4,242 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I102A | I102A | 1 | 1 | 0 | 0 | 102 | I | A | 4 | CONSERVATION | 1BNI | 159 | null | 102 | A | E | false | false | 95.025684 | 19.54125 | 8,667 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I55A | null | null | null | 1.28 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|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":["SAAFEC_S1262.csv"],"id":29388,"numValue":1.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29389,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20416,"numValue":4.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14413 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,413 | train | mutant | 4,576 | 302 | 5,096 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S104A | S104A | 1 | 1 | 0 | 0 | 104 | S | A | 4 | CONSERVATION | 1BNI | 159 | null | 104 | A | L | false | false | 84.247355 | 25.388333 | 10,759 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:S57A | null | null | 8.98 | -0.15 | 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":37007,"numValue":8.98,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":37008,"numValue":-0.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37009,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20418,"numValue":4.0,"position":104,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14414 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,414 | train | mutant | 3,653 | 302 | 4,099 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N105A | N105A | 1 | 1 | 0 | 0 | 105 | N | A | 9 | CONSERVATION | 1BNI | 159 | null | 105 | A | L | false | false | 24.987641 | 24.14375 | 8,398 | ProTherm | 6.8 | Hydrogen exchange | GdnHCl | Imidazole | 50 mM | 30 | HCl | 27.5 mM | 1BNI_A:N58A | null | null | null | 1.8 | null | null | null | null | 4.91 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | SAAFEC_S983.csv | 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":6.8,"strValue":null,"type":"PH"},{"numValue":30.0,"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":["SAAFEC_S983.csv"],"id":28548,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28549,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28550,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20419,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,415 | train | mutant | 3,653 | 302 | 4,099 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N105A | N105A | 1 | 1 | 0 | 0 | 105 | N | A | 9 | CONSERVATION | 1BNI | 159 | null | 105 | A | L | false | false | 24.987641 | 24.14375 | 8,494 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:N58A | null | null | null | 2.17 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["SAAFEC_S1262.csv"],"id":28887,"numValue":2.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28888,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20419,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14416 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,416 | train | mutant | 3,653 | 302 | 4,099 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N105A | N105A | 1 | 1 | 0 | 0 | 105 | N | A | 9 | CONSERVATION | 1BNI | 159 | null | 105 | A | L | false | false | 24.987641 | 24.14375 | 8,668 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:N58A | null | null | null | 2.17 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|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":["SAAFEC_S1262.csv"],"id":29390,"numValue":2.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29391,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20419,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14417 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,417 | train | mutant | 3,653 | 302 | 4,099 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N105A | N105A | 1 | 1 | 0 | 0 | 105 | N | A | 9 | CONSERVATION | 1BNI | 159 | null | 105 | A | L | false | false | 24.987641 | 24.14375 | 9,846 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:N58A | null | null | 6.82 | 2 | null | null | null | 3.4 | 1.97 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":33809,"numValue":6.82,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33810,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33811,"numValue":1.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33812,"numValue":3.4,... | [{"id":20419,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,418 | train | mutant | 4,257 | 302 | 4,764 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N105D | N105D | 1 | 1 | 0 | 0 | 105 | N | D | 9 | CONSERVATION | 1BNI | 159 | null | 105 | A | L | false | false | 24.987641 | 24.14375 | 9,847 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:N58D | null | null | 9.13 | -0.31 | null | null | null | 4.8 | 1.9 | 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 | 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":33814,"numValue":9.13,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":33815,"numValue":-0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33816,"numValue":1.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33... | [{"id":20419,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,419 | train | mutant | 4,257 | 302 | 4,764 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N105D | N105D | 1 | 1 | 0 | 0 | 105 | N | D | 9 | CONSERVATION | 1BNI | 159 | null | 105 | A | L | false | false | 24.987641 | 24.14375 | 10,758 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:N58D | null | null | 9.23 | -0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|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|_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":37004,"numValue":9.23,"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":37005,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37006... | [{"id":20419,"numValue":9.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14420 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,420 | train | mutant | 4,573 | 302 | 5,093 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R106A | R106A | 1 | 1 | 0 | 0 | 106 | R | A | 6 | CONSERVATION | 1BNI | 159 | null | 106 | A | T | false | false | 213.883717 | 40.311818 | 10,755 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:R59A | null | null | 9.47 | -0.64 | 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":36995,"numValue":9.47,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":36996,"numValue":-0.64,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36997,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20420,"numValue":6.0,"position":106,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,421 | train | mutant | 3,693 | 302 | 4,144 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K109R | K109R | 1 | 1 | 0 | 0 | 109 | K | R | 3 | CONSERVATION | 1BNI | 159 | null | 109 | A | L | false | false | 85.948159 | 23.05 | 8,495 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:K62R | null | null | null | 0.43 | 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 | 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"],"id":28889,"numValue":0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28890,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20423,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,422 | train | mutant | 3,693 | 302 | 4,144 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K109R | K109R | 1 | 1 | 0 | 0 | 109 | K | R | 3 | CONSERVATION | 1BNI | 159 | null | 109 | A | L | false | false | 85.948159 | 23.05 | 8,669 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:K62R | null | null | null | 0.43 | 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|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","potapov_with_uniprot_mapping.csv"],"id":29392,"numValue":0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29393,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20423,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14423 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,423 | train | mutant | 3,693 | 302 | 4,144 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K109R | K109R | 1 | 1 | 0 | 0 | 109 | K | R | 3 | CONSERVATION | 1BNI | 159 | null | 109 | A | L | false | false | 85.948159 | 23.05 | 9,848 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:K62R | null | null | 8.5 | 0.32 | null | null | null | 4.3 | 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":33819,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":33820,"numValue":0.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33821,"numValue":1.95,"r... | [{"id":20423,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14424 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,424 | train | mutant | 3,693 | 302 | 4,144 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K109R | K109R | 1 | 1 | 0 | 0 | 109 | K | R | 3 | CONSERVATION | 1BNI | 159 | null | 109 | A | L | false | false | 85.948159 | 23.05 | 9,971 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:K62R | null | null | 8.8 | 0.02 | null | null | null | 4.3 | 2.04 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":34270,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34271,"numValue":0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34272,"numValue":2.04,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34273,"numValue":4.3,"references":[],"s... | [{"id":20423,"numValue":3.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14425 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,425 | train | mutant | 4,294 | 302 | 4,802 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | G112S | G112S | 1 | 1 | 0 | 0 | 112 | G | S | 1 | CONSERVATION | 1BNI | 159 | null | 112 | A | L | false | false | 61.28151 | 25.035 | 9,972 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:G65S | null | null | 9.8 | -0.98 | null | null | null | 4.8 | 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|_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":34275,"numValue":9.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34276,"numValue":-0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34277,"numValue":2.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34278,"numValue":4.8... | [{"id":20426,"numValue":1.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,426 | train | mutant | 4,295 | 302 | 4,803 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K113A | K113A | 1 | 1 | 0 | 0 | 113 | K | A | 4 | CONSERVATION | 1BNI | 159 | null | 113 | A | L | false | false | 125.555629 | 29.584444 | 9,973 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:K66A | null | null | 9.8 | -0.98 | null | null | null | 4.7 | 2.09 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 662 | ARTICLE | Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. | 1,993 | 10.1006/jmbi.1993.1508 | 8377205 | J Mol Biol;233;305-12 | 3 | Serrano L|Fersht A R|Day A G | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":34280,"numValue":9.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34281,"numValue":-0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34282,"numValue":2.09,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34283,"numValue":4.7... | [{"id":20427,"numValue":4.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,427 | train | mutant | 279 | 302 | 311 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R116M | R116M | 1 | 1 | 0 | 0 | 116 | R | M | 8 | CONSERVATION | 1BNI | 159 | null | 116 | A | L | false | false | 40.744572 | 20.915455 | 493 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:R69M | 45.86 | -5.77 | null | null | 105.7 | null | 117.6 | 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":1986,"numValue":45.86,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1987,"numValue":-5.77,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1988,"numValue":105.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20430,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14428 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,428 | train | mutant | 279 | 302 | 311 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R116M | R116M | 1 | 1 | 0 | 0 | 116 | R | M | 8 | CONSERVATION | 1BNI | 159 | null | 116 | A | L | false | false | 40.744572 | 20.915455 | 8,776 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:R69M | null | null | 5.8 | 2.86 | 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":29655,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29656,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29657,"numValue":2.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29658,"numVal... | [{"id":20430,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,429 | train | mutant | 279 | 302 | 311 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R116M | R116M | 1 | 1 | 0 | 0 | 116 | R | M | 8 | CONSERVATION | 1BNI | 159 | null | 116 | A | L | false | false | 40.744572 | 20.915455 | 10,568 | ProTherm | 6.3 | Fluorescence | Urea | MES | 100 mM | 25 | 1BNI_A:R69M | null | null | null | 2.12 | null | null | null | 3.47 | 2.14 | null | null | null | null | null | null | null | yes | 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 | 694 | ARTICLE | Importance of two buried salt bridges in the stability and folding pathway of barnase. | 1,996 | 10.1021/bi952930e | 8639630 | Biochemistry;35;6786-94 | 3 | Vuilleumier S|Fersht A R|Tissot A C | [{"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":"100 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":36325,"numValue":2.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36326,"numValue":2.14,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36327,"numValue":3.47,"references":[],"strV... | [{"id":20430,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,430 | train | mutant | 4,472 | 302 | 4,992 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R116S | R116S | 1 | 1 | 0 | 0 | 116 | R | S | 8 | CONSERVATION | 1BNI | 159 | null | 116 | A | L | false | false | 40.744572 | 20.915455 | 10,565 | ProTherm | 6.3 | Fluorescence | Urea | MES | 100 mM | 25 | 1BNI_A:R69S | null | null | null | 2.72 | null | null | null | 3.16 | 1.86 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 694 | ARTICLE | Importance of two buried salt bridges in the stability and folding pathway of barnase. | 1,996 | 10.1021/bi952930e | 8639630 | Biochemistry;35;6786-94 | 3 | Vuilleumier S|Fersht A R|Tissot A C | [{"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":"100 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":36313,"numValue":2.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36314,"numValue":1.86,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36315,"n... | [{"id":20430,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,431 | train | mutant | 4,474 | 302 | 4,994 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R116K | R116K | 1 | 1 | 0 | 0 | 116 | R | K | 8 | CONSERVATION | 1BNI | 159 | null | 116 | A | L | false | false | 40.744572 | 20.915455 | 10,567 | ProTherm | 6.3 | CD | Urea | MES | 100 mM | 25 | 1BNI_A:R69K | null | null | null | 3.13 | null | null | null | 2.94 | 1.89 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 694 | ARTICLE | Importance of two buried salt bridges in the stability and folding pathway of barnase. | 1,996 | 10.1021/bi952930e | 8639630 | Biochemistry;35;6786-94 | 3 | Vuilleumier S|Fersht A R|Tissot A C | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":36321,"numValue":3.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36322,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36323,"n... | [{"id":20430,"numValue":8.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,433 | train | mutant | 849 | 302 | 955 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R119G | R119G | 1 | 1 | 0 | 0 | 119 | R | G | 4 | CONSERVATION | 1BNI | 159 | null | 119 | A | E | true | false | 89.620281 | 22.518182 | 1,476 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:R72G | 46.55 | -5.7 | null | null | null | null | 122.8 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:R72G","type":"_PDB_CHAI... | [{"datasets":[],"id":5409,"numValue":46.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5410,"numValue":-5.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5411,"numValue":122.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5412,"numValue":null,"references":[]... | [{"id":20433,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14434 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,434 | train | mutant | 849 | 302 | 955 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R119G | R119G | 1 | 1 | 0 | 0 | 119 | R | G | 4 | CONSERVATION | 1BNI | 159 | null | 119 | A | E | true | false | 89.620281 | 22.518182 | 9,134 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:R72G | null | null | 7 | 2.5 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31091,"numValue":7.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31092,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31093,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20433,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,435 | train | mutant | 850 | 302 | 956 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E120G | E120G | 1 | 1 | 0 | 0 | 120 | E | G | 9 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 120 | A | E | false | false | 13.103492 | 13.568889 | 1,477 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:E73G | 39.55 | -12.7 | null | null | null | null | 100.6 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:E73G","type":"_PDB_CHAI... | [{"datasets":[],"id":5413,"numValue":39.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5414,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5415,"numValue":100.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5416,"numValue":null,"references":[... | [{"id":100,"numValue":null,"position":120,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":20434,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,437 | train | mutant | 4,351 | 302 | 4,861 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E120F | E120F | 1 | 1 | 0 | 0 | 120 | E | F | 9 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 120 | A | E | false | false | 13.103492 | 13.568889 | 10,310 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:E73F | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 673 | ARTICLE | The role of Glu73 of barnase in catalysis and the binding of barstar. | 1,997 | 10.1006/jmbi.1997.1080 | 9231905 | J Mol Biol;270;111-22 | 3 | Schreiber G|Frisch C|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["SAAFEC_S1262.csv"],"id":35359,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35360,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":100,"numValue":null,"position":120,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":20434,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14438 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,438 | train | mutant | 4,352 | 302 | 4,862 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E120Q | E120Q | 1 | 1 | 0 | 0 | 120 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 120 | A | E | false | false | 13.103492 | 13.568889 | 10,311 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:E73Q | null | null | null | 2.7 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 673 | ARTICLE | The role of Glu73 of barnase in catalysis and the binding of barstar. | 1,997 | 10.1006/jmbi.1997.1080 | 9231905 | J Mol Biol;270;111-22 | 3 | Schreiber G|Frisch C|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["SAAFEC_S1262.csv"],"id":35361,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35362,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":100,"numValue":null,"position":120,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":20434,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,439 | train | mutant | 4,353 | 302 | 4,863 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E120W | E120W | 1 | 1 | 0 | 0 | 120 | E | W | 9 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 120 | A | E | false | false | 13.103492 | 13.568889 | 10,312 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:E73W | null | null | null | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 673 | ARTICLE | The role of Glu73 of barnase in catalysis and the binding of barstar. | 1,997 | 10.1006/jmbi.1997.1080 | 9231905 | J Mol Biol;270;111-22 | 3 | Schreiber G|Frisch C|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["SAAFEC_S1262.csv"],"id":35363,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35364,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":100,"numValue":null,"position":120,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":20434,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14440 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,440 | train | mutant | 4,577 | 302 | 5,097 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | E120A | E120A | 1 | 1 | 0 | 0 | 120 | E | A | 9 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 120 | A | E | false | false | 13.103492 | 13.568889 | 10,763 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:E73A | null | null | 6.53 | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | SAAFEC_S1262.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":37019,"numValue":6.53,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":37020,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37021,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":100,"numValue":null,"position":120,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":20434,"numValue":9.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14442 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,442 | train | mutant | 4,476 | 302 | 4,996 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D122N | D122N | 1 | 1 | 0 | 0 | 122 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 122 | A | E | true | false | 0.985203 | 7.975 | 10,571 | ProTherm | 6.3 | Fluorescence | Urea | MES | 100 mM | 25 | 1BNI_A:D75N | null | null | null | 4.8 | null | null | null | 2.08 | 1.69 | null | null | null | null | null | null | null | yes | 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 | 694 | ARTICLE | Importance of two buried salt bridges in the stability and folding pathway of barnase. | 1,996 | 10.1021/bi952930e | 8639630 | Biochemistry;35;6786-94 | 3 | Vuilleumier S|Fersht A R|Tissot A C | [{"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":"100 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":36337,"numValue":4.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36338,"numValue":1.69,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36339,"numValue":2.08,"references":[],"strVa... | [{"id":20436,"numValue":9.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14443 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,443 | train | mutant | 4,476 | 302 | 4,996 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D122N | D122N | 1 | 1 | 0 | 0 | 122 | D | N | 9 | CONSERVATION | 1BNI | 159 | null | 122 | A | E | true | false | 0.985203 | 7.975 | 10,812 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 25 | 1BNI_A:D75N | null | null | 5.2 | 5 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 718 | ARTICLE | pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds. | 1,995 | 10.1021/bi00029a018 | 7626612 | Biochemistry;34;9424-33 | 3 | Oliveberg M|Fersht A R|Arcus V L | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":[],"id":37210,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":37211,"numValue":5.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37212,"numValue":null,"references":[],"strValue":"Unknown","type":... | [{"id":20436,"numValue":9.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,445 | train | mutant | 3,718 | 302 | 4,169 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I123V | I123V | 1 | 1 | 0 | 0 | 123 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 123 | A | L | false | false | 0 | 7.0425 | 8,527 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:I76V | null | null | null | 0.82 | 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|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_S1262.csv","SAAFEC_S983.csv"],"id":28953,"numValue":0.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28954,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,446 | train | mutant | 3,718 | 302 | 4,169 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I123V | I123V | 1 | 1 | 0 | 0 | 123 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 123 | A | L | false | false | 0 | 7.0425 | 8,670 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I76V | null | null | null | 0.88 | 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":29394,"numValue":0.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29395,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,447 | train | mutant | 3,718 | 302 | 4,169 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I123V | I123V | 1 | 1 | 0 | 0 | 123 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 123 | A | L | false | false | 0 | 7.0425 | 9,849 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I76V | null | null | 7.84 | 0.98 | null | null | null | 4.1 | 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":33824,"numValue":7.84,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33825,"numValue":0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33826,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33827,"numValue":4.1... | [{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,448 | train | mutant | 3,787 | 302 | 4,243 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I123A | I123A | 1 | 1 | 0 | 0 | 123 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 123 | A | L | false | false | 0 | 7.0425 | 8,671 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I76A | null | null | null | 2.04 | 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":29396,"numValue":2.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29397,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14449 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,449 | train | mutant | 3,787 | 302 | 4,243 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I123A | I123A | 1 | 1 | 0 | 0 | 123 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 123 | A | L | false | false | 0 | 7.0425 | 8,672 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I76A | null | null | null | 1.16 | 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":29398,"numValue":1.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29399,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14450 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,450 | train | mutant | 3,787 | 302 | 4,243 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I123A | I123A | 1 | 1 | 0 | 0 | 123 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 123 | A | L | false | false | 0 | 7.0425 | 9,850 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I76A | null | null | 7.16 | 1.66 | null | null | null | 3.6 | 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|_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":33829,"numValue":7.16,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33830,"numValue":1.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33831,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33832,"numValue":3.6... | [{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14451 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,451 | train | mutant | 4,593 | 302 | 5,114 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I123T | I123T | 1 | 1 | 0 | 0 | 123 | I | T | 8 | CONSERVATION | 1BNI | 159 | null | 123 | A | L | false | false | 0 | 7.0425 | 10,792 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | NaCl | 0.15 M | 1BNI_A:I76T | null | null | 6.1 | 2.69 | null | null | null | 3.26 | 1.87 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 713 | ARTICLE | Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. | 1,993 | 10.1021/bi00212a026 | 8257694 | Biochemistry;32;13584-92 | 2 | Fersht A R|Sanz 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":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":37133,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":37134,"numValue":2.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37135,"numValue":1.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":37136,"numValue":3.26... | [{"id":20437,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14452 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,452 | train | mutant | 3,719 | 302 | 4,170 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N124A | N124A | 1 | 1 | 0 | 0 | 124 | N | A | 8 | CONSERVATION | 1BNI | 159 | null | 124 | A | S | false | false | 72.690603 | 13.16125 | 8,528 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:N77A | null | null | null | 1.66 | 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":28955,"numValue":1.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28956,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20438,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,453 | train | mutant | 3,719 | 302 | 4,170 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N124A | N124A | 1 | 1 | 0 | 0 | 124 | N | A | 8 | CONSERVATION | 1BNI | 159 | null | 124 | A | S | false | false | 72.690603 | 13.16125 | 8,673 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:N77A | null | null | null | 1.88 | 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":29400,"numValue":1.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29401,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20438,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14454 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,454 | train | mutant | 3,719 | 302 | 4,170 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N124A | N124A | 1 | 1 | 0 | 0 | 124 | N | A | 8 | CONSERVATION | 1BNI | 159 | null | 124 | A | S | false | false | 72.690603 | 13.16125 | 9,851 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:N77A | null | null | 7.37 | 1.45 | null | null | null | 3.7 | 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 | 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":33834,"numValue":7.37,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33835,"numValue":1.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33836,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33837,"numValue":3.7,... | [{"id":20438,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,455 | train | mutant | 3,720 | 302 | 4,171 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y125F | Y125F | 1 | 1 | 0 | 0 | 125 | Y | F | 8 | CONSERVATION | 1BNI | 159 | null | 125 | A | L | true | true | 9.962651 | 8.695 | 8,529 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:Y78F | null | null | null | 1.35 | 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":28957,"numValue":1.35,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28958,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20439,"numValue":8.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14456 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,456 | train | mutant | 3,720 | 302 | 4,171 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y125F | Y125F | 1 | 1 | 0 | 0 | 125 | Y | F | 8 | CONSERVATION | 1BNI | 159 | null | 125 | A | L | true | true | 9.962651 | 8.695 | 9,683 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Y78F | null | null | null | 1.5 | 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 | 651 | ARTICLE | Mapping the transition state and pathway of protein folding by protein engineering. | 1,989 | 10.1038/340122a0 | 2739734 | Nature;340;122-6 | 4 | Matouschek A|Serrano L|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":33252,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33253,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20439,"numValue":8.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,457 | train | mutant | 3,720 | 302 | 4,171 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y125F | Y125F | 1 | 1 | 0 | 0 | 125 | Y | F | 8 | CONSERVATION | 1BNI | 159 | null | 125 | A | L | true | true | 9.962651 | 8.695 | 9,852 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:Y78F | null | null | 7.68 | 1.14 | null | null | null | 3.8 | 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 | 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":33839,"numValue":7.68,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33840,"numValue":1.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33841,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33842,"numValue":3.8,... | [{"id":20439,"numValue":8.0,"position":125,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,458 | train | mutant | 4,296 | 302 | 4,804 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T126V | T126V | 1 | 1 | 0 | 0 | 126 | T | V | 1 | CONSERVATION | 1BNI | 159 | null | 126 | A | L | false | false | 108.960571 | 13.298571 | 9,974 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:T79V | null | null | 9 | -0.18 | null | null | null | 4.7 | 1.91 | 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":34285,"numValue":9.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34286,"numValue":-0.18,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34287,"numValue":1.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34... | [{"id":20440,"numValue":1.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,459 | train | mutant | 278 | 302 | 310 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R130Q | R130Q | 1 | 1 | 0 | 0 | 130 | R | Q | 9 | CONSERVATION | 1BNI | 159 | null | 130 | A | L | true | true | 70.621543 | 11.100909 | 492 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:R83Q | 48.34 | -3.29 | null | null | 116.6 | null | 122.5 | 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":1981,"numValue":48.34,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1982,"numValue":-3.29,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1983,"numValue":116.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20444,"numValue":9.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,460 | train | mutant | 278 | 302 | 310 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R130Q | R130Q | 1 | 1 | 0 | 0 | 130 | R | Q | 9 | CONSERVATION | 1BNI | 159 | null | 130 | A | L | true | true | 70.621543 | 11.100909 | 8,775 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:R83Q | null | null | 7.08 | 1.58 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":29651,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29652,"numValue":7.08,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":29653,"numValue":1.58,"references":[],"strValue":null,"type":"DDG"},... | [{"id":20444,"numValue":9.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14461 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,461 | train | mutant | 278 | 302 | 310 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R130Q | R130Q | 1 | 1 | 0 | 0 | 130 | R | Q | 9 | CONSERVATION | 1BNI | 159 | null | 130 | A | L | true | true | 70.621543 | 11.100909 | 10,570 | ProTherm | 6.3 | Fluorescence | Urea | MES | 100 mM | 25 | 1BNI_A:R83Q | null | null | null | 2.05 | null | null | null | 3.51 | 2.28 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 694 | ARTICLE | Importance of two buried salt bridges in the stability and folding pathway of barnase. | 1,996 | 10.1021/bi952930e | 8639630 | Biochemistry;35;6786-94 | 3 | Vuilleumier S|Fersht A R|Tissot A C | [{"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":"100 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":36333,"numValue":2.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36334,"numValue":2.28,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36335,"numValue":3.51,"references":[],"strValue":null,"type":"CM"},{"datase... | [{"id":20444,"numValue":9.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14462 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,462 | train | mutant | 4,475 | 302 | 4,995 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R130K | R130K | 1 | 1 | 0 | 0 | 130 | R | K | 9 | CONSERVATION | 1BNI | 159 | null | 130 | A | L | true | true | 70.621543 | 11.100909 | 10,569 | ProTherm | 6.3 | Fluorescence | Urea | MES | 100 mM | 25 | 1BNI_A:R83K | null | null | null | 4.13 | null | null | null | 2.43 | 1.68 | null | null | null | null | null | null | null | yes | DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 694 | ARTICLE | Importance of two buried salt bridges in the stability and folding pathway of barnase. | 1,996 | 10.1021/bi952930e | 8639630 | Biochemistry;35;6786-94 | 3 | Vuilleumier S|Fersht A R|Tissot A C | [{"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":"100 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":36329,"numValue":4.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36330,"numValue":1.68,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36331,"n... | [{"id":20444,"numValue":9.0,"position":130,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14463 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,463 | train | mutant | 3,721 | 302 | 4,172 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N131A | N131A | 1 | 1 | 0 | 0 | 131 | N | A | 6 | CONSERVATION | 1BNI | 159 | null | 131 | A | L | false | false | 47.157727 | 10.68375 | 8,530 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:N84A | null | null | null | 2.02 | 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":28959,"numValue":2.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28960,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20445,"numValue":6.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14464 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,464 | train | mutant | 3,721 | 302 | 4,172 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N131A | N131A | 1 | 1 | 0 | 0 | 131 | N | A | 6 | CONSERVATION | 1BNI | 159 | null | 131 | A | L | false | false | 47.157727 | 10.68375 | 8,674 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:N84A | null | null | null | 2.24 | 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":29402,"numValue":2.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29403,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20445,"numValue":6.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14465 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,465 | train | mutant | 3,721 | 302 | 4,172 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | N131A | N131A | 1 | 1 | 0 | 0 | 131 | N | A | 6 | CONSERVATION | 1BNI | 159 | null | 131 | A | L | false | false | 47.157727 | 10.68375 | 9,853 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:N84A | null | null | 7.23 | 1.59 | null | null | null | 3.5 | 2.04 | 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":33844,"numValue":7.23,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33845,"numValue":1.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33846,"numValue":2.04,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33847,"numValue":3.5,... | [{"id":20445,"numValue":6.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14466 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,466 | train | mutant | 4,297 | 302 | 4,805 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S132A | S132A | 1 | 1 | 0 | 0 | 132 | S | A | 5 | CONSERVATION | 1BNI | 159 | null | 132 | A | S | false | false | 28.450905 | 15.03 | 9,975 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:S85A | null | null | 9.1 | -0.28 | null | null | null | 4.51 | 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 | 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":34290,"numValue":9.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34291,"numValue":-0.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34292,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34... | [{"id":20446,"numValue":5.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14467 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,467 | train | mutant | 6,894 | 302 | 7,536 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S132C|H149C | S132C|H149C | 2 | 2 | 0 | 0 | 132 | S | C | 5 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 132|149 | A | S | false | false | 69.92607 | 25.389 | 14,730 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 20 mM | null | 1BNI_A:S85C 1BNI_A:H102C | 47.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 911 | ARTICLE | The A-state of barnase. | 1,994 | 10.1021/bi00203a015 | 7727370 | Biochemistry;33;11189-99 | 3 | Johnson C M|Fersht A R|Sanz J M | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:S85C 1BNI_A:H1... | [{"datasets":[],"id":54474,"numValue":47.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54475,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":101,"numValue":null,"position":149,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":20446,"numValue":5.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20463,"numValue":9.0,"position":149,"positionArray":null,"p... | |||||||||||||
fireprotdb:14468 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,468 | train | mutant | 6,894 | 302 | 7,536 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S132C|H149C | S132C|H149C | 2 | 2 | 0 | 0 | 132 | S | C | 5 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 132|149 | A | S | false | false | 69.92607 | 25.389 | 15,334 | ProTherm | 6.3 | Fluorescence | GdnHCl | MES | 450 mM | 25 | 1BNI_A:S85C 1BNI_A:H102C | null | null | 12.9 | -4.1 | null | null | null | 3 | 4.3 | 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":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFF... | [{"datasets":[],"id":56282,"numValue":12.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56283,"numValue":-4.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56284,"numValue":4.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56285,"numValue":3.0,"references":[],"s... | [{"id":101,"numValue":null,"position":149,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":20446,"numValue":5.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20463,"numValue":9.0,"position":149,"positionArray":null,"p... | |||||||||||||
fireprotdb:14469 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,469 | train | mutant | 6,894 | 302 | 7,536 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S132C|H149C | S132C|H149C | 2 | 2 | 0 | 0 | 132 | S | C | 5 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 132|149 | A | S | false | false | 69.92607 | 25.389 | 16,825 | ProTherm | 7.6 | Hydrogen exchange | GdnHCl | Imidazole | 50 mM | 37 | HCl | 27.5 mM | 1BNI_A:S85C 1BNI_A:H102C | null | null | null | -4.6 | 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":61786,"numValue":-4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61787,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":61788,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":101,"numValue":null,"position":149,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":20446,"numValue":5.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20463,"numValue":9.0,"position":149,"positionArray":null,"p... | |||||||||||
fireprotdb:14470 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,470 | train | mutant | 6,894 | 302 | 7,536 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S132C|H149C | S132C|H149C | 2 | 2 | 0 | 0 | 132 | S | C | 5 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 132|149 | A | S | false | false | 69.92607 | 25.389 | 16,826 | ProTherm | 7.9 | Hydrogen exchange | GdnHCl | Tris | 50 mM | 37 | HCl | 27.5 mM | 1BNI_A:S85C 1BNI_A:H102C | null | null | null | -4.5 | 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":61789,"numValue":-4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61790,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":61791,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":101,"numValue":null,"position":149,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":20446,"numValue":5.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20463,"numValue":9.0,"position":149,"positionArray":null,"p... | |||||||||||
fireprotdb:14471 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,471 | train | mutant | 6,894 | 302 | 7,536 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S132C|H149C | S132C|H149C | 2 | 2 | 0 | 0 | 132 | S | C | 5 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 132|149 | A | S | false | false | 69.92607 | 25.389 | 16,928 | ProTherm | 7.5 | Hydrogen exchange | GdnHCl | Imidazole | 50 mM | 25 | HCl | 27.5 mM | 1BNI_A:S85C 1BNI_A:H102C | null | null | null | -4.3 | 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":62204,"numValue":-4.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":62205,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62206,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":101,"numValue":null,"position":149,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":20446,"numValue":5.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20463,"numValue":9.0,"position":149,"positionArray":null,"p... | |||||||||||
fireprotdb:14472 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,472 | train | mutant | 272 | 302 | 304 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135V | I135V | 1 | 1 | 0 | 0 | 135 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 485 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:I88V | 48.11 | -3.37 | null | null | 119.2 | null | 124.8 | 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":1946,"numValue":48.11,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1947,"numValue":-3.37,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1948,"numValue":119.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14473 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,473 | train | mutant | 272 | 302 | 304 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135V | I135V | 1 | 1 | 0 | 0 | 135 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 1,089 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | null | 1BNI_A:I88V | 51 | -2.9 | null | null | null | null | 117 | null | null | null | null | null | null | null | null | null | yes (>85%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:I88V","type":... | [{"datasets":[],"id":4070,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4071,"numValue":-2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4072,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14475 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,475 | train | mutant | 272 | 302 | 304 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135V | I135V | 1 | 1 | 0 | 0 | 135 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 8,496 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:I88V | 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|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","SAAFEC_S983.csv"],"id":28891,"numValue":1.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28892,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14476 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,476 | train | mutant | 272 | 302 | 304 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135V | I135V | 1 | 1 | 0 | 0 | 135 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 8,768 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:I88V | null | null | 7.22 | 1.47 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|SAAFEC_S1262.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":29623,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29624,"numValue":7.22,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","SAAFEC_S1262.csv"],"id":29625,"numValue":1.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14477 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,477 | train | mutant | 272 | 302 | 304 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135V | I135V | 1 | 1 | 0 | 0 | 135 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 8,906 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:I88V | null | null | 7.95 | 1.47 | null | null | null | 3.87 | 2.06 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":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":30193,"numValue":7.95,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","SAAFEC_S1262.csv"],"id":30194,"numValue":1.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30195,"numValue":2.06,"references":[],"strValue":null,"type":"M"},{"datasets":[]... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,479 | train | mutant | 272 | 302 | 304 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135V | I135V | 1 | 1 | 0 | 0 | 135 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 9,854 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I88V | null | null | 7.18 | 1.64 | null | null | null | 3.8 | 1.85 | 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":33849,"numValue":7.18,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33850,"numValue":1.64,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33851,"numValue":1.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33852,"numValue":3.8,"references":[],"... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14480 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,480 | train | mutant | 663 | 302 | 718 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135A | I135A | 1 | 1 | 0 | 0 | 135 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 1,091 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | null | 1BNI_A:I88A | 42.7 | -11.2 | null | null | null | null | 106 | null | null | null | null | null | null | null | null | null | yes (>85%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:I88A","type":... | [{"datasets":[],"id":4078,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4079,"numValue":-11.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4080,"numValue":106.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14481 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,481 | train | mutant | 663 | 302 | 718 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135A | I135A | 1 | 1 | 0 | 0 | 135 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 7,782 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 48 | 1BNI_A:I88A | null | null | null | 3.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes (>85%) | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":48.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":26689,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26690,"numValue":null,"references":[],"strValue":"yes (>85%)","type":"REVERSIBILITY"}] | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,482 | train | mutant | 663 | 302 | 718 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135A | I135A | 1 | 1 | 0 | 0 | 135 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 8,675 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I88A | null | null | null | 2.76 | 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":29404,"numValue":2.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29405,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14483 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,483 | train | mutant | 663 | 302 | 718 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135A | I135A | 1 | 1 | 0 | 0 | 135 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 8,908 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:I88A | null | null | 5.34 | 4.08 | null | null | null | 2.47 | 2.16 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":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":30203,"numValue":5.34,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":30204,"numValue":4.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30205,"numValue":2.16,"references":[],"strValue":null,"type":"M"},{"datase... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,484 | train | mutant | 663 | 302 | 718 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135A | I135A | 1 | 1 | 0 | 0 | 135 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 9,686 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:I88A | null | null | null | 4.46 | 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":33258,"numValue":4.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33259,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,485 | train | mutant | 663 | 302 | 718 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135A | I135A | 1 | 1 | 0 | 0 | 135 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 9,855 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I88A | null | null | 4.8 | 4.02 | null | null | null | 2.4 | 1.94 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33854,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv"],"id":33855,"numValue":4.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33856,"numValue":1.94,"references":[],"strValue":null,"type":"M"},{"dataset... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14486 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,486 | train | mutant | 851 | 302 | 957 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135G | I135G | 1 | 1 | 0 | 0 | 135 | I | G | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 1,478 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:I88G | 31.45 | -20.8 | null | null | null | null | 100.4 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:I88G","type":"_PDB_CHAI... | [{"datasets":[],"id":5417,"numValue":31.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5418,"numValue":-20.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5419,"numValue":100.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5420,"numValue":null,"references":[... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14487 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,487 | train | mutant | 851 | 302 | 957 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135G | I135G | 1 | 1 | 0 | 0 | 135 | I | G | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 9,136 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:I88G | null | null | 2.1 | 7.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31097,"numValue":2.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31098,"numValue":7.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31099,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14488 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,488 | train | mutant | 4,298 | 302 | 4,806 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I135L | I135L | 1 | 1 | 0 | 0 | 135 | I | L | 7 | CONSERVATION | 1BNI | 159 | null | 135 | A | E | false | false | 0 | 8.99375 | 9,976 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:I88L | null | null | 8.8 | 0.02 | null | null | null | 4.4 | 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 | 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":34295,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34296,"numValue":0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34297,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":342... | [{"id":20449,"numValue":7.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,489 | train | mutant | 852 | 302 | 958 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136G | L136G | 1 | 1 | 0 | 0 | 136 | L | G | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 1,479 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:L89G | 43.55 | -8.7 | null | null | null | null | 58.5 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1BNI_A:L89G","type":"_PDB_CHAI... | [{"datasets":[],"id":5421,"numValue":43.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5422,"numValue":-8.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5423,"numValue":58.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5424,"numValue":null,"references":[],... | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,490 | train | mutant | 852 | 302 | 958 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136G | L136G | 1 | 1 | 0 | 0 | 136 | L | G | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 9,137 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:L89G | null | null | 2.5 | 7 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31100,"numValue":2.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31101,"numValue":7.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31102,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,491 | train | mutant | 3,788 | 302 | 4,244 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136V | L136V | 1 | 1 | 0 | 0 | 136 | L | V | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 8,676 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:L89V | null | null | null | 0.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | EXP_TEMPERATURE|PH|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":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":6.3,"strValue":null,"type":"PH"},{"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":29406,"numValue":0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29407,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14492 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,492 | train | mutant | 3,788 | 302 | 4,244 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136V | L136V | 1 | 1 | 0 | 0 | 136 | L | V | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 9,856 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:L89V | null | null | 8.35 | 0.47 | null | null | null | 4.4 | 1.89 | 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":33859,"numValue":8.35,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33860,"numValue":0.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33861,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33862,"numValue":4.4,"references":[],"... | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14493 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,493 | train | mutant | 3,788 | 302 | 4,244 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136V | L136V | 1 | 1 | 0 | 0 | 136 | L | V | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 9,977 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:L89V | null | null | 8.5 | 0.32 | null | null | null | 4.4 | 1.92 | 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":34300,"numValue":8.5,"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":34301,"numValue":0.32,"references":[],"strValue":null,"type... | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,494 | train | mutant | 3,789 | 302 | 4,245 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136T | L136T | 1 | 1 | 0 | 0 | 136 | L | T | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 8,677 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:L89T | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|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":["SAAFEC_S1262.csv"],"id":29408,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29409,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,495 | train | mutant | 3,789 | 302 | 4,245 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136T | L136T | 1 | 1 | 0 | 0 | 136 | L | T | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 8,678 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:L89T | null | null | null | 2.55 | 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_S983.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","potapov_with_uniprot_mapping.csv","SAAFEC_S983.csv"],"id":29410,"numValue":2.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29411,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY... | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14496 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,496 | train | mutant | 3,789 | 302 | 4,245 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L136T | L136T | 1 | 1 | 0 | 0 | 136 | L | T | 7 | CONSERVATION | 1BNI | 159 | null | 136 | A | E | false | false | 0 | 11.6175 | 9,857 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:L89T | null | null | 5.54 | 3.28 | null | null | null | 3.1 | 1.78 | 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":33864,"numValue":5.54,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33865,"numValue":3.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33866,"numValue":1.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33867,"numValue":3.1,"references":[],"... | [{"id":20450,"numValue":7.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14497 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,497 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 483 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:S91A | 46.67 | -4.81 | null | null | 125.6 | null | 116 | 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":1936,"numValue":46.67,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1937,"numValue":-4.81,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1938,"numValue":125.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,498 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 484 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:S91A | 46.68 | -4.8 | null | null | 128.7 | null | 115.1 | 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":1941,"numValue":46.68,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1942,"numValue":-4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1943,"numValue":128.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14499 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,499 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 8,397 | ProTherm | 6.8 | Hydrogen exchange | GdnHCl | Imidazole | 50 mM | 30 | HCl | 27.5 mM | 1BNI_A:S91A | null | null | null | 1.8 | null | null | null | null | 4.91 | null | null | null | null | null | null | null | yes | DDG|M|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|SAAFEC_S983.csv | 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":6.8,"strValue":null,"type":"PH"},{"numValue":30.0,"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":["capriotti_S1615_map.csv","capriotti_S388_map.csv","SAAFEC_S983.csv"],"id":28545,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28546,"numValue":4.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":28547,"numValue":null,"references":[],"strValue":"yes","ty... | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,500 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 8,497 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:S91A | null | null | null | 1.94 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.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","SAAFEC_S1262.csv"],"id":28893,"numValue":1.94,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28894,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14501 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,501 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 8,679 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:S91A | 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|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","SAAFEC_S1262.csv"],"id":29412,"numValue":1.93,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29413,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,502 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 8,766 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:S91A | null | null | 7.31 | 1.38 | 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":29615,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29616,"numValue":7.31,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29617,"numValue":1.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29618,"numVa... | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14503 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,503 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 8,767 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:S91A | null | null | 7.53 | 1.16 | null | 1.6 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | DCP|DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08... | [{"datasets":[],"id":29619,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29620,"numValue":7.53,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":29621,"numValue":1.16,"references":[],"strValue":null,"type":"DDG"},... | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,504 | train | mutant | 271 | 302 | 303 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S138A | S138A | 1 | 1 | 0 | 0 | 138 | S | A | 9 | CONSERVATION | 1BNI | 159 | null | 138 | A | E | false | false | 2.222398 | 12.778333 | 9,858 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:S91A | null | null | 6.41 | 2.41 | null | null | null | 3.5 | 1.79 | 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":33869,"numValue":6.41,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33870,"numValue":2.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33871,"numValue":1.79,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33872,"numValue":3.5,"references":[],"... | [{"id":20452,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,505 | train | mutant | 277 | 302 | 309 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | S139A | S139A | 1 | 1 | 0 | 0 | 139 | S | A | 5 | CONSERVATION | 1BNI | 159 | null | 139 | A | T | false | false | 53.388633 | 20.12 | 491 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:S92A | 44.5 | -7.13 | null | null | 110.9 | null | 110.3 | 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":1976,"numValue":44.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1977,"numValue":-7.13,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1978,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":20453,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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