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:14506 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,506 | 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 | 8,498 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:S92A | null | null | null | 2.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 587 | ARTICLE | The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. | 1,992 | 10.1016/0022-2836(92)90563-y | 1569558 | J Mol Biol;224;805-18 | 3 | Matouschek A|Serrano L|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 micro M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":28895,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28896,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20453,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14507 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,507 | 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 | 8,680 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:S92A | null | null | null | 2.74 | 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":29414,"numValue":2.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29415,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20453,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,508 | 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 | 8,774 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:S92A | null | null | 5.83 | 2.83 | 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":29647,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29648,"numValue":5.83,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","SAAFEC_S1262.csv"],"id":29649,"numValue":2.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[... | [{"id":20453,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,509 | 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 | 9,859 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:S92A | null | null | 5.6 | 3.22 | 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":33874,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33875,"numValue":3.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33876,"numValue":1.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33877,"numValue":3.1,"references":[],"s... | [{"id":20453,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,510 | train | mutant | 4,473 | 302 | 4,993 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | D140N | D140N | 1 | 1 | 0 | 0 | 140 | D | N | 8 | CONSERVATION | 1BNI | 159 | null | 140 | A | T | false | false | 68.981752 | 22.5375 | 10,566 | ProTherm | 6.3 | Fluorescence | Urea | MES | 100 mM | 25 | 1BNI_A:D93N | null | null | null | 4.11 | null | null | null | 2.44 | 1.99 | 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":36317,"numValue":4.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36318,"numValue":1.99,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36319,"n... | [{"id":20454,"numValue":8.0,"position":140,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14511 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,511 | train | mutant | 4,338 | 302 | 4,847 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141Y | W141Y | 1 | 1 | 0 | 0 | 141 | W | Y | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,030 | ProTherm | 5.8 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:W94Y | null | null | 9.73 | 1.27 | null | null | null | 4.96 | 1.98 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34457,"numValue":9.73,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":34458,"numValue":1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34459,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34460,"numVal... | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14512 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,512 | train | mutant | 4,338 | 302 | 4,847 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141Y | W141Y | 1 | 1 | 0 | 0 | 141 | W | Y | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,034 | ProTherm | 9 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:W94Y | null | null | 8.42 | 0.99 | null | null | null | 4.29 | 2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34477,"numValue":8.42,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S983.csv"],"id":34478,"numValue":0.99,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34479,"numValue":2.0,"references":[],"strValue":n... | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14513 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,513 | train | mutant | 4,339 | 302 | 4,848 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141F | W141F | 1 | 1 | 0 | 0 | 141 | W | F | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,031 | ProTherm | 5.8 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:W94F | null | null | 9.94 | 1.06 | null | null | null | 5.07 | 1.89 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv | EXP_TEMPERATURE|PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34462,"numValue":9.94,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":34463,"numValue":1.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34464,"numValue":1.89,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34465,"numVal... | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,514 | train | mutant | 4,339 | 302 | 4,848 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141F | W141F | 1 | 1 | 0 | 0 | 141 | W | F | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,035 | ProTherm | 9 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:W94F | null | null | 8.81 | 0.6 | null | null | null | 4.5 | 2.01 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34482,"numValue":8.81,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":34483,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34484,"numValue":2.01,"references":[],"strValue":null,"type":"M"},{"... | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14515 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,515 | train | mutant | 4,340 | 302 | 4,849 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141L | W141L | 1 | 1 | 0 | 0 | 141 | W | L | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,032 | ProTherm | 5.8 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:W94L | null | null | 9.41 | 1.59 | null | null | null | 4.8 | 2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":5.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34467,"numValue":9.41,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":34468,"numValue":1.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34469,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34470,"numValu... | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,516 | train | mutant | 4,340 | 302 | 4,849 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141L | W141L | 1 | 1 | 0 | 0 | 141 | W | L | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,036 | ProTherm | 9 | Fluorescence | Urea | MES,Tris, | 150 mM,150 mM, | 25 | NaCl | 1 M | 1BNI_A:W94L | null | null | 8.75 | 0.66 | null | null | null | 4.47 | 1.98 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 665 | ARTICLE | Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. | 1,992 | 10.1016/0022-2836(92)90560-7 | 1569555 | J Mol Biol;224;759-70 | 3 | Sancho J|Loewenthal R|Fersht A R | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES,Tris,","type":"BUFFER"},{"numValue":null,"strValue":"150 mM,150 mM,",... | [{"datasets":[],"id":34487,"numValue":8.75,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":34488,"numValue":0.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34489,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34490,"numVal... | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,517 | train | mutant | 4,340 | 302 | 4,849 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141L | W141L | 1 | 1 | 0 | 0 | 141 | W | L | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,764 | ProTherm | 5.9 | NMR | Urea | MES | 30 mM | 25 | NaCl | 1 M | 1BNI_A:W94L | null | null | 7.67 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":5.9,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"... | [{"datasets":[],"id":37022,"numValue":7.67,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37023,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14518 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,518 | train | mutant | 4,340 | 302 | 4,849 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | W141L | W141L | 1 | 1 | 0 | 0 | 141 | W | L | 7 | CONSERVATION | 1BNI | 159 | null | 141 | A | L | true | false | 62.672451 | 23.581429 | 10,768 | ProTherm | 8.9 | NMR | Urea | Tris | 30 mM | 25 | NaCl | 1 M | 1BNI_A:W94L | null | null | 7.41 | 0.64 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 707 | ARTICLE | Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. | 1,992 | 10.1021/bi00123a006 | 1540580 | Biochemistry;31;2253-8 | 3 | Serrano L|Sancho J|Fersht A R | [{"numValue":8.9,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":37033,"numValue":7.41,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":37034,"numValue":0.64,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37035,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20455,"numValue":7.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,519 | train | mutant | 853 | 302 | 959 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L142G | L142G | 1 | 1 | 0 | 0 | 142 | L | G | 7 | CONSERVATION | 1BNI | 159 | null | 142 | A | L | false | false | 47.836056 | 15.86625 | 1,480 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:L95G | 43.15 | -9.1 | null | null | null | null | 98.5 | 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:L95G","type":"_PDB_CHAI... | [{"datasets":[],"id":5425,"numValue":43.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5426,"numValue":-9.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5427,"numValue":98.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5428,"numValue":null,"references":[],... | [{"id":20456,"numValue":7.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,520 | train | mutant | 853 | 302 | 959 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | L142G | L142G | 1 | 1 | 0 | 0 | 142 | L | G | 7 | CONSERVATION | 1BNI | 159 | null | 142 | A | L | false | false | 47.836056 | 15.86625 | 9,138 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:L95G | null | null | 4.8 | 4.7 | 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":31103,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31104,"numValue":4.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31105,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20456,"numValue":7.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14521 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,521 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 486 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:I96V | 49.19 | -2.29 | null | null | 119.9 | null | 125.1 | 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":1951,"numValue":49.19,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1952,"numValue":-2.29,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1953,"numValue":119.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,522 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 487 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | null | 1BNI_A:I96V | 49.18 | -2.3 | null | null | 112 | null | 123.4 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 52 | ARTICLE | Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. | 1,994 | 10.1093/protein/7.9.1089 | 7831279 | Protein Eng;7;1089-95 | 4 | Matouschek A|Johnson C M|Fersht A R|Matthews J M | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate,Acetic acid,","type":"BUFFER"},{"numValue":null,"strValue":"6.08 mM,13.92 mM,","type":"BUFFER_CONC"},{"numValue":null,"strV... | [{"datasets":[],"id":1956,"numValue":49.18,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1957,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1958,"numValue":112.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,523 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 1,088 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | null | 1BNI_A:I96V | 51.5 | -2.4 | null | null | null | null | 121 | 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:I96V","type":... | [{"datasets":[],"id":4066,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4067,"numValue":-2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4068,"numValue":121.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14525 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,525 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 8,769 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:I96V | null | null | 7.51 | 1.18 | 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":29627,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29628,"numValue":7.51,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29629,"numValue":1.18,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29630,"numVa... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14526 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,526 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 8,770 | ProTherm | 4.4 | DSC | Thermal | Sodium acetate,Acetic acid, | 6.08 mM,13.92 mM, | 25 | 1BNI_A:I96V | null | null | 7.52 | 1.17 | 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":29631,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29632,"numValue":7.52,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":29633,"numValue":1.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29634,"numVa... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,527 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 8,905 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:I96V | null | null | 8.68 | 0.74 | null | null | null | 4.11 | 2.11 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.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":30188,"numValue":8.68,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":30189,"numValue":0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30190,"numValue":2.11,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30191,"numValue":4.11... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,528 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 8,910 | ProTherm | 6.3 | Fluorescence | GdnHCl | MES | 450 mM | 25 | 1BNI_A:I96V | null | null | 8.19 | 0.69 | null | null | null | 1.76 | 4.64 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.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":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFF... | [{"datasets":[],"id":30213,"numValue":8.19,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":30214,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30215,"numValue":4.64,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30216,"numValue":1.76... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,530 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 9,687 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:I96V | null | null | null | 0.98 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|SAAFEC_S1262.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","SAAFEC_S1262.csv"],"id":33260,"numValue":0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33261,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,531 | train | mutant | 273 | 302 | 305 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143V | I143V | 1 | 1 | 0 | 0 | 143 | I | V | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 9,860 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I96V | null | null | 7.8 | 1.02 | null | null | null | 4.1 | 1.9 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_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":33879,"numValue":7.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":33880,"numValue":1.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33881,"numValue":1.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33882,"numValue... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,532 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 1,090 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | null | 1BNI_A:I96A | 44.9 | -9.6 | null | null | null | null | 112 | 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:I96A","type":... | [{"datasets":[],"id":4074,"numValue":44.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4075,"numValue":-9.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4076,"numValue":112.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,533 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 7,781 | ProTherm | 6.3 | Fluorescence | Thermal | MES | 50 mM | 48 | 1BNI_A:I96A | null | null | null | 3.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes (>85%) | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":48.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFF... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":26687,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26688,"numValue":null,"references":[],"strValue":"yes (>85%)","type":"REVERSIBILITY"}] | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14534 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,534 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 8,681 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I96A | null | null | null | 2.37 | 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":29416,"numValue":2.37,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29417,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,535 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 8,907 | ProTherm | 6.3 | Fluorescence | Urea | MES | 450 mM | 25 | 1BNI_A:I96A | null | null | 6.29 | 3.13 | null | null | null | 2.89 | 2.18 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | 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":30198,"numValue":6.29,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30199,"numValue":3.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30200,"numValue":2.18,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30201,"numValue":2.8... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,536 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 8,911 | ProTherm | 6.3 | Fluorescence | GdnHCl | MES | 450 mM | 25 | 1BNI_A:I96A | null | null | 6.16 | 2.72 | null | null | null | 1.26 | 4.87 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 113 | ARTICLE | Energetics of complementary side-chain packing in a protein hydrophobic core. | 1,989 | 10.1021/bi00437a058 | 2669964 | Biochemistry;28;4914-22 | 3 | Nyberg K|Fersht A R|Kellis J T | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"BUFF... | [{"datasets":[],"id":30218,"numValue":6.16,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30219,"numValue":2.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30220,"numValue":4.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":30221,"numValue":1.26,"references":[],... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,537 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 9,569 | ProTherm | 6.3 | Fluorescence | Urea | MES | 19.3 mM | 25 | 1BNI_A:I96A | null | null | 6.5 | 4 | null | null | null | 2.24 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 645 | ARTICLE | Contribution of hydrophobic interactions to protein stability. | 1,988 | 10.1038/333784a0 | 3386721 | Nature;333;784-6 | 4 | Nyberg K|Fersht A R|Kellis J T|Sali D | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"19.3 mM","type":"BUFFE... | [{"datasets":[],"id":32764,"numValue":6.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv"],"id":32765,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":32766,"numValue":2.24,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":32767,"numValu... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,538 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 9,688 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:I96A | null | null | null | 3.52 | 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":33262,"numValue":3.52,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33263,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14539 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,539 | train | mutant | 662 | 302 | 717 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143A | I143A | 1 | 1 | 0 | 0 | 143 | I | A | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 9,861 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I96A | null | null | 5.67 | 3.15 | null | null | null | 2.8 | 1.96 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":33884,"numValue":5.67,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33885,"numValue":3.15,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33886,"numValue":1.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33887,"numValue":2.8... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,540 | train | mutant | 854 | 302 | 960 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I143G | I143G | 1 | 1 | 0 | 0 | 143 | I | G | 8 | CONSERVATION | 1BNI | 159 | null | 143 | A | E | false | false | 0 | 11.37375 | 1,481 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:I96G | 36.55 | -15.7 | null | null | null | null | 110.3 | 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:I96G","type":"_PDB_CHAI... | [{"datasets":[],"id":5429,"numValue":36.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5430,"numValue":-15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5431,"numValue":110.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5432,"numValue":null,"references":[... | [{"id":20457,"numValue":8.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,542 | train | mutant | 855 | 302 | 961 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y144G | Y144G | 1 | 1 | 0 | 0 | 144 | Y | G | 6 | CONSERVATION | 1BNI | 159 | null | 144 | A | E | false | false | 32.683743 | 9.946667 | 1,482 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | null | 1BNI_A:Y97G | 34.35 | -17.9 | null | null | null | null | 102.6 | 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:Y97G","type":"_PDB_CHAI... | [{"datasets":[],"id":5433,"numValue":34.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5434,"numValue":-17.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5435,"numValue":102.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5436,"numValue":null,"references":[... | [{"id":20458,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,543 | train | mutant | 855 | 302 | 961 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y144G | Y144G | 1 | 1 | 0 | 0 | 144 | Y | G | 6 | CONSERVATION | 1BNI | 159 | null | 144 | A | E | false | false | 32.683743 | 9.946667 | 9,140 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:Y97G | null | null | 2.9 | 6.6 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 157 | ARTICLE | The folding pathway of barnase: the rate-limiting transition state and a hidden intermediate under native conditions. | 2,004 | 10.1021/bi0362267 | 15035606 | Biochemistry;43;3346-56 | 3 | Vu Ngoc-Diep|Feng Hanqiao|Bai Yawen | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Mes","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":31109,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31110,"numValue":6.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31111,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20458,"numValue":6.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,544 | train | mutant | 3,699 | 302 | 4,150 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T146V | T146V | 1 | 1 | 0 | 0 | 146 | T | V | 9 | CONSERVATION | 1BNI | 159 | null | 146 | A | E | false | false | 1.074968 | 16.221429 | 8,505 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T99V | null | null | null | 2.99 | 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":28909,"numValue":2.99,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28910,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20460,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14545 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,545 | train | mutant | 3,699 | 302 | 4,150 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T146V | T146V | 1 | 1 | 0 | 0 | 146 | T | V | 9 | CONSERVATION | 1BNI | 159 | null | 146 | A | E | false | false | 1.074968 | 16.221429 | 9,862 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T99V | null | null | 5.9 | 2.92 | null | null | null | 3.2 | 1.84 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33889,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33890,"numValue":2.92,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33891,"numValue":1.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33892,"numValue":3.2,... | [{"id":20460,"numValue":9.0,"position":146,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,547 | train | mutant | 856 | 302 | 962 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T147G | T147G | 1 | 1 | 0 | 0 | 147 | T | G | 3 | CONSERVATION | 1BNI | 159 | null | 147 | A | S | false | false | 69.709787 | 20.022857 | 9,141 | ProTherm | 6.3 | CD | Thermal | Mes | 50 mM | 25 | 1BNI_A:T100G | null | null | 6.7 | 2.8 | 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":31112,"numValue":6.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":31113,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31114,"numValue":null,"references":[],"strValue":"Unknown","... | [{"id":20461,"numValue":3.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14548 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,548 | train | mutant | 4,575 | 302 | 5,095 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | H149A | H149A | 1 | 1 | 0 | 0 | 149 | H | A | 9 | ACTIVE_SITE|CONSERVATION | 1BNI | 159 | null | 149 | A | S | false | false | 111.401235 | 35.748 | 10,757 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:H102A | null | null | 8.59 | 0.24 | 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":37001,"numValue":8.59,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":37002,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":37003,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":101,"numValue":null,"position":149,"positionArray":null,"positionRange":null,"strValue":"Proton donor","type":"ACTIVE_SITE"},{"id":20463,"numValue":9.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,549 | train | mutant | 4,258 | 302 | 4,765 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y150F | Y150F | 1 | 1 | 0 | 0 | 150 | Y | F | 9 | CONSERVATION | 1BNI | 159 | null | 150 | A | S | false | false | 61.631659 | 27.746667 | 9,863 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:Y103F | null | null | 8.64 | 0.18 | null | null | null | 4.5 | 1.89 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":33894,"numValue":8.64,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":33895,"numValue":0.18,"references":[],"strValue":null,"type":"DDG"},{"datasets"... | [{"id":20464,"numValue":9.0,"position":150,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,550 | train | mutant | 4,258 | 302 | 4,765 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Y150F | Y150F | 1 | 1 | 0 | 0 | 150 | Y | F | 9 | CONSERVATION | 1BNI | 159 | null | 150 | A | S | false | false | 61.631659 | 27.746667 | 10,760 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Y103F | null | null | 8.83 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":37010,"numValue":8.83,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":37011,"numValue":0.0,"references":[],"strValue":null,"type":"... | [{"id":20464,"numValue":9.0,"position":150,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,551 | train | mutant | 4,299 | 302 | 4,807 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q151A | Q151A | 1 | 1 | 0 | 0 | 151 | Q | A | 4 | CONSERVATION | 1BNI | 159 | null | 151 | A | S | false | false | 89.675635 | 24.658333 | 9,978 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Q104A | 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":34305,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":34306,"numValue":0.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34307,"numValue":1.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":343... | [{"id":20465,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14552 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,552 | train | mutant | 4,299 | 302 | 4,807 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | Q151A | Q151A | 1 | 1 | 0 | 0 | 151 | Q | A | 4 | CONSERVATION | 1BNI | 159 | null | 151 | A | S | false | false | 89.675635 | 24.658333 | 10,761 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:Q104A | null | null | 8.67 | 0.16 | 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|potapov_with_uniprot_mapping.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":37013,"numValue":8.67,"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":37014,"numValue":0.16,"references":[],"strValue":null,"typ... | [{"id":20465,"numValue":4.0,"position":151,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,553 | train | mutant | 3,700 | 302 | 4,151 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T152V | T152V | 1 | 1 | 0 | 0 | 152 | T | V | 7 | CONSERVATION | 1BNI | 159 | null | 152 | A | L | false | false | 82.338871 | 21.698571 | 8,506 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:T105V | null | null | null | 2.25 | 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":28911,"numValue":2.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28912,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20466,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,554 | train | mutant | 3,700 | 302 | 4,151 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T152V | T152V | 1 | 1 | 0 | 0 | 152 | T | V | 7 | CONSERVATION | 1BNI | 159 | null | 152 | A | L | false | false | 82.338871 | 21.698571 | 8,682 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:T105V | null | null | null | 2.25 | 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":29418,"numValue":2.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29419,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20466,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,555 | train | mutant | 3,700 | 302 | 4,151 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | T152V | T152V | 1 | 1 | 0 | 0 | 152 | T | V | 7 | CONSERVATION | 1BNI | 159 | null | 152 | A | L | false | false | 82.338871 | 21.698571 | 9,864 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:T105V | null | null | 6.68 | 2.14 | null | null | null | 3.4 | 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":33899,"numValue":6.68,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":33900,"numValue":2.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33901,"numValue":1.95,"... | [{"id":20466,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,556 | train | mutant | 4,300 | 302 | 4,808 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | K155R | K155R | 1 | 1 | 0 | 0 | 155 | K | R | 5 | CONSERVATION | 1BNI | 159 | null | 155 | A | E | false | false | 110.390463 | 6.593333 | 9,979 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:K108R | null | null | 9.6 | -0.78 | null | null | null | 5 | 1.91 | 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":34310,"numValue":9.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34311,"numValue":-0.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34312,"numValue":1.91,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34313,"numValue":5.0... | [{"id":20469,"numValue":5.0,"position":155,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,557 | train | mutant | 3,701 | 302 | 4,152 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I156V | I156V | 1 | 1 | 0 | 0 | 156 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 156 | A | L | false | false | 44.77139 | 8.5025 | 8,507 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 micro M | 25 | 1BNI_A:I109V | null | null | null | 0.76 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv|SAAFEC_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":28913,"numValue":0.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28914,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20470,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,558 | train | mutant | 3,701 | 302 | 4,152 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I156V | I156V | 1 | 1 | 0 | 0 | 156 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 156 | A | L | false | false | 44.77139 | 8.5025 | 8,683 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I109V | 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 | 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":29420,"numValue":0.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29421,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20470,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,559 | train | mutant | 3,701 | 302 | 4,152 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I156V | I156V | 1 | 1 | 0 | 0 | 156 | I | V | 7 | CONSERVATION | 1BNI | 159 | null | 156 | A | L | false | false | 44.77139 | 8.5025 | 9,865 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I109V | null | null | 8.01 | 0.81 | null | null | null | 4.1 | 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|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":33904,"numValue":8.01,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":33905,"numValue":0.81,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33906,"numValue":1.92,"... | [{"id":20470,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,560 | train | mutant | 3,790 | 302 | 4,246 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I156A | I156A | 1 | 1 | 0 | 0 | 156 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 156 | A | L | false | false | 44.77139 | 8.5025 | 8,684 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I109A | null | null | null | 2.22 | 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":29422,"numValue":2.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29423,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20470,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:14561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,561 | train | mutant | 3,790 | 302 | 4,246 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I156A | I156A | 1 | 1 | 0 | 0 | 156 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 156 | A | L | false | false | 44.77139 | 8.5025 | 8,685 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:I109A | null | null | null | 1.4 | 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":29424,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29425,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":20470,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,562 | train | mutant | 3,790 | 302 | 4,246 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | I156A | I156A | 1 | 1 | 0 | 0 | 156 | I | A | 7 | CONSERVATION | 1BNI | 159 | null | 156 | A | L | false | false | 44.77139 | 8.5025 | 9,866 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:I109A | null | null | 7.55 | 1.27 | null | null | null | 3.5 | 2.15 | 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":33909,"numValue":7.55,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33910,"numValue":1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33911,"numValue":2.15,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33912,"numValue":3.5,"references":[],"... | [{"id":20470,"numValue":7.0,"position":156,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:14563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,563 | train | mutant | 4,259 | 302 | 4,766 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R157A | R157A | 1 | 1 | 0 | 0 | 157 | R | A | 6 | CONSERVATION | 1BNI | 159 | null | 157 | A | L | false | false | 73.658971 | 6.535455 | 9,867 | ProTherm | 6.3 | Fluorescence | Urea | MES-NaOH | 450 mM | 25 | 1BNI_A:R110A | null | null | 8.89 | -0.07 | null | null | null | 4.3 | 2.03 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 656 | ARTICLE | The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. | 1,992 | 10.1016/0022-2836(92)90562-x | 1569557 | J Mol Biol;224;783-804 | 5 | Matouschek A|Serrano L|Fersht A R|Kellis J T|Cann P | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"450 mM","type":"B... | [{"datasets":[],"id":33914,"numValue":8.89,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S983.csv"],"id":33915,"numValue":-0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33916,"numValue":2.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33917,"numValue":4.3... | [{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,564 | train | mutant | 4,259 | 302 | 4,766 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R157A | R157A | 1 | 1 | 0 | 0 | 157 | R | A | 6 | CONSERVATION | 1BNI | 159 | null | 157 | A | L | false | false | 73.658971 | 6.535455 | 11,105 | ProTherm | 6.3 | Fluorescence | Urea | MES | 1.00 M | 25 | NaCl | 613 mM | 1BNI_A:R110A | null | null | null | 0.46 | null | null | null | 4.37 | null | null | null | null | null | null | null | null | yes | DDG|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 745 | ARTICLE | Co-operative interactions during protein folding. | 1,992 | 10.1016/0022-2836(92)90557-z | 1569552 | J Mol Biol;224;733-40 | 2 | Horovitz A|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"1.00 M","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":38234,"numValue":0.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38235,"numValue":4.37,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38236,"numValue":null,"references":[],"str... | [{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:14565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,565 | train | mutant | 4,259 | 302 | 4,766 | 157 | 157 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | 32 | Ribonuclease | Bacillus amyloliquefaciens | 1 | P00648 | IPR001887|IPR000026|IPR016191|IPR053753 | 3.1.27.- | R157A | R157A | 1 | 1 | 0 | 0 | 157 | R | A | 6 | CONSERVATION | 1BNI | 159 | null | 157 | A | L | false | false | 73.658971 | 6.535455 | 11,338 | ProTherm | 6.3 | Fluorescence | Urea | MES | 50 mM | 25 | 1BNI_A:R110A | null | null | 9.47 | 0.46 | null | null | null | 4.37 | 2.26 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | capriotti_S1615_map.csv|capriotti_S388_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 757 | ARTICLE | Strength and co-operativity of contributions of surface salt bridges to protein stability. | 1,990 | 10.1016/S0022-2836(99)80018-7 | 2266554 | J Mol Biol;216;1031-44 | 5 | Serrano L|Bycroft M|Horovitz A|Avron B|Fersht A R | [{"numValue":6.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"MES","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_... | [{"datasets":[],"id":39036,"numValue":9.47,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","capriotti_S388_map.csv","khan_protherm_data_mapped.csv"],"id":39037,"numValue":0.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39038,"numValue":2.26,"references":[],"str... | [{"id":20471,"numValue":6.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:14566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,566 | train | sequence | 329 | 329 | -1 | 201 | -1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,975 | ProTherm | 7.4 | DSC | Thermal | Potassium phosphate | 20 mM | null | NaCl | 150 mM | 78 | null | null | null | 200 | 2.57 | 125 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1203 | ARTICLE | Analysis of the two-state behavior of the thermal unfolding serum retinol binding protein containing a single retinol ligand. | 1,992 | 10.1021/bi00139a019 | 1610801 | Biochemistry;31;5560-7 | 4 | Fish F|Brouillette C G|Muccio D D|Waterhous D V | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":70000,"numValue":78.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70001,"numValue":200.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":70002,"numValue":2.57,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":70003,"numValue":125.0,"references":... | ||||||||||||||||||||||||
fireprotdb:14567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,567 | train | sequence | 329 | 329 | -1 | 201 | -1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,976 | ProTherm | 7.4 | CD | Thermal | Potassium phosphate | 20 mM | null | NaCl | 150 mM | 78 | null | null | null | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1203 | ARTICLE | Analysis of the two-state behavior of the thermal unfolding serum retinol binding protein containing a single retinol ligand. | 1,992 | 10.1021/bi00139a019 | 1610801 | Biochemistry;31;5560-7 | 4 | Fish F|Brouillette C G|Muccio D D|Waterhous D V | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"... | [{"datasets":[],"id":70005,"numValue":78.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":70006,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":70007,"numValue":null,"references":[],"strValue":"yes (>95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,568 | train | sequence | 329 | 329 | -1 | 201 | -1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,334 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 68.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":80648,"numValue":68.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80649,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:14569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,569 | train | mutant | 7,307 | 329 | 7,977 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | G40A|W42F | G40A|W42F | 2 | 2 | 0 | 0 | 40 | G | A | 9 | CONSERVATION | 1RBP | 330 | null | 40|42 | A | E | true | false | 9.572578 | 14.36 | 15,667 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:G22A 1RBP_A:W24F | 52.2 | -16.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:G22A 1RBP_A... | [{"datasets":[],"id":57501,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57502,"numValue":-16.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57503,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20511,"numValue":9.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20513,"numValue":9.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,571 | train | mutant | 298 | 329 | 331 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | W42F | W42F | 1 | 1 | 0 | 0 | 42 | W | F | 9 | CONSERVATION | 1RBP | 330 | null | 42 | A | E | true | false | 0 | 12.485 | 540 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:W24F | 56.9 | -12 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:W24F","type... | [{"datasets":[],"id":2156,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2157,"numValue":-12.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2158,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20513,"numValue":9.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,573 | train | mutant | 7,310 | 329 | 7,980 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | W42Y|W85L|W123F | W42Y|W85L|W123F | 3 | 3 | 0 | 0 | 42 | W | Y | 9 | CONSERVATION | 1RBP | 330 | null | 42|85|123 | A | E | true | false | 53.58067 | 30.58619 | 15,670 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:W24Y 1RBP_A:W67L 1RBP_A:W105F | 55 | -13.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:W24Y 1RBP_A... | [{"datasets":[],"id":57510,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57511,"numValue":-13.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57512,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20513,"numValue":9.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20556,"numValue":7.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20594,"numValue":9.0,"position":123,"positionArray":null,"positionRan... | ||||||||||||||
fireprotdb:14574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,574 | train | mutant | 7,308 | 329 | 7,978 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | W85L|W109H | W85L|W109H | 2 | 2 | 0 | 0 | 85 | W | L | 7 | CONSERVATION | 1RBP | 330 | null | 85|109 | A | E | true | true | 109.351435 | 43.631072 | 15,668 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:W67L 1RBP_A:W91H | 66.2 | -2.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:W67L 1RBP_A... | [{"datasets":[],"id":57504,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57505,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57506,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20556,"numValue":7.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20580,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,575 | train | mutant | 7,309 | 329 | 7,979 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | W85L|W109L|W123F | W85L|W109L|W123F | 3 | 3 | 0 | 0 | 85 | W | L | 7 | CONSERVATION | 1RBP | 330 | null | 85|109|123 | A | E | true | true | 80.391631 | 33.062143 | 15,669 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:W67L 1RBP_A:W91L 1RBP_A:W105F | 66.7 | -2.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:W67L 1RBP_A... | [{"datasets":[],"id":57507,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57508,"numValue":-2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57509,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20556,"numValue":7.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20580,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":20594,"numValue":9.0,"position":123,"positionArray":null,"positionRa... | ||||||||||||||
fireprotdb:14576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,576 | train | mutant | 300 | 329 | 333 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | W109H | W109H | 1 | 1 | 0 | 0 | 109 | W | H | 7 | CONSERVATION | 1RBP | 330 | null | 109 | A | E | true | true | 80.432882 | 19.912857 | 542 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:W91H | 68.4 | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:W91H","type... | [{"datasets":[],"id":2162,"numValue":68.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2163,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2164,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20580,"numValue":7.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,577 | train | mutant | 301 | 329 | 334 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | W123F | W123F | 1 | 1 | 0 | 0 | 123 | W | F | 9 | CONSERVATION | 1RBP | 330 | null | 123 | A | E | true | false | 22.472023 | 11.924286 | 543 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:W105F | 66.7 | -2.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:W105F","typ... | [{"datasets":[],"id":2165,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2166,"numValue":-2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2167,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20594,"numValue":9.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,578 | train | mutant | 302 | 329 | 335 | 201 | 201 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | 33 | Retinol-binding protein 4 | Homo sapiens | 1 | P02753 | IPR012674|IPR022271|IPR022272|IPR000566|IPR002449 | R157Q | R157Q | 1 | 1 | 0 | 0 | 157 | R | Q | 9 | CONSERVATION | 1RBP | 330 | null | 157 | A | S | false | false | 62.985927 | 14.71 | 544 | ProTherm | 7.4 | CD | Thermal | sodium phosphate | 5 mM | null | 1RBP_A:R139Q | 56.5 | -12.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 55 | ARTICLE | Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily. | 2,001 | 10.1110/ps.22901 | 11604536 | Protein Sci;10;2301-16 | 6 | Brew K|Greene L H|Chrysina E D|Irons L I|Papageorgiou A C|Acharya K R | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1RBP_A:R139Q","typ... | [{"datasets":[],"id":2168,"numValue":56.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2169,"numValue":-12.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2170,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":20628,"numValue":9.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:14579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,579 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,964 | ProTherm | 4 | DSC | Thermal | Sodium acetate | 10 mM | null | NaCl | 100 mM | 33.2 | null | null | null | 22.71 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":73287,"numValue":33.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73288,"numValue":22.71,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73289,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,580 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,965 | ProTherm | 4.5 | DSC | Thermal | Sodium acetate | 10 mM | null | NaCl | 100 mM | 42.1 | null | null | null | 28.92 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":73290,"numValue":42.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73291,"numValue":28.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73292,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,581 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,966 | ProTherm | 5 | DSC | Thermal | Sodium acetate | 10 mM | null | NaCl | 100 mM | 47.7 | null | null | null | 32.98 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":5.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":73293,"numValue":47.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73294,"numValue":32.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73295,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,583 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,968 | ProTherm | 5.5 | DSC | Thermal | Sodium cacodylate | 10 mM | null | NaCl | 100 mM | 54.4 | null | null | null | 39.91 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":[],"id":73299,"numValue":54.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73300,"numValue":39.91,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73301,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,584 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,969 | ProTherm | 6 | DSC | Thermal | Sodium cacodylate | 10 mM | null | NaCl | 100 mM | 56.5 | null | null | null | 44.93 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":[],"id":73302,"numValue":56.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73303,"numValue":44.93,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73304,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,586 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,971 | ProTherm | 7 | DSC | Thermal | Sodium cacodylate | 10 mM | null | NaCl | 100 mM | 57 | null | null | null | 47.32 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":[],"id":73308,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73309,"numValue":47.32,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73310,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,587 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,972 | ProTherm | 6 | DSC | Thermal | Sodium phosphate | 10 mM | null | NaCl | 100 mM | 55.9 | null | null | null | 39.44 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":73311,"numValue":55.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73312,"numValue":39.44,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73313,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,588 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,973 | ProTherm | 6.5 | DSC | Thermal | Sodium phosphate | 10 mM | null | NaCl | 100 mM | 56.1 | null | null | null | 43.26 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":73314,"numValue":56.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73315,"numValue":43.26,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73316,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,589 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,974 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 10 mM | null | NaCl | 100 mM | 57 | null | null | null | 43.26 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":73317,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73318,"numValue":43.26,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73319,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,590 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,975 | ProTherm | 7.5 | DSC | Thermal | Sodium phosphate | 10 mM | null | NaCl | 100 mM | 57.1 | null | null | null | 46.85 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"IO... | [{"datasets":[],"id":73320,"numValue":57.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73321,"numValue":46.85,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73322,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,591 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,976 | ProTherm | 6.5 | DSC | Thermal | HEPES | 10 mM | null | NaCl | 100 mM | 56.5 | null | null | null | 43.5 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73323,"numValue":56.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73324,"numValue":43.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73325,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,592 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,977 | ProTherm | 7 | DSC | Thermal | HEPES | 10 mM | null | NaCl | 100 mM | 57.6 | null | null | null | 47.56 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73326,"numValue":57.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73327,"numValue":47.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73328,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,593 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,978 | ProTherm | 7.5 | DSC | Thermal | HEPES | 10 mM | null | NaCl | 100 mM | 57.8 | null | null | null | 49 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73329,"numValue":57.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73330,"numValue":49.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73331,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,595 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,980 | ProTherm | 8.5 | DSC | Thermal | HEPES | 10 mM | null | NaCl | 100 mM | 56.5 | null | null | null | 42.07 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":8.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73335,"numValue":56.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73336,"numValue":42.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73337,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,597 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,982 | ProTherm | 6.5 | DSC | Thermal | Sodium citrate | 10 mM | null | NaCl | 100 mM | 56.8 | null | null | null | 45.17 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium citrate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":73341,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73342,"numValue":45.17,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73343,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,598 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,983 | ProTherm | 7 | DSC | Thermal | Sodium citrate | 10 mM | null | NaCl | 100 mM | 57 | null | null | null | 46.37 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium citrate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":73344,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73345,"numValue":46.37,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73346,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,599 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,984 | ProTherm | 7.5 | DSC | Thermal | Sodium citrate | 10 mM | null | NaCl | 100 mM | 57.3 | null | null | null | 48.28 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium citrate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":73347,"numValue":57.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73348,"numValue":48.28,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73349,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,600 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,985 | ProTherm | 8.5 | DSC | Thermal | Sodium borate | 10 mM | null | NaCl | 100 mM | 57.7 | null | null | null | 44.46 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":8.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium borate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":73350,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73351,"numValue":44.46,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73352,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,601 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,986 | ProTherm | 8.7 | DSC | Thermal | Sodium borate | 10 mM | null | NaCl | 100 mM | 57.6 | null | null | null | 43.74 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":8.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium borate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":73353,"numValue":57.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73354,"numValue":43.74,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73355,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,602 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,987 | ProTherm | 6 | DSC | Thermal | PIPES | 10 mM | null | NaCl | 100 mM | 53.1 | null | null | null | 36.09 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73356,"numValue":53.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73357,"numValue":36.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73358,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,603 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,988 | ProTherm | 6.5 | DSC | Thermal | PIPES | 10 mM | null | NaCl | 100 mM | 55.2 | null | null | null | 41.35 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73359,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73360,"numValue":41.35,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73361,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,604 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,989 | ProTherm | 7 | DSC | Thermal | PIPES | 10 mM | null | NaCl | 100 mM | 55.7 | null | null | null | 41.35 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73362,"numValue":55.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73363,"numValue":41.35,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73364,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,605 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,990 | ProTherm | 7.5 | DSC | Thermal | PIPES | 10 mM | null | NaCl | 100 mM | 56 | null | null | null | 42.3 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":73365,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73366,"numValue":42.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73367,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,606 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,991 | ProTherm | 6 | DSC | Thermal | MOPS | 10 mM | null | NaCl | 100 mM | 54.1 | null | null | null | 39.91 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":73368,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73369,"numValue":39.91,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73370,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,607 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,992 | ProTherm | 6.5 | DSC | Thermal | MOPS | 10 mM | null | NaCl | 100 mM | 56.1 | null | null | null | 39.91 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":73371,"numValue":56.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73372,"numValue":39.91,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73373,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,608 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,993 | ProTherm | 7 | DSC | Thermal | MOPS | 10 mM | null | NaCl | 100 mM | 56.4 | null | null | null | 40.63 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":73374,"numValue":56.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73375,"numValue":40.63,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73376,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,609 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,994 | ProTherm | 7.5 | DSC | Thermal | MOPS | 10 mM | null | NaCl | 100 mM | 56.2 | null | null | null | 41.35 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":73377,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73378,"numValue":41.35,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73379,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,610 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,995 | ProTherm | 8 | DSC | Thermal | MOPS | 10 mM | null | NaCl | 100 mM | 57.1 | null | null | null | 42.54 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":73380,"numValue":57.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73381,"numValue":42.54,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73382,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,611 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,996 | ProTherm | 6.5 | DSC | Thermal | imidazole | 10 mM | null | NaCl | 100 mM | 53.7 | null | null | null | 39.2 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"imidazole","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":73383,"numValue":53.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73384,"numValue":39.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73385,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,612 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,997 | ProTherm | 7 | DSC | Thermal | imidazole | 10 mM | null | NaCl | 100 mM | 55.8 | null | null | null | 40.15 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"imidazole","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":73386,"numValue":55.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73387,"numValue":40.15,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73388,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,613 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,998 | ProTherm | 7.5 | DSC | Thermal | imidazole | 10 mM | null | NaCl | 100 mM | 55.9 | null | null | null | 38.96 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"imidazole","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":73389,"numValue":55.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73390,"numValue":38.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73391,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,614 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,999 | ProTherm | 8 | DSC | Thermal | imidazole | 10 mM | null | NaCl | 100 mM | 56.8 | null | null | null | 38.24 | null | null | null | null | null | null | null | null | null | null | null | yes(>85%) | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1312 | ARTICLE | Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. | 2,000 | 10.1110/ps.9.2.387 | 10716191 | Protein Sci;9;387-94 | 2 | Makhatadze G I|Petrosian S A | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"imidazole","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":73392,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73393,"numValue":38.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73394,"numValue":null,"references":[],"strValue":"yes(>85%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:14615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14,615 | train | sequence | 336 | 336 | -1 | 70 | -1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | 34 | Cold shock protein CspA | Escherichia coli (strain K12) | 1 | P0A9X9 | IPR012156|IPR050181|IPR011129|IPR019844|IPR002059|IPR012340 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,736 | ProTherm | 7 | CD | Urea | Potassium phosphate | 50 mM | 25 | KCl | 100 mM | null | null | 3 | null | null | null | null | 4.2 | 0.71 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 698 | ARTICLE | Coupling protein stability and protein function in Escherichia coli CspA. | 1,998 | 10.1016/S1359-0278(98)00014-5 | 9565753 | Fold Des;3;87-93 | 3 | Rodriguez H M|Gregoret L M|Hillier B J | [{"numValue":7.0,"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":75733,"numValue":3.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75734,"numValue":0.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75735,"numValue":4.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75736,"numValue":null,"references":[],"st... |
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