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:115 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 115 | train | mutant | 26 | 1 | 27 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28L | P28L | 1 | 1 | 0 | 0 | 28 | P | L | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 26 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:P28L | 54.9 | -4.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:P28L","typ... | [{"datasets":[],"id":76,"numValue":54.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":77,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":78,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:116 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 116 | train | mutant | 3,847 | 1 | 4,328 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28G | P28G | 1 | 1 | 0 | 0 | 28 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 8,860 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P28G | null | null | 2.3 | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":30007,"numValue":2.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30008,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30009,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":30010,"numValue":null,"references":[]... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:117 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 117 | train | mutant | 3,847 | 1 | 4,328 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28G | P28G | 1 | 1 | 0 | 0 | 28 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 8,861 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P28G | null | null | 4.9 | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":30011,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30012,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30013,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":30014,"numValue":null,"references":[... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:118 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 118 | train | mutant | 3,847 | 1 | 4,328 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28G | P28G | 1 | 1 | 0 | 0 | 28 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 9,282 | ProTherm | 7.8 | CD | Urea | potassium phosphate | 10 mM | 25 | 1WQ5_A:P28G | null | null | 4.47 | 1.66 | null | null | null | 2.08 | 2.15 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 629 | ARTICLE | A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein. | 2,002 | 10.1016/s0022-2836(02)00737-4 | 12215410 | J Mol Biol;322;7-13 | 2 | Wu Ying|Matthews C Robert | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":31675,"numValue":4.47,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":31676,"numValue":1.66,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31677,"numValue":2.15,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31678,"numValue":2.08,"references":[],... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:119 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 119 | train | mutant | 3,847 | 1 | 4,328 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28G | P28G | 1 | 1 | 0 | 0 | 28 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 9,284 | ProTherm | 7.8 | CD | Urea | potassium phosphate | 10 mM | 25 | 1WQ5_A:P28G | null | null | 4.84 | -0.12 | null | null | null | 4.1 | 1.18 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 629 | ARTICLE | A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein. | 2,002 | 10.1016/s0022-2836(02)00737-4 | 12215410 | J Mol Biol;322;7-13 | 2 | Wu Ying|Matthews C Robert | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":31687,"numValue":4.84,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":31688,"numValue":-0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31689,"numValue":1.18,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31690,"numValue":4.1,"references":[],... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:120 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 120 | train | mutant | 3,847 | 1 | 4,328 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28G | P28G | 1 | 1 | 0 | 0 | 28 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 11,352 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P28G | null | null | 7.2 | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":39073,"numValue":7.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39074,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39075,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:121 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 121 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 8,862 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P28A | null | null | 2.2 | 2.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":30015,"numValue":2.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30016,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30017,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":30018,"numValue":null,"references":[]... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:122 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 122 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 8,863 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P28A | null | null | 4.1 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":30019,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30020,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30021,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":30022,"numValue":null,"references":[]... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:123 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 123 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 9,281 | ProTherm | 7.8 | CD | Urea | potassium phosphate | 10 mM | 25 | 1WQ5_A:P28A | null | null | 2.01 | 4.12 | null | null | null | 1.36 | 1.48 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 629 | ARTICLE | A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein. | 2,002 | 10.1016/s0022-2836(02)00737-4 | 12215410 | J Mol Biol;322;7-13 | 2 | Wu Ying|Matthews C Robert | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":31669,"numValue":2.01,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":31670,"numValue":4.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31671,"numValue":1.48,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31672,"numValue":1.36,"references":[],... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:124 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 124 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 9,283 | ProTherm | 7.8 | CD | Urea | potassium phosphate | 10 mM | 25 | 1WQ5_A:P28A | null | null | 3.81 | 0.91 | null | null | null | 3.66 | 1.04 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 629 | ARTICLE | A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein. | 2,002 | 10.1016/s0022-2836(02)00737-4 | 12215410 | J Mol Biol;322;7-13 | 2 | Wu Ying|Matthews C Robert | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":31681,"numValue":3.81,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":31682,"numValue":0.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31683,"numValue":1.04,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31684,"numValue":3.66,"references":[],... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:125 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 125 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 10,038 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P28A | null | null | 6.29 | 1.91 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":34497,"numValue":6.29,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34498,"numValue":1.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34499,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:126 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 126 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 11,353 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P28A | null | null | 6.3 | 2.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":39076,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39077,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39078,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:127 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 127 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 11,370 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P28A | null | null | 2.27 | 1.96 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":39154,"numValue":2.27,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39155,"numValue":1.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39156,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39157,"numValue":null,"references":... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:128 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 128 | train | mutant | 3,848 | 1 | 4,329 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P28A | P28A | 1 | 1 | 0 | 0 | 28 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 28 | A | S | false | false | 57.711807 | 33.394286 | 11,371 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P28A | null | null | 4.04 | -0.05 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":39158,"numValue":4.04,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39159,"numValue":-0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39160,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39161,"numValue":null,"references"... | [{"id":6207,"numValue":9.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:129 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 129 | train | mutant | 2 | 1 | 3 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | S33L | S33L | 1 | 1 | 0 | 0 | 33 | S | L | 8 | CONSERVATION | 1WQ5 | 282 | null | 33 | A | H | false | false | 1.612176 | 21.753333 | 2 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:S33L | 51.9 | -7.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:S33L","typ... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4,"numValue":51.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":5,"numValue":-7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":6,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY... | [{"id":6212,"numValue":8.0,"position":33,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:130 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 130 | train | mutant | 4,219 | 1 | 4,724 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | I37A | I37A | 1 | 1 | 0 | 0 | 37 | I | A | 6 | CONSERVATION | 1WQ5 | 282 | null | 37 | A | H | false | false | 1.209338 | 21.605 | 9,650 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:I37A | null | null | 4.72 | 1.41 | null | null | null | null | 2.72 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 648 | ARTICLE | Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein. | 2,005 | 10.1016/j.jmb.2005.06.006 | 16023136 | J Mol Biol;351;445-52 | 4 | Wu Ying|Matthews C Robert|Vadrevu Ramakrishna|Yang Xiaoyan | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":33119,"numValue":4.72,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33120,"numValue":1.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33121,"numValue":2.72,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33122,"numValue":3.0,"references":[],"... | [{"id":6216,"numValue":6.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:131 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 131 | train | mutant | 4,219 | 1 | 4,724 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | I37A | I37A | 1 | 1 | 0 | 0 | 37 | I | A | 6 | CONSERVATION | 1WQ5 | 282 | null | 37 | A | H | false | false | 1.209338 | 21.605 | 9,655 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:I37A | null | null | 1.71 | 3.01 | null | null | null | null | 0.64 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 648 | ARTICLE | Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein. | 2,005 | 10.1016/j.jmb.2005.06.006 | 16023136 | J Mol Biol;351;445-52 | 4 | Wu Ying|Matthews C Robert|Vadrevu Ramakrishna|Yang Xiaoyan | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":33144,"numValue":1.71,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33145,"numValue":3.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33146,"numValue":0.64,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33147,"numValue":3.0,"references":[],"... | [{"id":6216,"numValue":6.0,"position":37,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:132 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 132 | train | mutant | 14 | 1 | 15 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49G | E49G | 1 | 1 | 0 | 0 | 49 | E | G | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 14 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:E49G | 57.7 | -1.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49G","typ... | [{"datasets":[],"id":40,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":41,"numValue":-1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":42,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:133 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 133 | train | mutant | 14 | 1 | 15 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49G | E49G | 1 | 1 | 0 | 0 | 49 | E | G | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,285 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49G | null | null | 18.24 | -0.08 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38874,"numValue":18.24,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38875,"numValue":-0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38876,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:134 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 134 | train | mutant | 14 | 1 | 15 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49G | E49G | 1 | 1 | 0 | 0 | 49 | E | G | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,303 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49G | null | null | 18.57 | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38928,"numValue":18.57,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38929,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38930,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:135 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 135 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 328 | ProTherm | 7.2 | CD | Thermal | tetra-borate | 1 mM | null | 1WQ5_A:E49Q | 59.6 | null | null | null | null | 2.68 | 14.3 | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49Q","type":"_... | [{"datasets":[],"id":1348,"numValue":59.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1349,"numValue":2.68,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1350,"numValue":14.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1351,"numValue":null,"references":[],"... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:136 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 136 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 329 | ProTherm | 9.3 | CD | Thermal | tetra-borate | 1 mM | null | 1WQ5_A:E49Q | 59.6 | null | null | null | null | 2.68 | 14.3 | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49Q","type":"_... | [{"datasets":[],"id":1352,"numValue":59.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1353,"numValue":2.68,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1354,"numValue":14.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1355,"numValue":null,"references":[],"... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:137 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 137 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 330 | ProTherm | 7 | DSC | Thermal | tetra-borate | 1 mM | null | 1WQ5_A:E49Q | 59.4 | null | null | null | null | 2.87 | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49Q","type":"... | [{"datasets":[],"id":1356,"numValue":59.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1357,"numValue":2.87,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1358,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:138 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 138 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 331 | ProTherm | 9.3 | DSC | Thermal | tetra-borate | 1 mM | null | 1WQ5_A:E49Q | 62.4 | null | null | null | null | 2.87 | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49Q","type":"... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1359,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1360,"numValue":2.87,"references":[],"strValue":null,"type":"DCP"},{"datasets":["HotMuSiC_S1626.csv"],"id":1361,"numValue":null,"references":[],"strValue":"yes(70-95%)","typ... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:140 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 140 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 460 | ProTherm | 9.3 | DSC | Thermal | sodium tetraborate | 1 mM | null | 1WQ5_A:E49Q | 62.4 | null | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(>70%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49Q","t... | [{"datasets":[],"id":1850,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1851,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1852,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:141 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 141 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,476 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25.8 | 1WQ5_A:E49Q | null | null | 6.3 | 2.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 586 | ARTICLE | Comparison of denaturation by guanidine hydrochloride of the wild type tryptophan synthase alpha-subunit of Escherichia coli and two mutant protein (Glu 49 replaced by Met or Gln). | 1,979 | 10.1093/oxfordjournals.jbchem.a132423 | 378988 | J Biochem;85;915-21 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":28833,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28834,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28835,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:142 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 142 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,533 | ProTherm | 9 | CD | GdnHCl | Tris-HCl | 0.025 M | 25 | 1WQ5_A:E49Q | null | null | 8.5 | -3.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.025 M","type":"BUFFER_C... | [{"datasets":[],"id":28965,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28966,"numValue":-3.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28967,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:143 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 143 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,538 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | 1WQ5_A:E49Q | null | null | 6.3 | 2.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":28980,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28981,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28982,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:144 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 144 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,543 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.05 M | 25 | 1WQ5_A:E49Q | null | null | 2.8 | 2.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CON... | [{"datasets":[],"id":28995,"numValue":2.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28996,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28997,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:145 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 145 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,686 | ProTherm | 7.2 | CD | Thermal | tetra-borate | 1 mM | 25 | 1WQ5_A:E49Q | null | null | 6.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.2,"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":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER... | [{"datasets":[],"id":29426,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29427,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:147 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 147 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,688 | ProTherm | 7 | DSC | Thermal | tetra-borate | 1 mM | 25 | 1WQ5_A:E49Q | null | null | 7.4 | null | 23.2 | null | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | DH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"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":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFE... | [{"datasets":[],"id":29430,"numValue":23.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":29431,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29432,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:149 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 149 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,753 | ProTherm | 7 | DSC | Thermal | potassium phosphate | 1 mM | 25 | 1WQ5_A:E49Q | null | null | 7.4 | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(<50%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":7.0,"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":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type"... | [{"datasets":[],"id":29567,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29568,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29569,"numValue":null,"references":[],"strValue":"yes(<50%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:150 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 150 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,755 | ProTherm | 9.3 | DSC | Thermal | sodium tetraborate | 1 mM | 25 | 1WQ5_A:E49Q | null | null | 8.4 | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(>70%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":9.3,"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 tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":... | [{"datasets":[],"id":29573,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29574,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29575,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:151 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 151 | train | mutant | 187 | 1 | 215 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Q | E49Q | 1 | 1 | 0 | 0 | 49 | E | Q | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,297 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49Q | null | null | 17.93 | 0.23 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38910,"numValue":17.93,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":38911,"numValue":0.23,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38912,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:153 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 153 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 459 | ProTherm | 7 | DSC | Thermal | potassium phosphate | 1 mM | null | 1WQ5_A:E49S | 60.5 | null | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(<50%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":7.0,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49S","... | [{"datasets":[],"id":1847,"numValue":60.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1848,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1849,"numValue":null,"references":[],"strValue":"yes(<50%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:154 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 154 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 461 | ProTherm | 9.3 | DSC | Thermal | sodium tetraborate | 1 mM | null | 1WQ5_A:E49S | 58.6 | null | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(>70%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:E49S","t... | [{"datasets":[],"id":1853,"numValue":58.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1854,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1855,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:155 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 155 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,534 | ProTherm | 9 | CD | GdnHCl | Tris-HCl | 0.025 M | 25 | 1WQ5_A:E49S | null | null | 8 | -3.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.025 M","type":"BUFFER_C... | [{"datasets":[],"id":28968,"numValue":8.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28969,"numValue":-3.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28970,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:156 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 156 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,539 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | 1WQ5_A:E49S | null | null | 7.4 | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":28983,"numValue":7.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28984,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28985,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:157 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 157 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,544 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.05 M | 25 | 1WQ5_A:E49S | null | null | 3.9 | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CON... | [{"datasets":[],"id":28998,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28999,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29000,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:158 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 158 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,754 | ProTherm | 7 | DSC | Thermal | potassium phosphate | 1 mM | 25 | 1WQ5_A:E49S | null | null | 7.7 | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(<50%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":7.0,"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":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type"... | [{"datasets":[],"id":29570,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29571,"numValue":7.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29572,"numValue":null,"references":[],"strValue":"yes(<50%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:159 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 159 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,756 | ProTherm | 9.3 | DSC | Thermal | sodium tetraborate | 1 mM | 25 | 1WQ5_A:E49S | null | null | 7.1 | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(>70%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":9.3,"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 tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":... | [{"datasets":[],"id":29576,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":29577,"numValue":7.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29578,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:160 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 160 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,302 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49S | null | null | 17.57 | 0.59 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38925,"numValue":17.57,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38926,"numValue":0.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38927,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:161 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 161 | train | mutant | 255 | 1 | 286 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49S | E49S | 1 | 1 | 0 | 0 | 49 | E | S | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,320 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49S | null | null | 18.06 | -0.09 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38979,"numValue":18.06,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38980,"numValue":-0.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38981,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:162 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 162 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,477 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25.8 | 1WQ5_A:E49M | null | null | 13.4 | -4.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 586 | ARTICLE | Comparison of denaturation by guanidine hydrochloride of the wild type tryptophan synthase alpha-subunit of Escherichia coli and two mutant protein (Glu 49 replaced by Met or Gln). | 1,979 | 10.1093/oxfordjournals.jbchem.a132423 | 378988 | J Biochem;85;915-21 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":28836,"numValue":13.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28837,"numValue":-4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28838,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:163 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 163 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,535 | ProTherm | 9 | CD | GdnHCl | Tris-HCl | 0.025 M | 25 | 1WQ5_A:E49M | null | null | 8.4 | -3.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.025 M","type":"BUFFER_C... | [{"datasets":[],"id":28971,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28972,"numValue":-3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28973,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:164 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 164 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,540 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | 1WQ5_A:E49M | null | null | 13.3 | -4.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":28986,"numValue":13.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28987,"numValue":-4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28988,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:165 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 165 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,545 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.05 M | 25 | 1WQ5_A:E49M | null | null | 5.9 | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CON... | [{"datasets":[],"id":29001,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29002,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29003,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:166 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 166 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 10,457 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:E49M | null | null | 9.4 | -3.7 | null | null | null | 3.33 | 2.8 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 681 | ARTICLE | Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,986 | 10.1021/bi00358a035 | 2872918 | Biochemistry;25;2965-74 | 6 | Stackhouse T|Matthews C R|Beasty A M|Hurle M R|Manz J T|Onuffer J J | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":35836,"numValue":9.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35837,"numValue":-3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35838,"numValue":2.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35839,"numValue":3.33,"references":[],"s... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:167 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 167 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 10,458 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:E49M | null | null | 7 | -2 | null | null | null | 4.92 | 1.4 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 681 | ARTICLE | Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,986 | 10.1021/bi00358a035 | 2872918 | Biochemistry;25;2965-74 | 6 | Stackhouse T|Matthews C R|Beasty A M|Hurle M R|Manz J T|Onuffer J J | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":35842,"numValue":7.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35843,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35844,"numValue":1.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35845,"numValue":4.92,"references":[],"s... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:168 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 168 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,300 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49M | null | null | 18.11 | 0.05 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38919,"numValue":18.11,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38920,"numValue":0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38921,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:169 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 169 | train | mutant | 3,691 | 1 | 4,142 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49M | E49M | 1 | 1 | 0 | 0 | 49 | E | M | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,318 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49M | null | null | 18.49 | -0.52 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38973,"numValue":18.49,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38974,"numValue":-0.52,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38975,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:170 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 170 | train | mutant | 3,722 | 1 | 4,173 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49V | E49V | 1 | 1 | 0 | 0 | 49 | E | V | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,536 | ProTherm | 9 | CD | GdnHCl | Tris-HCl | 0.025 M | 25 | 1WQ5_A:E49V | null | null | 9.4 | -4.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.025 M","type":"BUFFER_C... | [{"datasets":[],"id":28974,"numValue":9.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28975,"numValue":-4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28976,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:171 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 171 | train | mutant | 3,722 | 1 | 4,173 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49V | E49V | 1 | 1 | 0 | 0 | 49 | E | V | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,541 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | 1WQ5_A:E49V | null | null | 12 | -3.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":28989,"numValue":12.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28990,"numValue":-3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28991,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:172 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 172 | train | mutant | 3,722 | 1 | 4,173 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49V | E49V | 1 | 1 | 0 | 0 | 49 | E | V | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,546 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.05 M | 25 | 1WQ5_A:E49V | null | null | 6.1 | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CON... | [{"datasets":[],"id":29004,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29005,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29006,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:173 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 173 | train | mutant | 3,722 | 1 | 4,173 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49V | E49V | 1 | 1 | 0 | 0 | 49 | E | V | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,287 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49V | null | null | 18.3 | -0.14 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38880,"numValue":18.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38881,"numValue":-0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38882,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:175 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 175 | train | mutant | 3,723 | 1 | 4,174 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Y | E49Y | 1 | 1 | 0 | 0 | 49 | E | Y | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,537 | ProTherm | 9 | CD | GdnHCl | Tris-HCl | 0.025 M | 25 | 1WQ5_A:E49Y | null | null | 6.8 | -1.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.025 M","type":"BUFFER_C... | [{"datasets":[],"id":28977,"numValue":6.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":28978,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28979,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:176 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 176 | train | mutant | 3,723 | 1 | 4,174 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Y | E49Y | 1 | 1 | 0 | 0 | 49 | E | Y | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,542 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | 1WQ5_A:E49Y | null | null | 8.8 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":28992,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":28993,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28994,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:177 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 177 | train | mutant | 3,723 | 1 | 4,174 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Y | E49Y | 1 | 1 | 0 | 0 | 49 | E | Y | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 8,547 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.05 M | 25 | 1WQ5_A:E49Y | null | null | 4.8 | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CON... | [{"datasets":[],"id":29007,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29008,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29009,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:178 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 178 | train | mutant | 3,723 | 1 | 4,174 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Y | E49Y | 1 | 1 | 0 | 0 | 49 | E | Y | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,291 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49Y | null | null | 17.99 | 0.17 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38892,"numValue":17.99,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38893,"numValue":0.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38894,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:179 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 179 | train | mutant | 3,723 | 1 | 4,174 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49Y | E49Y | 1 | 1 | 0 | 0 | 49 | E | Y | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,309 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49Y | null | null | 18.23 | -0.26 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38946,"numValue":18.23,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38947,"numValue":-0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38948,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:180 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 180 | train | mutant | 4,804 | 1 | 5,345 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49A | E49A | 1 | 1 | 0 | 0 | 49 | E | A | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,286 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49A | null | null | 18.08 | 0.08 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38877,"numValue":18.08,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38878,"numValue":0.08,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38879,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:181 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 181 | train | mutant | 4,804 | 1 | 5,345 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49A | E49A | 1 | 1 | 0 | 0 | 49 | E | A | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,304 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49A | null | null | 18.56 | -0.59 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38931,"numValue":18.56,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38932,"numValue":-0.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38933,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:182 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 182 | train | mutant | 4,805 | 1 | 5,346 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49I | E49I | 1 | 1 | 0 | 0 | 49 | E | I | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,288 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49I | null | null | 18.62 | -0.46 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38883,"numValue":18.62,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38884,"numValue":-0.46,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38885,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:183 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 183 | train | mutant | 4,805 | 1 | 5,346 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49I | E49I | 1 | 1 | 0 | 0 | 49 | E | I | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,306 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49I | null | null | 19.21 | -1.24 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38937,"numValue":19.21,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38938,"numValue":-1.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38939,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:184 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 184 | train | mutant | 4,806 | 1 | 5,347 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49L | E49L | 1 | 1 | 0 | 0 | 49 | E | L | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,289 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49L | null | null | 18.6 | -0.44 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38886,"numValue":18.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38887,"numValue":-0.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38888,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:185 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 185 | train | mutant | 4,806 | 1 | 5,347 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49L | E49L | 1 | 1 | 0 | 0 | 49 | E | L | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,307 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49L | null | null | 19.01 | -1.04 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38940,"numValue":19.01,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38941,"numValue":-1.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38942,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:186 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 186 | train | mutant | 4,807 | 1 | 5,348 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49P | E49P | 1 | 1 | 0 | 0 | 49 | E | P | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,290 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49P | null | null | 18.16 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":38889,"numValue":18.16,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38890,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38891,"numValue":null,"referenc... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:187 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 187 | train | mutant | 4,807 | 1 | 5,348 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49P | E49P | 1 | 1 | 0 | 0 | 49 | E | P | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,308 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49P | null | null | 18.77 | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":38943,"numValue":18.77,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38944,"numValue":-0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38945,"numValue":null,"referen... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:188 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 188 | train | mutant | 4,808 | 1 | 5,349 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49F | E49F | 1 | 1 | 0 | 0 | 49 | E | F | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,292 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49F | null | null | 17.3 | 0.86 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38895,"numValue":17.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38896,"numValue":0.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38897,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:190 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 190 | train | mutant | 4,809 | 1 | 5,350 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49W | E49W | 1 | 1 | 0 | 0 | 49 | E | W | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,293 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49W | null | null | 17.19 | 0.97 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38898,"numValue":17.19,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":38899,"numValue":0.97,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38900,"numValue":null,"references":[],... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:191 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 191 | train | mutant | 4,809 | 1 | 5,350 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49W | E49W | 1 | 1 | 0 | 0 | 49 | E | W | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,311 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49W | null | null | 16.87 | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38952,"numValue":16.87,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":38953,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38954,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:192 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 192 | train | mutant | 4,810 | 1 | 5,351 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49H | E49H | 1 | 1 | 0 | 0 | 49 | E | H | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,294 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49H | null | null | 18.49 | -0.33 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38901,"numValue":18.49,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38902,"numValue":-0.33,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38903,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:193 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 193 | train | mutant | 4,810 | 1 | 5,351 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49H | E49H | 1 | 1 | 0 | 0 | 49 | E | H | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,312 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49H | null | null | 18.64 | -0.67 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38955,"numValue":18.64,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38956,"numValue":-0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38957,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:194 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 194 | train | mutant | 4,811 | 1 | 5,352 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49K | E49K | 1 | 1 | 0 | 0 | 49 | E | K | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,295 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49K | null | null | 17.96 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38904,"numValue":17.96,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":38905,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38906,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:195 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 195 | train | mutant | 4,811 | 1 | 5,352 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49K | E49K | 1 | 1 | 0 | 0 | 49 | E | K | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,313 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49K | null | null | 18.36 | -0.39 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38958,"numValue":18.36,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":38959,"numValue":-0.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38960,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:197 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 197 | train | mutant | 4,812 | 1 | 5,353 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49N | E49N | 1 | 1 | 0 | 0 | 49 | E | N | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,314 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49N | null | null | 18.24 | -0.27 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38961,"numValue":18.24,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":38962,"numValue":-0.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38963,"numValue":null,"references":[]... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:198 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 198 | train | mutant | 4,813 | 1 | 5,354 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49D | E49D | 1 | 1 | 0 | 0 | 49 | E | D | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,298 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49D | null | null | 17.36 | 0.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38913,"numValue":17.36,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":38914,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38915,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:199 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 199 | train | mutant | 4,813 | 1 | 5,354 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49D | E49D | 1 | 1 | 0 | 0 | 49 | E | D | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,316 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49D | null | null | 17.94 | 0.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38967,"numValue":17.94,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38968,"numValue":0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38969,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:200 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 200 | train | mutant | 4,814 | 1 | 5,355 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49C | E49C | 1 | 1 | 0 | 0 | 49 | E | C | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,299 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49C | null | null | 18.17 | -0.01 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38916,"numValue":18.17,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":38917,"numValue":-0.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38918,"numValue":null,"references":[],"strValue":"yes","... | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:201 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 201 | train | mutant | 4,814 | 1 | 5,355 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49C | E49C | 1 | 1 | 0 | 0 | 49 | E | C | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,317 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49C | null | null | 17.84 | 0.13 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38970,"numValue":17.84,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":38971,"numValue":0.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38972,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:202 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 202 | train | mutant | 4,815 | 1 | 5,356 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49T | E49T | 1 | 1 | 0 | 0 | 49 | E | T | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,301 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49T | null | null | 17.54 | 0.62 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38922,"numValue":17.54,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38923,"numValue":0.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38924,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:203 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 203 | train | mutant | 4,815 | 1 | 5,356 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | E49T | E49T | 1 | 1 | 0 | 0 | 49 | E | T | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | 49 | A | E | true | true | 1.460017 | 32.138889 | 11,319 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | 1WQ5_A:E49T | null | null | 17.71 | 0.26 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":38976,"numValue":17.71,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38977,"numValue":0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38978,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":1,"numValue":null,"position":49,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6228,"numValue":9.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:204 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 204 | train | mutant | 4,220 | 1 | 4,725 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | L50A | L50A | 1 | 1 | 0 | 0 | 50 | L | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 50 | A | E | false | false | 0.134371 | 19.75875 | 9,651 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L50A | null | null | 5.99 | 0.14 | null | null | null | null | 2.87 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 648 | ARTICLE | Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein. | 2,005 | 10.1016/j.jmb.2005.06.006 | 16023136 | J Mol Biol;351;445-52 | 4 | Wu Ying|Matthews C Robert|Vadrevu Ramakrishna|Yang Xiaoyan | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":33124,"numValue":5.99,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33125,"numValue":0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33126,"numValue":2.87,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33127,"numValue":3.0,"references":[],"... | [{"id":6229,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:205 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 205 | train | mutant | 4,220 | 1 | 4,725 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | L50A | L50A | 1 | 1 | 0 | 0 | 50 | L | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 50 | A | E | false | false | 0.134371 | 19.75875 | 9,656 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L50A | null | null | 1.87 | 2.85 | null | null | null | null | 0.7 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 648 | ARTICLE | Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein. | 2,005 | 10.1016/j.jmb.2005.06.006 | 16023136 | J Mol Biol;351;445-52 | 4 | Wu Ying|Matthews C Robert|Vadrevu Ramakrishna|Yang Xiaoyan | [{"numValue":7.8,"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":"10 mM","type":"B... | [{"datasets":[],"id":33149,"numValue":1.87,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33150,"numValue":2.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33151,"numValue":0.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33152,"numValue":3.0,"references":[],"s... | [{"id":6229,"numValue":7.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:206 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 206 | train | mutant | 25 | 1 | 26 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | G51D | G51D | 1 | 1 | 0 | 0 | 51 | G | D | 9 | CONSERVATION | 1WQ5 | 282 | null | 51 | A | E | true | false | 6.020028 | 28.4825 | 25 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:G51D | 55 | -4.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:G51D","typ... | [{"datasets":[],"id":73,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":74,"numValue":-4.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv"],"id":75,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6230,"numValue":9.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:207 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 207 | train | mutant | 21 | 1 | 22 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P53H | P53H | 1 | 1 | 0 | 0 | 53 | P | H | 9 | CONSERVATION | 1WQ5 | 282 | null | 53 | A | L | true | false | 47.111188 | 39.942857 | 21 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:P53H | 56.2 | -3.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:P53H","typ... | [{"datasets":[],"id":61,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":62,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":63,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6232,"numValue":9.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:208 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 208 | train | mutant | 23 | 1 | 24 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P53T | P53T | 1 | 1 | 0 | 0 | 53 | P | T | 9 | CONSERVATION | 1WQ5 | 282 | null | 53 | A | L | true | false | 47.111188 | 39.942857 | 23 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:P53T | 55.2 | -4.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:P53T","typ... | [{"datasets":[],"id":67,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":68,"numValue":-4.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":69,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6232,"numValue":9.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:209 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 209 | train | mutant | 15 | 1 | 16 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | D56G | D56G | 1 | 1 | 0 | 0 | 56 | D | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 56 | A | L | true | false | 164.902387 | 76.884999 | 15 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:D56G | 57.5 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:D56G","typ... | [{"datasets":[],"id":43,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":44,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":45,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6235,"numValue":9.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:210 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 210 | train | mutant | 520 | 1 | 571 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P57A | P57A | 1 | 1 | 0 | 0 | 57 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 848 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_B:P1057A | 54 | -0.1 | null | null | 121.1 | 4.7 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_B:P1057A",... | [{"datasets":[],"id":3191,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3192,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3193,"numValue":121.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":3194,"numValue":4.7,"references":[],"st... | [{"id":6236,"numValue":9.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||
fireprotdb:211 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 211 | train | mutant | 520 | 1 | 571 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P57A | P57A | 1 | 1 | 0 | 0 | 57 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 7,309 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 54.1 | EDTA | 1 mM | 1WQ5_B:P1057A | null | null | null | 0.04 | null | 4.7 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":54.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":... | [{"datasets":[],"id":25514,"numValue":4.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25515,"numValue":0.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25516,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6236,"numValue":9.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:212 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 212 | train | mutant | 520 | 1 | 571 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P57A | P57A | 1 | 1 | 0 | 0 | 57 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 10,039 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_B:P1057A | null | null | 7.73 | 0.48 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":34500,"numValue":7.73,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34501,"numValue":0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34502,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6236,"numValue":9.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||
fireprotdb:213 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 213 | train | mutant | 520 | 1 | 571 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P57A | P57A | 1 | 1 | 0 | 0 | 57 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 11,372 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_B:P1057A | null | null | 4 | 0.24 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":39162,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39163,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39164,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39165,"numValue":null,"references":[... | [{"id":6236,"numValue":9.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||
fireprotdb:214 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 214 | train | mutant | 520 | 1 | 571 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P57A | P57A | 1 | 1 | 0 | 0 | 57 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 11,373 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_B:P1057A | null | null | 3.76 | 0.24 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":39166,"numValue":3.76,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39167,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39168,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39169,"numValue":null,"references":... | [{"id":6236,"numValue":9.0,"position":57,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||
fireprotdb:215 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 215 | train | mutant | 17 | 1 | 18 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | D60G | D60G | 1 | 1 | 0 | 0 | 60 | D | G | 9 | ACTIVE_SITE|CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 17 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:D60G | 56.9 | -2.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:D60G","typ... | [{"datasets":[],"id":49,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":50,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":51,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":2,"numValue":null,"position":60,"positionArray":null,"positionRange":null,"strValue":"Proton acceptor","type":"ACTIVE_SITE"},{"id":6239,"numValue":9.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||
fireprotdb:216 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 216 | train | mutant | 12 | 1 | 13 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P62Q | P62Q | 1 | 1 | 0 | 0 | 62 | P | Q | 7 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 12 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 58.9 | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":34,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":35,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":36,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6241,"numValue":7.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:218 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 218 | train | mutant | 521 | 1 | 572 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P62A | P62A | 1 | 1 | 0 | 0 | 62 | P | A | 7 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 7,310 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 54.1 | EDTA | 1 mM | null | null | null | 0.52 | null | 4.9 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":54.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":... | [{"datasets":[],"id":25517,"numValue":4.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25518,"numValue":0.52,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25519,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6241,"numValue":7.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||
fireprotdb:219 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 219 | train | mutant | 521 | 1 | 572 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P62A | P62A | 1 | 1 | 0 | 0 | 62 | P | A | 7 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 10,040 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | null | null | 7.89 | 0.31 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":34503,"numValue":7.89,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34504,"numValue":0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34505,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6241,"numValue":7.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:220 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 220 | train | mutant | 521 | 1 | 572 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P62A | P62A | 1 | 1 | 0 | 0 | 62 | P | A | 7 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 11,374 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | null | null | 3.54 | 0.69 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":39170,"numValue":3.54,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39171,"numValue":0.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39172,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39173,"numValue":null,"references":... | [{"id":6241,"numValue":7.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||
fireprotdb:221 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 221 | train | mutant | 521 | 1 | 572 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | P62A | P62A | 1 | 1 | 0 | 0 | 62 | P | A | 7 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 11,375 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | null | null | 4.35 | -0.36 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":39174,"numValue":4.35,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39175,"numValue":-0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39176,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39177,"numValue":null,"references"... | [{"id":6241,"numValue":7.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||
fireprotdb:222 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 222 | train | mutant | 22 | 1 | 23 | 268 | 268 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | 1 | Tryptophan synthase alpha chain | Escherichia coli (strain K12) | 1 | P0A877 | IPR013785|IPR011060|IPR018204|IPR002028 | 4.2.1.20 | T63K | T63K | 1 | 1 | 0 | 0 | 63 | T | K | 8 | CONSERVATION | 1WQ5 | 282 | null | false | false | null | null | 22 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:T63K | 56.2 | -3.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"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":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:T63K","typ... | [{"datasets":[],"id":64,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":66,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6242,"numValue":8.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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