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:223 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 223 | train | mutant | 11 | 1 | 12 | 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 | Q65R | Q65R | 1 | 1 | 0 | 0 | 65 | Q | R | 9 | CONSERVATION | 1WQ5 | 282 | null | 65 | A | L | false | false | 228.142732 | 87.204444 | 11 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:Q65R | 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|_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:Q65R","typ... | [{"datasets":[],"id":31,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":32,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":33,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6244,"numValue":9.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:224 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 224 | train | mutant | 18 | 1 | 19 | 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 | A67V | A67V | 1 | 1 | 0 | 0 | 67 | A | V | 9 | CONSERVATION | 1WQ5 | 282 | null | 67 | A | L | false | false | 90.279389 | 54.108 | 18 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:A67V | 56.8 | -2.7 | 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:A67V","typ... | [{"datasets":[],"id":52,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6246,"numValue":9.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:225 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 225 | train | mutant | 7 | 1 | 8 | 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 | P78L | P78L | 1 | 1 | 0 | 0 | 78 | P | L | 5 | CONSERVATION | 1WQ5 | 282 | null | 78 | A | H | true | false | 23.640398 | 33.967143 | 7 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:P78L | 61.4 | 1.9 | 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:P78L","typ... | [{"datasets":["HotMuSiC_S1626.csv"],"id":19,"numValue":61.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":20,"numValue":1.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":21,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILI... | [{"id":6257,"numValue":5.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:226 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 226 | train | mutant | 13 | 1 | 14 | 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 | P78S | P78S | 1 | 1 | 0 | 0 | 78 | P | S | 5 | CONSERVATION | 1WQ5 | 282 | null | 78 | A | H | true | false | 23.640398 | 33.967143 | 13 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:P78S | 57.9 | -1.6 | 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:P78S","typ... | [{"datasets":[],"id":37,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":38,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":39,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6257,"numValue":5.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:227 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 227 | train | mutant | 261 | 1 | 292 | 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 | C81S | C81S | 1 | 1 | 0 | 0 | 81 | C | S | 7 | CONSERVATION | 1WQ5 | 282 | null | 81 | A | H | false | false | 0 | 28.176667 | 467 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C81S | 49.1 | -4.4 | null | null | 92.82 | 5.02 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C81S","t... | [{"datasets":[],"id":1866,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1867,"numValue":-4.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1868,"numValue":92.82,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1869,"numValue":5.02,"references":[],"s... | [{"id":6260,"numValue":7.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:228 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 228 | train | mutant | 262 | 1 | 293 | 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 | C81G | C81G | 1 | 1 | 0 | 0 | 81 | C | G | 7 | CONSERVATION | 1WQ5 | 282 | null | 81 | A | H | false | false | 0 | 28.176667 | 468 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C81G | 48.7 | -4.8 | null | null | 104.31 | 6.82 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C81G","t... | [{"datasets":[],"id":1871,"numValue":48.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1872,"numValue":-4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1873,"numValue":104.31,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1874,"numValue":6.82,"references":[],"... | [{"id":6260,"numValue":7.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:229 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 229 | train | mutant | 263 | 1 | 294 | 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 | C81A | C81A | 1 | 1 | 0 | 0 | 81 | C | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 81 | A | H | false | false | 0 | 28.176667 | 469 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C81A | 51.8 | -1.7 | null | null | 83.49 | 4.11 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C81A","t... | [{"datasets":[],"id":1876,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1877,"numValue":-1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1878,"numValue":83.49,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1879,"numValue":4.11,"references":[],"s... | [{"id":6260,"numValue":7.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:230 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 230 | train | mutant | 263 | 1 | 294 | 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 | C81A | C81A | 1 | 1 | 0 | 0 | 81 | C | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 81 | A | H | false | false | 0 | 28.176667 | 7,667 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 50 | 1WQ5_A:C81A | null | null | 0.48 | 0.69 | null | 4.11 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":50.0,"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":26399,"numValue":4.11,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26400,"numValue":0.48,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26401,"numValue":0.69,"references":[],"strValue":null,"typ... | [{"id":6260,"numValue":7.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:231 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 231 | train | mutant | 264 | 1 | 295 | 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 | C81V | C81V | 1 | 1 | 0 | 0 | 81 | C | V | 7 | CONSERVATION | 1WQ5 | 282 | null | 81 | A | H | false | false | 0 | 28.176667 | 470 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C81V | 49.1 | -4.4 | null | null | 57.42 | 4.31 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C81V","t... | [{"datasets":[],"id":1881,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1882,"numValue":-4.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1883,"numValue":57.42,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1884,"numValue":4.31,"references":[],"s... | [{"id":6260,"numValue":7.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:233 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 233 | train | mutant | 7,122 | 1 | 7,775 | 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 | P93A|H244A | P93A|H244A | 2 | 2 | 0 | 0 | 93 | P | A | 4 | CONSERVATION | 1WQ5 | 282 | null | 93|244 | A | S|T | true | false | 59.553038 | 31.851715 | 15,351 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | 1WQ5_A:P93A 1WQ5_A:H244A | null | null | 3.4 | null | null | null | null | 5.4 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 717 | ARTICLE | Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. | 1,996 | 10.1021/bi951726o | 8639683 | Biochemistry;35;1988-94 | 3 | Matthews C R|Saab-Rinc?n G|Gualfetti P J | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"... | [{"datasets":[],"id":56345,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56346,"numValue":5.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56347,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6272,"numValue":4.0,"position":93,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6423,"numValue":4.0,"position":244,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:234 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 234 | train | mutant | 4,600 | 1 | 5,122 | 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 | I95A | I95A | 1 | 1 | 0 | 0 | 95 | I | A | 6 | CONSERVATION | 1WQ5 | 282 | null | 95 | A | S | true | false | 15.832892 | 21.91375 | 10,803 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | 1WQ5_A:I95A | null | null | 7.9 | null | null | null | null | 6.2 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 717 | ARTICLE | Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. | 1,996 | 10.1021/bi951726o | 8639683 | Biochemistry;35;1988-94 | 3 | Matthews C R|Saab-Rinc?n G|Gualfetti P J | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"... | [{"datasets":[],"id":37182,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37183,"numValue":6.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":37184,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6274,"numValue":6.0,"position":95,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:235 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 235 | train | mutant | 524 | 1 | 575 | 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 | P96A | P96A | 1 | 1 | 0 | 0 | 96 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 96 | A | L | true | false | 1.47808 | 18.415714 | 852 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:P96A | 47.8 | -6.3 | null | null | 113.2 | 3.6 | 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_A:P96A","t... | [{"datasets":[],"id":3211,"numValue":47.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3212,"numValue":-6.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3213,"numValue":113.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":3214,"numValue":3.6,"references":[],"st... | [{"id":6275,"numValue":9.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:236 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 236 | train | mutant | 524 | 1 | 575 | 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 | P96A | P96A | 1 | 1 | 0 | 0 | 96 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 96 | A | L | true | false | 1.47808 | 18.415714 | 7,313 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 54.1 | EDTA | 1 mM | 1WQ5_A:P96A | null | null | null | 2 | null | 3.6 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | 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":25526,"numValue":3.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25527,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25528,"numValue":null,"references":[],"strValue":"yes","typ... | [{"id":6275,"numValue":9.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:237 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 237 | train | mutant | 524 | 1 | 575 | 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 | P96A | P96A | 1 | 1 | 0 | 0 | 96 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 96 | A | L | true | false | 1.47808 | 18.415714 | 10,041 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P96A | null | null | 6.08 | 2.13 | 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":34506,"numValue":6.08,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34507,"numValue":2.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34508,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6275,"numValue":9.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:238 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 238 | train | mutant | 524 | 1 | 575 | 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 | P96A | P96A | 1 | 1 | 0 | 0 | 96 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 96 | A | L | true | false | 1.47808 | 18.415714 | 10,804 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | 1WQ5_A:P96A | null | null | 4.9 | null | null | null | null | 8.6 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 717 | ARTICLE | Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. | 1,996 | 10.1021/bi951726o | 8639683 | Biochemistry;35;1988-94 | 3 | Matthews C R|Saab-Rinc?n G|Gualfetti P J | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"... | [{"datasets":[],"id":37185,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37186,"numValue":8.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":37187,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6275,"numValue":9.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:239 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 239 | train | mutant | 524 | 1 | 575 | 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 | P96A | P96A | 1 | 1 | 0 | 0 | 96 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 96 | A | L | true | false | 1.47808 | 18.415714 | 11,376 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P96A | null | null | 2.63 | 1.6 | 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":39178,"numValue":2.63,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39179,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39180,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39181,"numValue":null,"references":[... | [{"id":6275,"numValue":9.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:240 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 240 | train | mutant | 524 | 1 | 575 | 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 | P96A | P96A | 1 | 1 | 0 | 0 | 96 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 96 | A | L | true | false | 1.47808 | 18.415714 | 11,377 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P96A | null | null | 3.44 | 0.55 | 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":39182,"numValue":3.44,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39183,"numValue":0.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39184,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39185,"numValue":null,"references":... | [{"id":6275,"numValue":9.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:241 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 241 | train | mutant | 4,601 | 1 | 5,123 | 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 | I97A | I97A | 1 | 1 | 0 | 0 | 97 | I | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 97 | A | E | false | false | 1.209338 | 17.74 | 10,805 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | 1WQ5_A:I97A | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 717 | ARTICLE | Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. | 1,996 | 10.1021/bi951726o | 8639683 | Biochemistry;35;1988-94 | 3 | Matthews C R|Saab-Rinc?n G|Gualfetti P J | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"... | [{"datasets":[],"id":37188,"numValue":null,"references":[],"strValue":"<4.0","type":"CM"},{"datasets":[],"id":37189,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6276,"numValue":7.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:242 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 242 | train | mutant | 4,221 | 1 | 4,726 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 99 | A | E | false | false | 1.182244 | 17.9125 | 9,652 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L99A | null | null | 4.44 | 1.69 | null | null | null | null | 2.39 | 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":33129,"numValue":4.44,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33130,"numValue":1.69,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33131,"numValue":2.39,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33132,"numValue":3.0,"references":[],"... | [{"id":6278,"numValue":7.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:243 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 243 | train | mutant | 4,221 | 1 | 4,726 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 99 | A | E | false | false | 1.182244 | 17.9125 | 9,657 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L99A | null | null | 2.34 | 2.38 | null | null | null | null | 0.94 | 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":33154,"numValue":2.34,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33155,"numValue":2.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33156,"numValue":0.94,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33157,"numValue":3.0,"references":[],"... | [{"id":6278,"numValue":7.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:244 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 244 | train | mutant | 4,602 | 1 | 5,124 | 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 | L100A | L100A | 1 | 1 | 0 | 0 | 100 | L | A | 8 | CONSERVATION | 1WQ5 | 282 | null | 100 | A | E | true | true | 45.882611 | 22.8075 | 10,806 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | 1WQ5_A:L100A | null | null | 4.7 | null | null | null | null | 5.2 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 717 | ARTICLE | Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. | 1,996 | 10.1021/bi951726o | 8639683 | Biochemistry;35;1988-94 | 3 | Matthews C R|Saab-Rinc?n G|Gualfetti P J | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"... | [{"datasets":[],"id":37190,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37191,"numValue":5.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":37192,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6279,"numValue":8.0,"position":100,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:245 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 245 | train | mutant | 3 | 1 | 4 | 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 | M101V | M101V | 1 | 1 | 0 | 0 | 101 | M | V | 7 | CONSERVATION | 1WQ5 | 282 | null | 101 | A | E | true | false | 8.868482 | 27.3 | 3 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:M101V | 67.1 | 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:M101V","ty... | [{"datasets":["HotMuSiC_S1626.csv"],"id":7,"numValue":67.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":8,"numValue":7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":9,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"... | [{"id":6280,"numValue":7.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:246 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 246 | train | mutant | 4 | 1 | 5 | 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 | M101T | M101T | 1 | 1 | 0 | 0 | 101 | M | T | 7 | CONSERVATION | 1WQ5 | 282 | null | 101 | A | E | true | false | 8.868482 | 27.3 | 4 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:M101T | 67.1 | 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:M101T","ty... | [{"datasets":["HotMuSiC_S1626.csv"],"id":10,"numValue":67.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11,"numValue":7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6280,"numValue":7.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:247 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 247 | train | mutant | 5 | 1 | 6 | 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 | M101I | M101I | 1 | 1 | 0 | 0 | 101 | M | I | 7 | CONSERVATION | 1WQ5 | 282 | null | 101 | A | E | true | false | 8.868482 | 27.3 | 5 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:M101I | 63.2 | 3.7 | 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:M101I","ty... | [{"datasets":["HotMuSiC_S1626.csv"],"id":13,"numValue":63.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":14,"numValue":3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6280,"numValue":7.0,"position":101,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:248 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 248 | train | mutant | 8 | 1 | 9 | 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 | Y102C | Y102C | 1 | 1 | 0 | 0 | 102 | Y | C | 9 | CONSERVATION | 1WQ5 | 282 | null | 102 | A | L | true | false | 130.375369 | 37.594167 | 8 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:Y102C | 60.9 | 1.4 | 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:Y102C","ty... | [{"datasets":[],"id":22,"numValue":60.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":23,"numValue":1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":24,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6281,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:249 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 249 | train | mutant | 9 | 1 | 10 | 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 | Y102H | Y102H | 1 | 1 | 0 | 0 | 102 | Y | H | 9 | CONSERVATION | 1WQ5 | 282 | null | 102 | A | L | true | false | 130.375369 | 37.594167 | 9 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:Y102H | 60.3 | 0.8 | 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:Y102H","ty... | [{"datasets":["HotMuSiC_S1626.csv"],"id":25,"numValue":60.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":26,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":27,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILI... | [{"id":6281,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:250 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 250 | train | mutant | 4,603 | 1 | 5,125 | 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 | Y102A | Y102A | 1 | 1 | 0 | 0 | 102 | Y | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 102 | A | L | true | false | 130.375369 | 37.594167 | 10,807 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | 1WQ5_A:Y102A | null | null | 5.4 | null | null | null | null | 5 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 717 | ARTICLE | Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. | 1,996 | 10.1021/bi951726o | 8639683 | Biochemistry;35;1988-94 | 3 | Matthews C R|Saab-Rinc?n G|Gualfetti P J | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"... | [{"datasets":[],"id":37193,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37194,"numValue":5.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":37195,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6281,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:251 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 251 | train | mutant | 2,080 | 1 | 2,321 | 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 | K109N | K109N | 1 | 1 | 0 | 0 | 109 | K | N | 5 | CONSERVATION | 1WQ5 | 282 | null | 109 | A | H | true | false | 94.391195 | 44.241111 | 4,106 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:K109N | 52.5 | -1.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(>70%) | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 379 | ARTICLE | A thermodynamic analysis of conformational change due to the alpha 2 beta 2 complex formation of tryptophan synthase. | 1,996 | 10.1111/j.1432-1033.1996.0063h.x | 8797836 | Eur J Biochem;240;63-70 | 2 | Yutani K|Hiraga K | [{"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_A:K109N","... | [{"datasets":[],"id":15172,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15173,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15174,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | [{"id":6288,"numValue":5.0,"position":109,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:252 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 252 | train | mutant | 19 | 1 | 20 | 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 | D112N | D112N | 1 | 1 | 0 | 0 | 112 | D | N | 4 | CONSERVATION | 1WQ5 | 282 | null | 112 | A | H | false | false | 65.463721 | 30.845 | 19 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:D112N | 56.4 | -3.1 | 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:D112N","ty... | [{"datasets":[],"id":55,"numValue":56.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":56,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6291,"numValue":4.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:253 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 253 | train | mutant | 27 | 1 | 28 | 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 | D112G | D112G | 1 | 1 | 0 | 0 | 112 | D | G | 4 | CONSERVATION | 1WQ5 | 282 | null | 112 | A | H | false | false | 65.463721 | 30.845 | 27 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:D112G | 54.4 | -5.1 | 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:D112G","ty... | [{"datasets":[],"id":79,"numValue":54.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80,"numValue":-5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":81,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6291,"numValue":4.0,"position":112,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:254 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 254 | train | mutant | 20 | 1 | 21 | 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 | F114L | F114L | 1 | 1 | 0 | 0 | 114 | F | L | 9 | CONSERVATION | 1WQ5 | 282 | null | 114 | A | H | true | false | 1.997788 | 21.177273 | 20 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:F114L | 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:F114L","ty... | [{"datasets":[],"id":58,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":59,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":60,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6293,"numValue":9.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:255 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 255 | train | mutant | 16 | 1 | 17 | 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 | Y115C | Y115C | 1 | 1 | 0 | 0 | 115 | Y | C | 5 | CONSERVATION | 1WQ5 | 282 | null | 115 | A | H | true | false | 3.940814 | 20.02 | 16 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:Y115C | 57.2 | -2.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.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:Y115C","ty... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":46,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":47,"numValue":-2.3,"references":[],"strV... | [{"id":6294,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:256 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 256 | train | mutant | 265 | 1 | 296 | 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 | C118S | C118S | 1 | 1 | 0 | 0 | 118 | C | S | 7 | CONSERVATION | 1WQ5 | 282 | null | 118 | A | H | true | false | 0 | 22.833333 | 471 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C118S | 45 | -8.5 | null | null | 75.6 | 2.3 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C118S","... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1886,"numValue":45.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1887,"numValue":-8.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1888,"numValue":75.6,"references":[],"strValue":null,"type":"DH"},... | [{"id":6297,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:257 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 257 | train | mutant | 266 | 1 | 297 | 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 | C118A | C118A | 1 | 1 | 0 | 0 | 118 | C | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 118 | A | H | true | false | 0 | 22.833333 | 472 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C118A | 49.2 | -4.3 | null | null | 82.3 | 3.3 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C118A","... | [{"datasets":[],"id":1891,"numValue":49.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1892,"numValue":-4.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1893,"numValue":82.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1894,"numValue":3.3,"references":[],"str... | [{"id":6297,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 258 | train | mutant | 267 | 1 | 298 | 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 | C118V | C118V | 1 | 1 | 0 | 0 | 118 | C | V | 7 | CONSERVATION | 1WQ5 | 282 | null | 118 | A | H | true | false | 0 | 22.833333 | 473 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C118V | 49.3 | -4.2 | null | null | 72.97 | 2.42 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C118V","... | [{"datasets":[],"id":1896,"numValue":49.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1897,"numValue":-4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1898,"numValue":72.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1899,"numValue":2.42,"references":[],"s... | [{"id":6297,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 259 | train | mutant | 4,222 | 1 | 4,727 | 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 | L127A | L127A | 1 | 1 | 0 | 0 | 127 | L | A | 8 | CONSERVATION | 1WQ5 | 282 | null | 127 | A | E | true | false | 3.610543 | 22.0575 | 9,653 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L127A | null | null | 5.4 | 0.73 | null | null | null | null | 2.55 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|STATE|REVERSIBILITY | SAAFEC_S1262.csv | 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":33134,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33135,"numValue":0.73,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33136,"numValue":2.55,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33137,"numValue":3.0,... | [{"id":6306,"numValue":8.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:260 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 260 | train | mutant | 4,222 | 1 | 4,727 | 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 | L127A | L127A | 1 | 1 | 0 | 0 | 127 | L | A | 8 | CONSERVATION | 1WQ5 | 282 | null | 127 | A | E | true | false | 3.610543 | 22.0575 | 9,658 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L127A | null | null | 4.17 | 0.55 | null | null | null | null | 1.1 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|DDG|M|STATE|REVERSIBILITY | SAAFEC_S1262.csv | 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":33159,"numValue":4.17,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":33160,"numValue":0.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33161,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33162,"numValue":3.0,... | [{"id":6306,"numValue":8.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 261 | train | mutant | 522 | 1 | 573 | 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 | P132A | P132A | 1 | 1 | 0 | 0 | 132 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 850 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:P132A | 51.5 | -2.6 | null | null | 121.2 | 4.8 | 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_A:P132A","... | [{"datasets":[],"id":3201,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3202,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3203,"numValue":121.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":3204,"numValue":4.8,"references":[],"st... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 262 | train | mutant | 522 | 1 | 573 | 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 | P132A | P132A | 1 | 1 | 0 | 0 | 132 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 7,311 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 54.1 | EDTA | 1 mM | 1WQ5_A:P132A | null | null | null | 0.92 | null | 4.8 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | 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":25520,"numValue":4.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25521,"numValue":0.92,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25522,"numValue":null,"references":[],"strValue":"yes","ty... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:263 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 263 | train | mutant | 522 | 1 | 573 | 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 | P132A | P132A | 1 | 1 | 0 | 0 | 132 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 10,042 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P132A | null | null | 7.15 | 1.05 | 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":34509,"numValue":7.15,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":34510,"numValue":1.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34511,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:264 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 264 | train | mutant | 522 | 1 | 573 | 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 | P132A | P132A | 1 | 1 | 0 | 0 | 132 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 11,378 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P132A | null | null | 3.33 | 0.91 | 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":39186,"numValue":3.33,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39187,"numValue":0.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39188,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39189,"numValue":null,"references":... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 265 | train | mutant | 522 | 1 | 573 | 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 | P132A | P132A | 1 | 1 | 0 | 0 | 132 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 11,379 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P132A | null | null | 3.85 | -0.14 | 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":39190,"numValue":3.85,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39191,"numValue":-0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39192,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39193,"numValue":null,"references"... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:266 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 266 | train | mutant | 523 | 1 | 574 | 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 | P132G | P132G | 1 | 1 | 0 | 0 | 132 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 851 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:P132G | 51.8 | -2.3 | null | null | 116.6 | 5.1 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | HotMuSiC_S1626.csv | 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_A:P132G","... | [{"datasets":["HotMuSiC_S1626.csv"],"id":3206,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3207,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3208,"numValue":116.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":3209,"numValue":5.1... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:267 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 267 | train | mutant | 523 | 1 | 574 | 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 | P132G | P132G | 1 | 1 | 0 | 0 | 132 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 7,312 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 54.1 | EDTA | 1 mM | 1WQ5_A:P132G | null | null | null | 0.78 | null | 5.1 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | 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":25523,"numValue":5.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25524,"numValue":0.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25525,"numValue":null,"references":[],"strValue":"yes","ty... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 268 | train | mutant | 523 | 1 | 574 | 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 | P132G | P132G | 1 | 1 | 0 | 0 | 132 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 8,864 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P132G | null | null | 3.6 | 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":30023,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30024,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30025,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":30026,"numValue":null,"references":[]... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 269 | train | mutant | 523 | 1 | 574 | 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 | P132G | P132G | 1 | 1 | 0 | 0 | 132 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 8,865 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P132G | null | null | 4.6 | -0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|STATE|REVERSIBILITY | SAAFEC_S1262.csv | 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":30027,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":30028,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30029,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":30030,"numValue":n... | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:270 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 270 | train | mutant | 523 | 1 | 574 | 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 | P132G | P132G | 1 | 1 | 0 | 0 | 132 | P | G | 9 | CONSERVATION | 1WQ5 | 282 | null | 132 | A | L | true | false | 65.841763 | 27.044286 | 11,354 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P132G | null | null | 8.2 | 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 | 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":39079,"numValue":8.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39080,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39081,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6311,"numValue":9.0,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:271 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 271 | train | mutant | 4,607 | 1 | 5,134 | 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 | F139W | F139W | 1 | 1 | 0 | 0 | 139 | F | W | 5 | CONSERVATION | 1WQ5 | 282 | null | 139 | A | H | true | false | 15.42025 | 21.885455 | 10,820 | ProTherm | 7.8 | Fluorescence | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:F139W | null | null | 5.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 721 | ARTICLE | Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. | 1,995 | 10.1074/jbc.270.47.28177 | 7499309 | J Biol Chem;270;28177-82 | 2 | Hardman J K|Choi S G | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM"... | [{"datasets":[],"id":37232,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37233,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":37234,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6318,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:272 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 272 | train | mutant | 4,607 | 1 | 5,134 | 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 | F139W | F139W | 1 | 1 | 0 | 0 | 139 | F | W | 5 | CONSERVATION | 1WQ5 | 282 | null | 139 | A | H | true | false | 15.42025 | 21.885455 | 10,821 | ProTherm | 7.8 | Fluorescence | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:F139W | null | null | 4.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 3.0 | DG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 721 | ARTICLE | Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. | 1,995 | 10.1074/jbc.270.47.28177 | 7499309 | J Biol Chem;270;28177-82 | 2 | Hardman J K|Choi S G | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM"... | [{"datasets":[],"id":37235,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37236,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":37237,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6318,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 273 | train | mutant | 4,607 | 1 | 5,134 | 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 | F139W | F139W | 1 | 1 | 0 | 0 | 139 | F | W | 5 | CONSERVATION | 1WQ5 | 282 | null | 139 | A | H | true | false | 15.42025 | 21.885455 | 12,570 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | 1WQ5_A:F139W | null | null | 5.7 | 0.7 | null | null | null | 2.46 | 2.3 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 804 | ARTICLE | Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. | 1,995 | 10.1074/jbc.270.30.17712 | 7629069 | J Biol Chem;270;17712-5 | 4 | Hardman J K|Choi S G|O'Donnell S E|Sarken K D | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":45608,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":45609,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45610,"numValue":2.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45611,"numValue":2.46,"... | [{"id":6318,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 274 | train | mutant | 4,607 | 1 | 5,134 | 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 | F139W | F139W | 1 | 1 | 0 | 0 | 139 | F | W | 5 | CONSERVATION | 1WQ5 | 282 | null | 139 | A | H | true | false | 15.42025 | 21.885455 | 12,571 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | 1WQ5_A:F139W | null | null | 4.6 | 0.6 | null | null | null | 3.8 | 1.2 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 804 | ARTICLE | Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. | 1,995 | 10.1074/jbc.270.30.17712 | 7629069 | J Biol Chem;270;17712-5 | 4 | Hardman J K|Choi S G|O'Donnell S E|Sarken K D | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":45614,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":45615,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45616,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45617,"numValue":3.8,"r... | [{"id":6318,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 275 | train | mutant | 7,170 | 1 | 7,825 | 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 | F139W|F258W | F139W|F258W | 2 | 2 | 0 | 0 | 139 | F | W | 5 | CONSERVATION | 1WQ5 | 282 | null | 139|258 | A | H | true | false | 22.73721 | 26.582273 | 15,469 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | 1WQ5_A:F139W 1WQ5_A:F258W | null | null | 5.6 | 0.8 | null | null | null | 2.67 | 2.1 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 804 | ARTICLE | Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. | 1,995 | 10.1074/jbc.270.30.17712 | 7629069 | J Biol Chem;270;17712-5 | 4 | Hardman J K|Choi S G|O'Donnell S E|Sarken K D | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":56808,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56809,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56810,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56811,"numValue":2.67,"references":[],"st... | [{"id":6318,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6437,"numValue":7.0,"position":258,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 276 | train | mutant | 7,170 | 1 | 7,825 | 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 | F139W|F258W | F139W|F258W | 2 | 2 | 0 | 0 | 139 | F | W | 5 | CONSERVATION | 1WQ5 | 282 | null | 139|258 | A | H | true | false | 22.73721 | 26.582273 | 15,470 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | 1WQ5_A:F139W 1WQ5_A:F258W | null | null | 4.4 | 0.8 | null | null | null | 3.51 | 1.3 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 804 | ARTICLE | Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. | 1,995 | 10.1074/jbc.270.30.17712 | 7629069 | J Biol Chem;270;17712-5 | 4 | Hardman J K|Choi S G|O'Donnell S E|Sarken K D | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":56814,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56815,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56816,"numValue":1.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56817,"numValue":3.51,"references":[],"st... | [{"id":6318,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6437,"numValue":7.0,"position":258,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:277 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 277 | train | mutant | 268 | 1 | 299 | 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 | C154S | C154S | 1 | 1 | 0 | 0 | 154 | C | S | 7 | CONSERVATION | 1WQ5 | 282 | null | 154 | A | E | false | false | 0 | 20.763333 | 474 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C154S | 45.3 | -8.2 | null | null | 46.41 | 3.52 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C154S","... | [{"datasets":[],"id":1901,"numValue":45.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1902,"numValue":-8.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1903,"numValue":46.41,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1904,"numValue":3.52,"references":[],"s... | [{"id":6333,"numValue":7.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:278 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 278 | train | mutant | 269 | 1 | 300 | 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 | C154A | C154A | 1 | 1 | 0 | 0 | 154 | C | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 154 | A | E | false | false | 0 | 20.763333 | 475 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C154A | 50.6 | -2.9 | null | null | 72.97 | 4.11 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C154A","... | [{"datasets":[],"id":1906,"numValue":50.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1907,"numValue":-2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1908,"numValue":72.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1909,"numValue":4.11,"references":[],"s... | [{"id":6333,"numValue":7.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 279 | train | mutant | 269 | 1 | 300 | 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 | C154A | C154A | 1 | 1 | 0 | 0 | 154 | C | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 154 | A | E | false | false | 0 | 20.763333 | 7,668 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 50 | 1WQ5_A:C154A | null | null | 0.14 | 1.03 | null | 4.11 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":50.0,"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":26403,"numValue":4.11,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26404,"numValue":0.14,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26405,"numValue":1.03,"references":[],"strValue":null,"typ... | [{"id":6333,"numValue":7.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:280 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 280 | train | mutant | 270 | 1 | 301 | 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 | C154V | C154V | 1 | 1 | 0 | 0 | 154 | C | V | 7 | CONSERVATION | 1WQ5 | 282 | null | 154 | A | E | false | false | 0 | 20.763333 | 476 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:C154V | 50.2 | -3.3 | null | null | 71.53 | 4.21 | 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 | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"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_A:C154V","... | [{"datasets":[],"id":1911,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1912,"numValue":-3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1913,"numValue":71.53,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1914,"numValue":4.21,"references":[],"s... | [{"id":6333,"numValue":7.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 281 | train | mutant | 270 | 1 | 301 | 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 | C154V | C154V | 1 | 1 | 0 | 0 | 154 | C | V | 7 | CONSERVATION | 1WQ5 | 282 | null | 154 | A | E | false | false | 0 | 20.763333 | 7,669 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 50 | 1WQ5_A:C154V | null | null | 0.05 | 1.12 | null | 4.21 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 50 | ARTICLE | Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 1. Role in conformational stability. | 1,996 | 10.1093/protein/9.5.425 | 8795042 | Protein Eng;9;425-31 | 2 | Yutani K|Hiraga K | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":50.0,"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":26407,"numValue":4.21,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":26408,"numValue":0.05,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26409,"numValue":1.12,"references":[],"strValue":null,"typ... | [{"id":6333,"numValue":7.0,"position":154,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 282 | train | mutant | 4,563 | 1 | 5,083 | 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 | Y175C | Y175C | 1 | 1 | 0 | 0 | 175 | Y | C | 9 | CONSERVATION | 1WQ5 | 282 | null | 175 | A | E | true | true | 29.456457 | 23.250833 | 10,732 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:Y175C | null | null | null | 0.1 | null | null | null | 2.58 | 3 | null | null | null | null | null | null | null | Unknown | 3.0 | DDG|M|CM|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 702 | ARTICLE | Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. | 1,986 | 10.1021/bi00369a002 | 3539187 | Biochemistry;25;6356-60 | 3 | Matthews C R|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":36894,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36895,"numValue":3.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36896,"numValue":2.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":36897,"nu... | [{"id":6354,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 283 | train | mutant | 4,563 | 1 | 5,083 | 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 | Y175C | Y175C | 1 | 1 | 0 | 0 | 175 | Y | C | 9 | CONSERVATION | 1WQ5 | 282 | null | 175 | A | E | true | true | 29.456457 | 23.250833 | 10,733 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:Y175C | null | null | null | 0.5 | null | null | null | 3.71 | 1.1 | null | null | null | null | null | null | null | Unknown | 3.0 | DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 702 | ARTICLE | Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. | 1,986 | 10.1021/bi00369a002 | 3539187 | Biochemistry;25;6356-60 | 3 | Matthews C R|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":36899,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36900,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36901,"numValue":3.71,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":36902,"numValue":3.0,"references":[],"st... | [{"id":6354,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 284 | train | mutant | 7,103 | 1 | 7,756 | 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 | Y175C|G211E | Y175C|G211E | 2 | 2 | 0 | 0 | 175 | Y | C | 9 | CONSERVATION | 1WQ5 | 282 | null | 175|211 | A | E | true | true | 14.8626 | 20.730417 | 15,317 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:Y175C 1WQ5_A:G211E | null | null | null | 1.3 | null | null | null | 2.2 | 3 | null | null | null | null | null | null | null | Unknown | 3.0 | DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 702 | ARTICLE | Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. | 1,986 | 10.1021/bi00369a002 | 3539187 | Biochemistry;25;6356-60 | 3 | Matthews C R|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":56213,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56214,"numValue":3.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56215,"numValue":2.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56216,"numValue":3.0,"references":[],"str... | [{"id":6354,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 285 | train | mutant | 7,103 | 1 | 7,756 | 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 | Y175C|G211E | Y175C|G211E | 2 | 2 | 0 | 0 | 175 | Y | C | 9 | CONSERVATION | 1WQ5 | 282 | null | 175|211 | A | E | true | true | 14.8626 | 20.730417 | 15,318 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:Y175C 1WQ5_A:G211E | null | null | null | 1 | null | null | null | 3.49 | 1.4 | null | null | null | null | null | null | null | Unknown | 3.0 | DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 702 | ARTICLE | Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. | 1,986 | 10.1021/bi00369a002 | 3539187 | Biochemistry;25;6356-60 | 3 | Matthews C R|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":56218,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56219,"numValue":1.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56220,"numValue":3.49,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56221,"numValue":3.0,"references":[],"st... | [{"id":6354,"numValue":9.0,"position":175,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 286 | train | mutant | 4,223 | 1 | 4,728 | 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 | L176A | L176A | 1 | 1 | 0 | 0 | 176 | L | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 176 | A | E | true | false | 0.537484 | 25.3525 | 9,654 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L176A | null | null | 3.25 | 2.88 | null | null | null | null | 2.16 | 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":33139,"numValue":3.25,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33140,"numValue":2.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33141,"numValue":2.16,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33142,"numValue":3.0,"references":[],"... | [{"id":6355,"numValue":7.0,"position":176,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 287 | train | mutant | 4,223 | 1 | 4,728 | 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 | L176A | L176A | 1 | 1 | 0 | 0 | 176 | L | A | 7 | CONSERVATION | 1WQ5 | 282 | null | 176 | A | E | true | false | 0.537484 | 25.3525 | 9,659 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:L176A | null | null | 3.59 | 1.13 | null | null | null | null | 1.01 | 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":33164,"numValue":3.59,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33165,"numValue":1.13,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33166,"numValue":1.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33167,"numValue":3.0,"references":[],"... | [{"id":6355,"numValue":7.0,"position":176,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 288 | train | mutant | 525 | 1 | 576 | 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 | P207A | P207A | 1 | 1 | 0 | 0 | 207 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 207 | A | L | true | false | 48.37354 | 23.285714 | 853 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 1WQ5_A:P207A | 47.4 | -6.7 | null | null | 95 | 4.9 | 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_A:P207A","... | [{"datasets":[],"id":3216,"numValue":47.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3217,"numValue":-6.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3218,"numValue":95.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":3219,"numValue":4.9,"references":[],"str... | [{"id":6386,"numValue":9.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 290 | train | mutant | 525 | 1 | 576 | 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 | P207A | P207A | 1 | 1 | 0 | 0 | 207 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 207 | A | L | true | false | 48.37354 | 23.285714 | 8,866 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P207A | null | null | 2.4 | 2.2 | 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":30031,"numValue":2.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":30032,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":30033,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":30034,"numValue":null,"references":[]... | [{"id":6386,"numValue":9.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 293 | train | mutant | 525 | 1 | 576 | 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 | P207A | P207A | 1 | 1 | 0 | 0 | 207 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 207 | A | L | true | false | 48.37354 | 23.285714 | 11,355 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | 1WQ5_A:P207A | null | null | 7 | 1.8 | 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":39082,"numValue":7.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39083,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39084,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6386,"numValue":9.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 294 | train | mutant | 525 | 1 | 576 | 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 | P207A | P207A | 1 | 1 | 0 | 0 | 207 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 207 | A | L | true | false | 48.37354 | 23.285714 | 11,380 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P207A | null | null | 2.44 | 1.79 | 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":39194,"numValue":2.44,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39195,"numValue":1.79,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39196,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39197,"numValue":null,"references":... | [{"id":6386,"numValue":9.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:295 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 295 | train | mutant | 525 | 1 | 576 | 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 | P207A | P207A | 1 | 1 | 0 | 0 | 207 | P | A | 9 | CONSERVATION | 1WQ5 | 282 | null | 207 | A | L | true | false | 48.37354 | 23.285714 | 11,381 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 1WQ5_A:P207A | null | null | 4.62 | -0.62 | 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":39198,"numValue":4.62,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39199,"numValue":-0.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39200,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39201,"numValue":null,"references"... | [{"id":6386,"numValue":9.0,"position":207,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 296 | train | mutant | 2,181 | 1 | 2,477 | 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 | G211R | G211R | 1 | 1 | 0 | 0 | 211 | G | R | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 4,281 | ProTherm | 7.8 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:G211R | 58 | 0.2 | null | null | 111 | 2.8 | 113 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 410 | ARTICLE | Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase. | 1,980 | 10.1021/bi00548a004 | 6992862 | Biochemistry;19;1290-3 | 5 | Velicelebi G|Sturtevant J M|Matthews C R|Crisanti M M|Gepner G L | [{"numValue":7.8,"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:G211R","ty... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":15850,"numValue":58.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":15851,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":15852,"numValue":111.0,... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 297 | train | mutant | 2,181 | 1 | 2,477 | 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 | G211R | G211R | 1 | 1 | 0 | 0 | 211 | G | R | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 7,159 | ProTherm | 7.8 | DSC | Thermal | Sodium phosphate | 1 mM | 57.8 | EDTA | 0.2 mM | 1WQ5_A:G211R | null | null | null | -0.1 | null | 2.8 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 410 | ARTICLE | Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase. | 1,980 | 10.1021/bi00548a004 | 6992862 | Biochemistry;19;1290-3 | 5 | Velicelebi G|Sturtevant J M|Matthews C R|Crisanti M M|Gepner G L | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":57.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"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":"B... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":25074,"numValue":2.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25075,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.c... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 298 | train | mutant | 2,181 | 1 | 2,477 | 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 | G211R | G211R | 1 | 1 | 0 | 0 | 211 | G | R | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 14,308 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 4 | 1WQ5_A:G211R | null | null | 2.2 | 2.8 | null | null | null | 1.4 | 1.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":4.0,"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":"BU... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":52952,"numValue":2.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":52953,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":52954,"numValue":1.6,"re... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 299 | train | mutant | 2,181 | 1 | 2,477 | 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 | G211R | G211R | 1 | 1 | 0 | 0 | 211 | G | R | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 14,309 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 4 | 1WQ5_A:G211R | null | null | 7.3 | -1.3 | null | null | null | 3.28 | 2.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":4.0,"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":"BU... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":52957,"numValue":7.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":52958,"numValue":-1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":52959,"numValue":2.2,"r... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 300 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 4,282 | ProTherm | 7.8 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:G211E | 59.6 | 1.8 | null | null | 109 | 2.7 | 107 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 410 | ARTICLE | Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase. | 1,980 | 10.1021/bi00548a004 | 6992862 | Biochemistry;19;1290-3 | 5 | Velicelebi G|Sturtevant J M|Matthews C R|Crisanti M M|Gepner G L | [{"numValue":7.8,"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:G211E","ty... | [{"datasets":[],"id":15856,"numValue":59.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15857,"numValue":1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15858,"numValue":109.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15859,"numValue":2.7,"references":[],... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:301 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 301 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 7,160 | ProTherm | 7.8 | DSC | Thermal | Sodium phosphate | 1 mM | 57.8 | EDTA | 0.2 mM | 1WQ5_A:G211E | null | null | null | -0.6 | null | 2.7 | 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 | 410 | ARTICLE | Effect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase. | 1,980 | 10.1021/bi00548a004 | 6992862 | Biochemistry;19;1290-3 | 5 | Velicelebi G|Sturtevant J M|Matthews C R|Crisanti M M|Gepner G L | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":57.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"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":"B... | [{"datasets":[],"id":25077,"numValue":2.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25078,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25079,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 302 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,459 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211E | null | null | 8.1 | -2.4 | null | null | null | 2.73 | 3 | 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":35848,"numValue":8.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35849,"numValue":-2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35850,"numValue":3.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35851,"numValue":2.73,"references":[],"s... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 303 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,460 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211E | null | null | 5.4 | -0.4 | null | null | null | 3.72 | 1.5 | 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":35854,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35855,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35856,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35857,"numValue":3.72,"references":[],"s... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 304 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,715 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211E | null | null | 8.1 | -2.4 | null | null | null | 2.73 | 3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36809,"numValue":8.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36810,"numValue":-2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36811,"numValue":3.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36812,"numValue":2.73,"references":[],"s... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 305 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,716 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211E | null | null | 5.5 | -0.5 | null | null | null | 3.72 | 1.5 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36814,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36815,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36816,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36817,"numValue":3.72,"references":[],"s... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 306 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,734 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211E | null | null | null | -0.3 | null | null | null | 2.73 | 3 | null | null | null | null | null | null | null | Unknown | 3.0 | DDG|M|CM|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 702 | ARTICLE | Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. | 1,986 | 10.1021/bi00369a002 | 3539187 | Biochemistry;25;6356-60 | 3 | Matthews C R|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":36904,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36905,"numValue":3.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36906,"numValue":2.73,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":36907,"n... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 307 | train | mutant | 2,182 | 1 | 2,478 | 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 | G211E | G211E | 1 | 1 | 0 | 0 | 211 | G | E | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,735 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211E | null | null | null | 0.7 | null | null | null | 3.72 | 1.5 | null | null | null | null | null | null | null | Unknown | 3.0 | DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 702 | ARTICLE | Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase. | 1,986 | 10.1021/bi00369a002 | 3539187 | Biochemistry;25;6356-60 | 3 | Matthews C R|Hurle M R|Tweedy N B | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":36909,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36910,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36911,"numValue":3.72,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":36912,"numValue":3.0,"references":[],"st... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:308 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 308 | train | mutant | 4,559 | 1 | 5,079 | 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 | G211D | G211D | 1 | 1 | 0 | 0 | 211 | G | D | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,717 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211D | null | null | 5.4 | 0.3 | null | null | null | 2.7 | 2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36819,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":36820,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36821,"numValue":2.0,"references":[],"strValue":null,"type":... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 309 | train | mutant | 4,559 | 1 | 5,079 | 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 | G211D | G211D | 1 | 1 | 0 | 0 | 211 | G | D | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,718 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211D | null | null | 4.2 | 0.8 | null | null | null | 3.61 | 1.2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36824,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36825,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36826,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36827,"numValue":3.61,"references":[],"st... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 310 | train | mutant | 4,560 | 1 | 5,080 | 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 | G211S | G211S | 1 | 1 | 0 | 0 | 211 | G | S | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,719 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211S | null | null | 5.9 | -0.2 | null | null | null | 2.46 | 2.4 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36829,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":36830,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36831,"numValue":2.4,"references":[],"strValue":null,"type":"M"},{"datasets... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 311 | train | mutant | 4,560 | 1 | 5,080 | 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 | G211S | G211S | 1 | 1 | 0 | 0 | 211 | G | S | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,720 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211S | null | null | 5.2 | -0.2 | null | null | null | 3.97 | 1.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | khan_protherm_data_mapped.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36834,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","SAAFEC_S1262.csv"],"id":36835,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36836,"numValue":1.3,"references":[],"strValue":null,"type":"M"},{"datasets... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 312 | train | mutant | 4,561 | 1 | 5,081 | 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 | G211V | G211V | 1 | 1 | 0 | 0 | 211 | G | V | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,721 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211V | null | null | 5.4 | 0.3 | null | null | null | 2.78 | 1.9 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36839,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":36840,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36841,"numValue":1.9,"references":[],"strValue":null,"type":... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 313 | train | mutant | 4,561 | 1 | 5,081 | 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 | G211V | G211V | 1 | 1 | 0 | 0 | 211 | G | V | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,722 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211V | null | null | 6.9 | -1.9 | null | null | null | 4.3 | 1.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36844,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36845,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36846,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36847,"numValue":4.3,"references":[],"st... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:314 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 314 | train | mutant | 4,562 | 1 | 5,082 | 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 | G211W | G211W | 1 | 1 | 0 | 0 | 211 | G | W | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,723 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211W | null | null | 4.1 | 1.6 | null | null | null | 2.25 | 1.8 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36849,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36850,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36851,"numValue":1.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36852,"numValue":2.25,"references":[],"st... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 315 | train | mutant | 4,562 | 1 | 5,082 | 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 | G211W | G211W | 1 | 1 | 0 | 0 | 211 | G | W | 9 | CONSERVATION | 1WQ5 | 282 | null | 211 | A | E | true | true | 0.268742 | 18.21 | 10,724 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G211W | null | null | 3.9 | 1.1 | null | null | null | 3.62 | 1.1 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 699 | ARTICLE | Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction. | 1,990 | 10.1021/bi00458a027 | 2185841 | Biochemistry;29;1539-45 | 4 | Matthews C R|Chrunyk B A|Hurle M R|Tweedy N B | [{"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":36854,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36855,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36856,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36857,"numValue":3.62,"references":[],"st... | [{"id":6390,"numValue":9.0,"position":211,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:316 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 316 | train | mutant | 4,408 | 1 | 4,925 | 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 | G234D | G234D | 1 | 1 | 0 | 0 | 234 | G | D | 9 | CONSERVATION | 1WQ5 | 282 | null | 234 | A | L | true | true | 18.720076 | 25.9075 | 10,461 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G234D | null | null | 7.1 | -1.4 | null | null | null | 2.78 | 2.6 | 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":35860,"numValue":7.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35861,"numValue":-1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35862,"numValue":2.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35863,"numValue":2.78,"references":[],"s... | [{"id":6413,"numValue":9.0,"position":234,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 317 | train | mutant | 4,408 | 1 | 4,925 | 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 | G234D | G234D | 1 | 1 | 0 | 0 | 234 | G | D | 9 | CONSERVATION | 1WQ5 | 282 | null | 234 | A | L | true | true | 18.720076 | 25.9075 | 10,462 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G234D | null | null | 7 | -2 | null | null | null | 3.99 | 1.8 | 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":35866,"numValue":7.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35867,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35868,"numValue":1.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35869,"numValue":3.99,"references":[],"s... | [{"id":6413,"numValue":9.0,"position":234,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 318 | train | mutant | 4,409 | 1 | 4,926 | 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 | G234K | G234K | 1 | 1 | 0 | 0 | 234 | G | K | 9 | CONSERVATION | 1WQ5 | 282 | null | 234 | A | L | true | true | 18.720076 | 25.9075 | 10,463 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G234K | null | null | 6.2 | -0.5 | null | null | null | 2.65 | 2.3 | 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":35872,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35873,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35874,"numValue":2.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35875,"numValue":2.65,"references":[],"s... | [{"id":6413,"numValue":9.0,"position":234,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 319 | train | mutant | 4,409 | 1 | 4,926 | 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 | G234K | G234K | 1 | 1 | 0 | 0 | 234 | G | K | 9 | CONSERVATION | 1WQ5 | 282 | null | 234 | A | L | true | true | 18.720076 | 25.9075 | 10,464 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:G234K | null | null | 4.7 | 0.3 | null | null | null | 3.81 | 1.2 | 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":35878,"numValue":4.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35879,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35880,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35881,"numValue":3.81,"references":[],"st... | [{"id":6413,"numValue":9.0,"position":234,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 320 | train | mutant | 6,583 | 1 | 7,223 | 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 | H244A | H244A | 1 | 1 | 0 | 0 | 244 | H | A | 4 | CONSERVATION | 1WQ5 | 282 | null | 244 | A | T | false | false | 36.208784 | 38.202001 | 14,189 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 5 | 1WQ5_A:H244A | null | null | 4 | null | null | null | null | 4.8 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 717 | ARTICLE | Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase. | 1,996 | 10.1021/bi951726o | 8639683 | Biochemistry;35;1988-94 | 3 | Matthews C R|Saab-Rinc?n G|Gualfetti P J | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":5.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"B... | [{"datasets":[],"id":52541,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52542,"numValue":4.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":52543,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6423,"numValue":4.0,"position":244,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 321 | train | mutant | 4,608 | 1 | 5,135 | 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 | F258W | F258W | 1 | 1 | 0 | 0 | 258 | F | W | 7 | CONSERVATION | 1WQ5 | 282 | null | 258 | A | H | false | false | 30.054169 | 31.279091 | 10,822 | ProTherm | 7.8 | Fluorescence | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:F258W | null | null | 7 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 721 | ARTICLE | Unfolding properties of tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. | 1,995 | 10.1074/jbc.270.47.28177 | 7499309 | J Biol Chem;270;28177-82 | 2 | Hardman J K|Choi S G | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM"... | [{"datasets":[],"id":37238,"numValue":7.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37239,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6437,"numValue":7.0,"position":258,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:322 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 322 | train | mutant | 4,608 | 1 | 5,135 | 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 | F258W | F258W | 1 | 1 | 0 | 0 | 258 | F | W | 7 | CONSERVATION | 1WQ5 | 282 | null | 258 | A | H | false | false | 30.054169 | 31.279091 | 12,572 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | 1WQ5_A:F258W | null | null | 5 | 1.4 | null | null | null | 2.68 | 1.9 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 804 | ARTICLE | Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. | 1,995 | 10.1074/jbc.270.30.17712 | 7629069 | J Biol Chem;270;17712-5 | 4 | Hardman J K|Choi S G|O'Donnell S E|Sarken K D | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":45620,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45621,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45622,"numValue":1.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45623,"numValue":2.68,"references":[],"st... | [{"id":6437,"numValue":7.0,"position":258,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 323 | train | mutant | 4,608 | 1 | 5,135 | 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 | F258W | F258W | 1 | 1 | 0 | 0 | 258 | F | W | 7 | CONSERVATION | 1WQ5 | 282 | null | 258 | A | H | false | false | 30.054169 | 31.279091 | 12,573 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | 1WQ5_A:F258W | null | null | 4.2 | 1 | null | null | null | 3.58 | 1.2 | null | null | null | null | null | null | null | yes | 3.0 | DG|DDG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 804 | ARTICLE | Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. | 1,995 | 10.1074/jbc.270.30.17712 | 7629069 | J Biol Chem;270;17712-5 | 4 | Hardman J K|Choi S G|O'Donnell S E|Sarken K D | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":23.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Absorbance","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","... | [{"datasets":[],"id":45626,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45627,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45628,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":45629,"numValue":3.58,"references":[],"st... | [{"id":6437,"numValue":7.0,"position":258,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 324 | train | sequence | 30 | 30 | -1 | 130 | -1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,404 | ProTherm | 6 | DSC | Thermal | sodium acetate, calcium acetate | 20 mM, 2 mM | null | Mops | 50 mM | 57.2 | null | null | null | 96.56 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 3 | ARTICLE | X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1. | 1,994 | 10.1111/j.1432-1033.1994.tb18652.x | 8125111 | Eur J Biochem;220;527-34 | 4 | Schluckebier G|Backmann J|Granzin J|Schubert W D | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate, calcium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM, 2 mM","type":"BUFFER_CONC"},{"numValue":null,"strVal... | [{"datasets":[],"id":64249,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64250,"numValue":96.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64251,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 325 | train | sequence | 30 | 30 | -1 | 130 | -1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,482 | ProTherm | 4.4 | NMR | Thermal | Unknown | null | 52.3 | null | null | null | null | null | 126.67 | null | null | null | null | null | null | null | null | null | Unknown | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 1010 | ARTICLE | Thermal stabilization of ribonuclease T1 by carboxymethylation at Glu-58 as revealed by 1H nuclear magnetic resonance spectroscopy. | 1,994 | 10.1016/0014-5793(94)00890-6 | 7915996 | FEBS Lett;351;389-92 | 6 | Tanokura M|Kojima M|Mizukoshi T|Miyano H|Suzuki E|Takahashi K | [{"numValue":4.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"}] | [{"datasets":[],"id":64495,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64496,"numValue":126.67,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":64497,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 326 | train | sequence | 30 | 30 | -1 | 130 | -1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | 2 | Guanyl-specific ribonuclease T1 | Aspergillus oryzae (strain ATCC 42149 / RIB 40) | 1 | P00651 | IPR000026|IPR016191|IPR051386|IPR048269 | 4.6.1.24 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,516 | ProTherm | 7 | DSC | Thermal | PIPES | 30 mM | null | NaCl | 0 M | 48.91 | null | null | null | 95.5 | 1.35 | 118.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1018 | ARTICLE | Thermodynamics of ribonuclease T1 denaturation. | 1,992 | 10.1021/bi00135a019 | 1591247 | Biochemistry;31;4876-82 | 5 | Sturtevant J M|Hu C Q|Pace C N|Thomson J A|Erickson R E | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PIPES","type":"BUFFER"},{"numValue":null,"strValue":"30 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVa... | [{"datasets":[],"id":64604,"numValue":48.91,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64605,"numValue":95.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64606,"numValue":1.35,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64607,"numValue":118.4,"references":... |
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