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:0 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 0 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,395 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 59.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64221,"numValue":59.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64222,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:2 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,725 | ProTherm | 8.98 | DSC | Thermal | sodium tetraborate | 1 mM | null | 54.2 | null | null | null | 4.09 | null | 3.15 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1028 | ARTICLE | -1 | DOI: 10.1016/0040-6031(90)80386-D | 4 | Yutani K|Ogasahara K|Sugisaki Y|Miles EW | [{"numValue":8.98,"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"}] | [{"datasets":[],"id":65493,"numValue":54.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65494,"numValue":4.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65495,"numValue":3.15,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":65496,"numValue":null,"references":[... | ||||||||||||||||||||||||||||
fireprotdb:3 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,943 | ProTherm | 7 | CD | Thermal | tetra-borate | 1 mM | null | 61.2 | null | null | null | null | 2.45 | 19.7 | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66356,"numValue":61.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66357,"numValue":2.45,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66358,"numValue":19.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66359,"numValue":null,"references":... | ||||||||||||||||||||||||||
fireprotdb:4 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 4 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,944 | ProTherm | 9.3 | CD | Thermal | tetra-borate | 1 mM | null | 50.4 | null | null | null | null | 2.45 | 19.7 | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66360,"numValue":50.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66361,"numValue":2.45,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66362,"numValue":19.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":66363,"numValue":null,"references":... | ||||||||||||||||||||||||||
fireprotdb:5 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 5 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,945 | ProTherm | 7 | DSC | Thermal | tetra-borate | 1 mM | null | 62.4 | null | null | null | null | 2.87 | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66364,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66365,"numValue":2.87,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66366,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:6 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 6 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,946 | ProTherm | 9.3 | DSC | Thermal | tetra-borate | 1 mM | null | 54.3 | null | null | null | null | 2.87 | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66367,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66368,"numValue":2.87,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66369,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,002 | ProTherm | 7 | DSC | Thermal | potassium phosphate | 1 mM | null | 62.4 | null | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(<50%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66552,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66553,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66554,"numValue":null,"references":[],"strValue":"yes(<50%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,003 | ProTherm | 9.3 | DSC | Thermal | sodium tetraborate | 1 mM | null | 54.3 | null | null | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(>70%) | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":66555,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":66556,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":66557,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:12 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 12 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,927 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | null | 54.1 | null | null | null | 120.4 | 4.6 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":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"}] | [{"datasets":[],"id":73178,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":73179,"numValue":120.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":73180,"numValue":4.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73181,"numValue":null,"references":[]... | |||||||||||||||||||||||||
fireprotdb:13 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 13 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,154 | ProTherm | 9 | DSC | Thermal | Sodium tetraborate | 1 mM | 50 | null | null | 1.17 | null | null | 4.81 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":73855,"numValue":4.81,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":73856,"numValue":1.17,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73857,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:14 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 14 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,403 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25.8 | null | null | 8.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 586 | ARTICLE | Comparison of denaturation by guanidine hydrochloride of the wild type tryptophan synthase alpha-subunit of Escherichia coli and two mutant protein (Glu 49 replaced by Met or Gln). | 1,979 | 10.1093/oxfordjournals.jbchem.a132423 | 378988 | J Biochem;85;915-21 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":74626,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74627,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:15 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 15 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,408 | ProTherm | 9 | CD | GdnHCl | Tris-HCl | 0.025 M | 25 | null | null | 4.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.025 M","type":"BUFFER_C... | [{"datasets":[],"id":74644,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74645,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:16 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 16 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,409 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | null | null | 8.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":74646,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74647,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:17 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 17 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,410 | ProTherm | 5.5 | CD | GdnHCl | acetate | 0.05 M | 25 | null | null | 5.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 588 | ARTICLE | Effect of single amino acid substitutions at the same position on stability of a two-domain protein. | 1,982 | 10.1016/0022-2836(82)90184-x | 6757449 | J Mol Biol;160;387-90 | 4 | Yutani K|Ogasahara K|Sugino Y|Kimura A | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CON... | [{"datasets":[],"id":74648,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74649,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:18 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 18 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,512 | ProTherm | 7 | CD | Thermal | tetra-borate | 1 mM | 25 | null | null | 6.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER... | [{"datasets":[],"id":74962,"numValue":6.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74963,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:19 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 19 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,513 | ProTherm | 9.3 | CD | Thermal | tetra-borate | 1 mM | 25 | null | null | 3.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER... | [{"datasets":[],"id":74964,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74965,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:20 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 20 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,514 | ProTherm | 7 | DSC | Thermal | tetra-borate | 1 mM | 25 | null | null | 8.4 | null | 23.2 | null | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | DH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFE... | [{"datasets":[],"id":74966,"numValue":23.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":74967,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74968,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:21 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 21 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,515 | ProTherm | 9.3 | DSC | Thermal | tetra-borate | 1 mM | 25 | null | null | 5.8 | null | 23.2 | null | null | null | null | null | null | null | null | null | null | null | yes(70-95%) | DH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 37 | ARTICLE | Thermal denaturation of tryptophan synthase alpha-subunit. Comparison of the values of thermodynamic parameters of unfolding obtained from van't Hoff analysis of CD measurement with those from calorimetry. | 1,984 | 6384087 | Int J Pept Protein Res;24;147-54 | 4 | Yutani K|Ogasahara K|Suzuki M|Sugino Y | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"tetra-borate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFE... | [{"datasets":[],"id":74969,"numValue":23.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":74970,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74971,"numValue":null,"references":[],"strValue":"yes(70-95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:22 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 22 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,522 | ProTherm | 7 | DSC | Thermal | potassium phosphate | 1 mM | 25 | null | null | 8.4 | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(<50%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type"... | [{"datasets":[],"id":74986,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":74987,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74988,"numValue":null,"references":[],"strValue":"yes(<50%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:23 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 23 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,523 | ProTherm | 9.3 | DSC | Thermal | sodium tetraborate | 1 mM | 25 | null | null | 5.8 | null | null | 2.9 | null | null | null | null | null | null | null | null | null | null | yes(>70%) | DCP|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 48 | ARTICLE | Calorimetric study of tryptophan synthase alpha-subunit and two mutant proteins. | 1,982 | 10.1111/j.1399-3011.1982.tb00898.x | 6816746 | Int J Pept Protein Res;20;331-6 | 5 | Yutani K|Sugino Y|Khechinashvili N N|Lapshina E A|Privalov P L | [{"numValue":9.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium tetraborate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":... | [{"datasets":[],"id":74989,"numValue":2.9,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":74990,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":74991,"numValue":null,"references":[],"strValue":"yes(>70%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:24 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 24 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,593 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | null | null | 4.6 | 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 | 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":75226,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75227,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":75228,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:26 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 26 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,626 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.91 | null | null | null | null | null | 2.23 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1371 | ARTICLE | Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. | 1,999 | 10.1021/bi982365q | 9893998 | Biochemistry;38;1018-29 | 4 | Bilsel O|Matthews C R|Zitzewitz J A|Bowers K E | [{"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":75346,"numValue":5.91,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75347,"numValue":2.23,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75348,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:27 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 27 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,627 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 7.9 | null | null | null | null | null | 2.9 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1371 | ARTICLE | Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. | 1,999 | 10.1021/bi982365q | 9893998 | Biochemistry;38;1018-29 | 4 | Bilsel O|Matthews C R|Zitzewitz J A|Bowers K E | [{"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":75349,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75350,"numValue":2.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75351,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":75352,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:28 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 28 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,628 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.4 | null | null | null | null | null | 1.3 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1371 | ARTICLE | Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. | 1,999 | 10.1021/bi982365q | 9893998 | Biochemistry;38;1018-29 | 4 | Bilsel O|Matthews C R|Zitzewitz J A|Bowers K E | [{"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":75353,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75354,"numValue":1.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75355,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":75356,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:29 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 29 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,670 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | null | null | 8.21 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 666 | ARTICLE | Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit. | 1,997 | 10.1021/bi961660c | 9020793 | Biochemistry;36;932-40 | 2 | Yutani K|Ogasahara K | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":75483,"numValue":8.21,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75484,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:30 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 30 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,695 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.16 | null | null | null | null | 3.73 | 1.12 | null | null | null | null | null | null | null | Unknown | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1376 | ARTICLE | Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. | 1,999 | 10.1021/bi9909041 | 10433729 | Biochemistry;38;10205-14 | 2 | Matthews C R|Zitzewitz J A | [{"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":75573,"numValue":4.16,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75574,"numValue":1.12,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75575,"numValue":3.73,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75576,"numValue":2.0,"references":[],"s... | ||||||||||||||||||||||||
fireprotdb:31 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 31 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,696 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.08 | null | null | null | null | 3.67 | 1.11 | null | null | null | null | null | null | null | Unknown | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1376 | ARTICLE | Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. | 1,999 | 10.1021/bi9909041 | 10433729 | Biochemistry;38;10205-14 | 2 | Matthews C R|Zitzewitz J A | [{"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":75578,"numValue":4.08,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75579,"numValue":1.11,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75580,"numValue":3.67,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75581,"numValue":2.0,"references":[],"s... | ||||||||||||||||||||||||
fireprotdb:33 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 33 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,698 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 3.96 | null | null | null | null | 3.65 | 1.09 | null | null | null | null | null | null | null | Unknown | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1376 | ARTICLE | Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. | 1,999 | 10.1021/bi9909041 | 10433729 | Biochemistry;38;10205-14 | 2 | Matthews C R|Zitzewitz J A | [{"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":75588,"numValue":3.96,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75589,"numValue":1.09,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75590,"numValue":3.65,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75591,"numValue":2.0,"references":[],"s... | ||||||||||||||||||||||||
fireprotdb:35 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 35 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,700 | ProTherm | 7.8 | Fluorescence | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.14 | null | null | null | null | 3.81 | 1.09 | null | null | null | null | null | null | null | Unknown | 2.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1376 | ARTICLE | Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. | 1,999 | 10.1021/bi9909041 | 10433729 | Biochemistry;38;10205-14 | 2 | Matthews C R|Zitzewitz J A | [{"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":75598,"numValue":4.14,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75599,"numValue":1.09,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75600,"numValue":3.81,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75601,"numValue":2.0,"references":[],"s... | ||||||||||||||||||||||||
fireprotdb:36 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 36 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,707 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.7 | null | null | null | null | 2.62 | 2.2 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":75626,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75627,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75628,"numValue":2.62,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75629,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:37 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 37 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,708 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5 | null | null | null | null | 4.18 | 1.2 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":75631,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75632,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75633,"numValue":4.18,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75634,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:39 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 39 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,738 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5 | null | null | null | null | 4.18 | 1.2 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":75741,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75742,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75743,"numValue":4.18,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75744,"numValue":null,"references":[],"st... | |||||||||||||||||||||||||
fireprotdb:40 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 40 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,753 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | null | null | null | null | null | 2.62 | 2.2 | null | null | null | null | null | null | null | Unknown | 3.0 | M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":75787,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75788,"numValue":2.62,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75789,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":75790,"numValue":null,"references":[],... | ||||||||||||||||||||||||
fireprotdb:41 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 41 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,754 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | null | null | null | null | null | 4.18 | 1.2 | null | null | null | null | null | null | null | Unknown | 3.0 | M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":75791,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75792,"numValue":4.18,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75793,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":75794,"numValue":null,"references":[],... | ||||||||||||||||||||||||
fireprotdb:42 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 42 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,813 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.7 | null | null | null | null | 2.62 | 2.18 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75957,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75958,"numValue":2.18,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75959,"numValue":2.62,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75960,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:44 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 44 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,815 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 6.1 | null | null | null | null | 2.76 | 2.19 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75967,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75968,"numValue":2.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75969,"numValue":2.76,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75970,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:45 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 45 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,816 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 6.2 | null | null | null | null | 3.93 | 1.56 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75972,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75973,"numValue":1.56,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75974,"numValue":3.93,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75975,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:46 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 46 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,817 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.4 | null | null | null | null | 1.98 | 2.73 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75977,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75978,"numValue":2.73,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75979,"numValue":1.98,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75980,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:47 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 47 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,818 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.8 | null | null | null | null | 3.4 | 1.4 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75982,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75983,"numValue":1.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75984,"numValue":3.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75985,"numValue":3.0,"references":[],"strV... | ||||||||||||||||||||||||
fireprotdb:48 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 48 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,819 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.4 | null | null | null | null | 2.17 | 2.49 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75987,"numValue":5.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75988,"numValue":2.49,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75989,"numValue":2.17,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75990,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:49 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 49 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,820 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 6.2 | null | null | null | null | 3.37 | 1.84 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75992,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75993,"numValue":1.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75994,"numValue":3.37,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":75995,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:50 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 50 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,821 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 6.4 | null | null | null | null | 1.95 | 3.28 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":75997,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":75998,"numValue":3.28,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":75999,"numValue":1.95,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76000,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:51 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 51 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,822 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4 | null | null | null | null | 3.01 | 1.34 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":76002,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76003,"numValue":1.34,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76004,"numValue":3.01,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76005,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:52 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 52 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,823 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5 | null | null | null | null | 2.01 | 2.5 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":76007,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76008,"numValue":2.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76009,"numValue":2.01,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76010,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:53 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 53 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,824 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 6.3 | null | null | null | null | 3.54 | 1.78 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":76012,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76013,"numValue":1.78,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76014,"numValue":3.54,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76015,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:54 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 54 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,825 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 3.9 | null | null | null | null | 1.92 | 2.02 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":76017,"numValue":3.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76018,"numValue":2.02,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76019,"numValue":1.92,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76020,"numValue":3.0,"references":[],"st... | ||||||||||||||||||||||||
fireprotdb:55 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 55 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,826 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 25 | null | null | 3.7 | null | null | null | null | 3.33 | 1.1 | null | null | null | null | null | null | null | yes (>90%) | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1393 | ARTICLE | Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids. | 1,988 | 10.1021/bi00402a050 | 3280027 | Biochemistry;27;824-32 | 5 | Ahmed S A|Miles E W|Matthews C R|Onuffer J J|Stackhouse T M | [{"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":76022,"numValue":3.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76023,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76024,"numValue":3.33,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76025,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:56 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 56 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,851 | ProTherm | 7.8 | Absorbance | Urea | phosphate | 58 mM | 25 | null | null | 6.8 | null | null | null | null | 2.5 | 2.8 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1403 | ARTICLE | Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. | 1,993 | 10.1021/bi00213a031 | 8268176 | Biochemistry;32;13981-90 | 3 | Matthews C R|Saab-Rinc?n G|Froebe C L | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"BUF... | [{"datasets":[],"id":76105,"numValue":6.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76106,"numValue":2.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76107,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76108,"numValue":3.0,"references":[],"strV... | ||||||||||||||||||||||||
fireprotdb:57 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 57 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,852 | ProTherm | 7.8 | Absorbance | Urea | phosphate | 58 mM | 25 | null | null | 5.1 | null | null | null | null | 3.9 | 1.3 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1403 | ARTICLE | Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. | 1,993 | 10.1021/bi00213a031 | 8268176 | Biochemistry;32;13981-90 | 3 | Matthews C R|Saab-Rinc?n G|Froebe C L | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"BUF... | [{"datasets":[],"id":76110,"numValue":5.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76111,"numValue":1.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76112,"numValue":3.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76113,"numValue":3.0,"references":[],"strV... | ||||||||||||||||||||||||
fireprotdb:58 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 58 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,853 | ProTherm | 7.8 | CD | Urea | phosphate | 58 mM | 25 | null | null | 6.2 | null | null | null | null | 2.5 | 2.5 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1403 | ARTICLE | Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. | 1,993 | 10.1021/bi00213a031 | 8268176 | Biochemistry;32;13981-90 | 3 | Matthews C R|Saab-Rinc?n G|Froebe C L | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":76115,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76116,"numValue":2.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76117,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76118,"numValue":3.0,"references":[],"strV... | ||||||||||||||||||||||||
fireprotdb:59 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 59 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,854 | ProTherm | 7.8 | CD | Urea | phosphate | 58 mM | 25 | null | null | 4.6 | null | null | null | null | 4 | 1.2 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1403 | ARTICLE | Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration. | 1,993 | 10.1021/bi00213a031 | 8268176 | Biochemistry;32;13981-90 | 3 | Matthews C R|Saab-Rinc?n G|Froebe C L | [{"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":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"58 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":76120,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76121,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76122,"numValue":4.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76123,"numValue":3.0,"references":[],"strV... | ||||||||||||||||||||||||
fireprotdb:60 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 60 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,878 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | null | null | 8.2 | null | null | null | null | 5.9 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":76216,"numValue":8.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76217,"numValue":5.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76218,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:61 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 61 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,988 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 6 | null | null | null | null | null | 2.2 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1432 | ARTICLE | Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. | 1,999 | 10.1021/bi991296s | 10529212 | Biochemistry;38;13367-78 | 6 | Iwakura M|Bilsel O|Kihara H|Gualfetti P J|Zitzewitz J A|Lee J C | [{"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":76568,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76569,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76570,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76571,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:62 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 62 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,989 | ProTherm | 7.8 | SEC | Urea | Potassium phosphate | 100 mM | 25 | null | null | 5.7 | null | null | null | null | null | 2 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1432 | ARTICLE | Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. | 1,999 | 10.1021/bi991296s | 10529212 | Biochemistry;38;13367-78 | 6 | Iwakura M|Bilsel O|Kihara H|Gualfetti P J|Zitzewitz J A|Lee J C | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SEC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":... | [{"datasets":[],"id":76572,"numValue":5.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76573,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76574,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76575,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:63 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 63 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,990 | ProTherm | 7.8 | SAXS | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.3 | null | null | null | null | null | 2 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1432 | ARTICLE | Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. | 1,999 | 10.1021/bi991296s | 10529212 | Biochemistry;38;13367-78 | 6 | Iwakura M|Bilsel O|Kihara H|Gualfetti P J|Zitzewitz J A|Lee J C | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SAXS","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":76576,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76577,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76578,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76579,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:64 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 64 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,991 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.5 | null | null | null | null | null | 1.1 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1432 | ARTICLE | Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. | 1,999 | 10.1021/bi991296s | 10529212 | Biochemistry;38;13367-78 | 6 | Iwakura M|Bilsel O|Kihara H|Gualfetti P J|Zitzewitz J A|Lee J C | [{"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":76580,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76581,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76582,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76583,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:65 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 65 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,992 | ProTherm | 7.8 | SEC | Urea | Potassium phosphate | 100 mM | 25 | null | null | 4.9 | null | null | null | null | null | 1.2 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1432 | ARTICLE | Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. | 1,999 | 10.1021/bi991296s | 10529212 | Biochemistry;38;13367-78 | 6 | Iwakura M|Bilsel O|Kihara H|Gualfetti P J|Zitzewitz J A|Lee J C | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SEC","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":... | [{"datasets":[],"id":76584,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76585,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76586,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76587,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:66 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 66 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,993 | ProTherm | 7.8 | SAXS | Urea | Potassium phosphate | 10 mM | 25 | null | null | 3.1 | null | null | null | null | null | 0.9 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1432 | ARTICLE | Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. | 1,999 | 10.1021/bi991296s | 10529212 | Biochemistry;38;13367-78 | 6 | Iwakura M|Bilsel O|Kihara H|Gualfetti P J|Zitzewitz J A|Lee J C | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"SAXS","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":76588,"numValue":3.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76589,"numValue":0.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76590,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76591,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:67 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 67 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,994 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.9 | null | null | null | null | null | 0.84 | null | null | null | null | null | null | null | Unknown | 4.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1432 | ARTICLE | Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. | 1,999 | 10.1021/bi991296s | 10529212 | Biochemistry;38;13367-78 | 6 | Iwakura M|Bilsel O|Kihara H|Gualfetti P J|Zitzewitz J A|Lee J C | [{"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":76592,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76593,"numValue":0.84,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76594,"numValue":4.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76595,"numValue":null,"references":[],... | ||||||||||||||||||||||||
fireprotdb:69 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 69 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,084 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 3.71 | null | null | null | null | 3.71 | 1 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76813,"numValue":3.71,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76814,"numValue":1.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76815,"numValue":3.71,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76816,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:70 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 70 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,085 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 3.6 | null | null | null | null | 3.72 | 0.97 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76817,"numValue":3.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76818,"numValue":0.97,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76819,"numValue":3.72,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76820,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:71 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 71 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,086 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.05 | null | null | null | null | 3.73 | 1.09 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76821,"numValue":4.05,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76822,"numValue":1.09,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76823,"numValue":3.73,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76824,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:73 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 73 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,088 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 2.41 | null | null | null | null | 2.8 | 0.86 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76829,"numValue":2.41,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76830,"numValue":0.86,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76831,"numValue":2.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76832,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:74 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 74 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,089 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 2.31 | null | null | null | null | 2.7 | 0.85 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76833,"numValue":2.31,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76834,"numValue":0.85,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76835,"numValue":2.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76836,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:75 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 75 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,090 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 5.27 | null | null | null | null | 2.62 | 2.01 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76837,"numValue":5.27,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76838,"numValue":2.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76839,"numValue":2.62,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76840,"numValue":null,"references":[],"... | |||||||||||||||||||||||||
fireprotdb:76 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 76 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,091 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.8 | null | null | null | null | 3.93 | 1.22 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76841,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76842,"numValue":1.22,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76843,"numValue":3.93,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76844,"numValue":null,"references":[],"s... | |||||||||||||||||||||||||
fireprotdb:77 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 77 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,092 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | null | null | 7.7 | null | null | null | null | 5.9 | 1.3 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76845,"numValue":7.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76846,"numValue":1.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76847,"numValue":5.9,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76848,"numValue":null,"references":[],"str... | |||||||||||||||||||||||||
fireprotdb:78 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 78 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,093 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | null | null | 4.3 | null | null | null | null | 6.1 | 0.7 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76849,"numValue":4.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76850,"numValue":0.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76851,"numValue":6.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76852,"numValue":null,"references":[],"str... | |||||||||||||||||||||||||
fireprotdb:79 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 79 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,094 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | null | null | 4.8 | null | null | null | null | 5.2 | 0.9 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76853,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76854,"numValue":0.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76855,"numValue":5.2,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76856,"numValue":null,"references":[],"str... | |||||||||||||||||||||||||
fireprotdb:80 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 80 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,095 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | null | null | 4.2 | null | null | null | null | 5.1 | 0.8 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76857,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76858,"numValue":0.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76859,"numValue":5.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76860,"numValue":null,"references":[],"str... | |||||||||||||||||||||||||
fireprotdb:81 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 81 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,096 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 25 | null | null | 4.2 | null | null | null | null | 5.4 | 0.8 | null | null | null | null | null | null | null | yes(>90%) | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1440 | ARTICLE | Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. | 1,999 | 10.1110/ps.8.6.1200 | 10386870 | Protein Sci;8;1200-9 | 5 | Matthews C R|Gualfetti P J|Zitzewitz J A|Perkons I A|Wasta S A | [{"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":76861,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76862,"numValue":0.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76863,"numValue":5.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":76864,"numValue":null,"references":[],"str... | |||||||||||||||||||||||||
fireprotdb:84 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 84 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,099 | ProTherm | 7.8 | Fluorescence | Urea | Potassium phosphate | 100 mM | 25 | null | null | 6 | null | null | null | null | null | 2.2 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1441 | ARTICLE | The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,999 | 10.1110/ps.8.8.1623 | 10452606 | Protein Sci;8;1623-35 | 3 | Bilsel O|Matthews C R|Gualfetti P J | [{"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":"100 mM... | [{"datasets":[],"id":76873,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76874,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76875,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76876,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:85 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 85 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,100 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 100 mM | 25 | null | null | 6.6 | null | null | null | null | null | 2.4 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1441 | ARTICLE | The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,999 | 10.1110/ps.8.8.1623 | 10452606 | Protein Sci;8;1623-35 | 3 | Bilsel O|Matthews C R|Gualfetti P 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":"100 mM","type":"... | [{"datasets":[],"id":76877,"numValue":6.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76878,"numValue":2.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76879,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76880,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:86 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 86 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,101 | ProTherm | 7.8 | Fluorescence | Urea | Potassium phosphate | 100 mM | 25 | null | null | 4.5 | null | null | null | null | null | 1.1 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1441 | ARTICLE | The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,999 | 10.1110/ps.8.8.1623 | 10452606 | Protein Sci;8;1623-35 | 3 | Bilsel O|Matthews C R|Gualfetti P J | [{"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":"100 mM... | [{"datasets":[],"id":76881,"numValue":4.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76882,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76883,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76884,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:87 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 87 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,102 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 100 mM | 25 | null | null | 4.6 | null | null | null | null | null | 1.1 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1441 | ARTICLE | The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,999 | 10.1110/ps.8.8.1623 | 10452606 | Protein Sci;8;1623-35 | 3 | Bilsel O|Matthews C R|Gualfetti P 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":"100 mM","type":"... | [{"datasets":[],"id":76885,"numValue":4.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76886,"numValue":1.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76887,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76888,"numValue":null,"references":[],"... | ||||||||||||||||||||||||
fireprotdb:88 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 88 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,103 | ProTherm | 7.8 | Fluorescence | Urea | Potassium phosphate | 100 mM | 25 | null | null | 4.9 | null | null | null | null | null | 0.83 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1441 | ARTICLE | The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,999 | 10.1110/ps.8.8.1623 | 10452606 | Protein Sci;8;1623-35 | 3 | Bilsel O|Matthews C R|Gualfetti P J | [{"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":"100 mM... | [{"datasets":[],"id":76889,"numValue":4.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76890,"numValue":0.83,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76891,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76892,"numValue":null,"references":[],... | ||||||||||||||||||||||||
fireprotdb:89 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 89 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,104 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 100 mM | 25 | null | null | 4.4 | null | null | null | null | null | 0.69 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1441 | ARTICLE | The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. | 1,999 | 10.1110/ps.8.8.1623 | 10452606 | Protein Sci;8;1623-35 | 3 | Bilsel O|Matthews C R|Gualfetti P 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":"100 mM","type":"... | [{"datasets":[],"id":76893,"numValue":4.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":76894,"numValue":0.69,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":76895,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":76896,"numValue":null,"references":[],... | ||||||||||||||||||||||||
fireprotdb:90 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 90 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,250 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 0.01 M | 25 | null | null | 9.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1452 | ARTICLE | Comparison of denaturation of tryptophan synthase alpha-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid. | 1,984 | 10.1016/0003-9861(84)90174-7 | 6367660 | Arch Biochem Biophys;229;448-54 | 4 | Yutani K|Sato T|Ogasahara K|Miles E W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type"... | [{"datasets":[],"id":77322,"numValue":9.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77323,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:91 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 91 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,367 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | null | null | 18.16 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":77726,"numValue":18.16,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77727,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:92 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 92 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,368 | ProTherm | 9 | CD | GdnHCl | Potassium phosphate | 20 mM | 25 | null | null | 17.97 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 754 | ARTICLE | Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit. | 1,987 | 10.1073/pnas.84.13.4441 | 3299367 | Proc Natl Acad Sci U S A;84;4441-4 | 4 | Yutani K|Ogasahara K|Sugino Y|Tsujita T | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":... | [{"datasets":[],"id":77728,"numValue":17.97,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77729,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:93 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 93 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,381 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 10 mM | 25 | null | null | 8.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 93 | ARTICLE | Role of conserved proline residues in stabilizing tryptophan synthase alpha subunit: analysis by mutants with alanine or glycine. | 1,991 | 10.1002/prot.340090203 | 2008436 | Proteins;9;90-8 | 4 | Yutani K|Ogasahara K|Sugisaki Y|Hayashi S | [{"numValue":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":77768,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77769,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:94 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 94 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,404 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | null | null | 4.23 | 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 | 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":77846,"numValue":4.23,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77847,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":77848,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:95 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 95 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,405 | ProTherm | 7 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | null | null | 4 | 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 | 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":77849,"numValue":4.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77850,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":77851,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:96 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 96 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,512 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | null | null | 6.4 | null | null | null | null | 2.51 | 2.5 | null | null | null | null | null | null | null | yes | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":78161,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78162,"numValue":2.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78163,"numValue":2.51,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78164,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:97 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 97 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,513 | ProTherm | 7.8 | Absorbance | Urea | Potassium phosphate | 10 mM | 23 | null | null | 5.2 | null | null | null | null | 3.73 | 1.4 | null | null | null | null | null | null | null | yes | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":78166,"numValue":5.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78167,"numValue":1.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":78168,"numValue":3.73,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78169,"numValue":3.0,"references":[],"str... | ||||||||||||||||||||||||
fireprotdb:98 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 98 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,724 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 20 | null | null | 7.5 | 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 | 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":20.0,"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":78819,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78820,"numValue":5.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":78821,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:99 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 99 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,930 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 15 | null | null | 6.1 | null | null | null | null | 4.7 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":15.0,"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":79453,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79454,"numValue":4.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79455,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:100 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 100 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,981 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 10 | null | null | 5.5 | null | null | null | null | 4.6 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":10.0,"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":79618,"numValue":5.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79619,"numValue":4.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79620,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:101 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 101 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,020 | ProTherm | 7.8 | NMR | Urea | Potassium phosphate | 58 mM | 5 | null | null | 4.8 | 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 | 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":79751,"numValue":4.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79752,"numValue":4.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79753,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:102 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 102 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,049 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 4 | null | null | 5 | null | null | null | null | 1.63 | 3.1 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":[],"id":79848,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79849,"numValue":3.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79850,"numValue":1.63,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79851,"numValue":null,"references":[],"st... | |||||||||||||||||||||||||
fireprotdb:103 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 103 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,050 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 4 | null | null | 6 | null | null | null | null | 3.17 | 1.9 | null | null | null | null | null | null | null | Unknown | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":[],"id":79852,"numValue":6.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79853,"numValue":1.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79854,"numValue":3.17,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":79855,"numValue":null,"references":[],"st... | |||||||||||||||||||||||||
fireprotdb:104 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 104 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,001 | ProTherm | 7.8 | CD | Urea | potassium phosphate | 10 mM | 25 | null | null | 6.13 | null | null | null | null | 2.68 | 2.29 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 629 | ARTICLE | A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein. | 2,002 | 10.1016/s0022-2836(02)00737-4 | 12215410 | J Mol Biol;322;7-13 | 2 | Wu Ying|Matthews C Robert | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":91369,"numValue":6.13,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91370,"numValue":2.29,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":91371,"numValue":2.68,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":91372,"numValue":3.0,"references":[],"s... | ||||||||||||||||||||||||
fireprotdb:106 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 106 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,098 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 6.13 | null | null | null | null | null | 2.29 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":91694,"numValue":6.13,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91695,"numValue":2.29,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":91696,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":91697,"numValue":null,"references":[]... | ||||||||||||||||||||||||
fireprotdb:107 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 107 | train | sequence | 1 | 1 | -1 | 268 | -1 | 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 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,099 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | null | null | 4.72 | null | null | null | null | null | 1.2 | null | null | null | null | null | null | null | Unknown | 3.0 | DG|M|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 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":91698,"numValue":4.72,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":91699,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":91700,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":91701,"numValue":null,"references":[],... | ||||||||||||||||||||||||
fireprotdb:108 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 108 | train | mutant | 28 | 1 | 29 | 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 | S6P | S6P | 1 | 1 | 0 | 0 | 6 | S | P | 2 | CONSERVATION | 1WQ5 | 282 | null | 6 | A | H | true | false | 60.938195 | 22.05 | 28 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:S6P | 54.3 | -5.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:S6P","type... | [{"datasets":[],"id":82,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":83,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":84,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6185,"numValue":2.0,"position":6,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:109 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 109 | train | mutant | 24 | 1 | 25 | 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 | P21S | P21S | 1 | 1 | 0 | 0 | 21 | P | S | 5 | CONSERVATION | 1WQ5 | 282 | null | 21 | A | E | false | false | 0.492602 | 16.06 | 24 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:P21S | 55.2 | -4.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 2 | ARTICLE | Thermal stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. | 1,992 | 10.1016/0003-9861(92)90047-z | 1727648 | Arch Biochem Biophys;292;34-41 | 3 | Lim W K|Brouillette C|Hardman J K | [{"numValue":7.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"1 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1WQ5_A:P21S","typ... | [{"datasets":[],"id":70,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":71,"numValue":-4.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":72,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6200,"numValue":5.0,"position":21,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:110 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 110 | train | mutant | 10 | 1 | 11 | 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 | F22S | F22S | 1 | 1 | 0 | 0 | 22 | F | S | 8 | CONSERVATION | 1WQ5 | 282 | null | 22 | A | E | true | true | 40.206761 | 20.991818 | 10 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:F22S | 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:F22S","typ... | [{"datasets":["HotMuSiC_S1626.csv"],"id":28,"numValue":60.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":29,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":30,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6201,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:111 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 111 | train | mutant | 4,407 | 1 | 4,924 | 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 | F22L | F22L | 1 | 1 | 0 | 0 | 22 | F | L | 8 | CONSERVATION | 1WQ5 | 282 | null | 22 | A | E | true | true | 40.206761 | 20.991818 | 10,455 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:F22L | null | null | 7.9 | -2.2 | null | null | null | 2.54 | 3.1 | 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":35824,"numValue":7.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35825,"numValue":-2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35826,"numValue":3.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35827,"numValue":2.54,"references":[],"s... | [{"id":6201,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:112 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 112 | train | mutant | 4,407 | 1 | 4,924 | 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 | F22L | F22L | 1 | 1 | 0 | 0 | 22 | F | L | 8 | CONSERVATION | 1WQ5 | 282 | null | 22 | A | E | true | true | 40.206761 | 20.991818 | 10,456 | ProTherm | 7.8 | CD | Urea | Potassium phosphate | 10 mM | 25 | 1WQ5_A:F22L | null | null | 4.2 | 0.8 | null | null | null | 3.62 | 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":35830,"numValue":4.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":35831,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35832,"numValue":1.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35833,"numValue":3.62,"references":[],"st... | [{"id":6201,"numValue":8.0,"position":22,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:113 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 113 | train | mutant | 6 | 1 | 7 | 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 | T24M | T24M | 1 | 1 | 0 | 0 | 24 | T | M | 8 | CONSERVATION | 1WQ5 | 282 | null | 24 | A | E | true | false | 50.865846 | 24.547143 | 6 | ProTherm | 7.2 | DSC | Thermal | Sodium phosphate | 1 mM | null | 1WQ5_A:T24M | 61.8 | 2.3 | 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:T24M","typ... | [{"datasets":["HotMuSiC_S1626.csv"],"id":16,"numValue":61.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":17,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":18,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6203,"numValue":8.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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