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:7803 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,803 | train | mutant | 6,889 | 126 | 7,531 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S | C33S|C36S | 2 | 2 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36 | A | L|H | true | true | 4.2852 | 29.000834 | 14,723 | ProTherm | 6 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S | 77.06 | 3.05 | null | null | 50.43 | 1.07 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 910 | ARTICLE | Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry. | 1,994 | 10.1021/bi00178a027 | 8142367 | Biochemistry;33;3688-92 | 5 | Wynn R|Kishore N|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54442,"numValue":77.06,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54443,"numValue":3.05,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54444,"numValue":50.43,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54445,"numValue":1.07,"references":... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7804 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,804 | train | mutant | 6,889 | 126 | 7,531 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S | C33S|C36S | 2 | 2 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36 | A | L|H | true | true | 4.2852 | 29.000834 | 14,724 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S | 74.49 | 1.15 | null | null | 89.24 | 2.29 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 910 | ARTICLE | Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry. | 1,994 | 10.1021/bi00178a027 | 8142367 | Biochemistry;33;3688-92 | 5 | Wynn R|Kishore N|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54447,"numValue":74.49,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54448,"numValue":1.15,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54449,"numValue":89.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54450,"numValue":2.29,"references":... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,805 | train | mutant | 6,889 | 126 | 7,531 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S | C33S|C36S | 2 | 2 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36 | A | L|H | true | true | 4.2852 | 29.000834 | 14,725 | ProTherm | 8 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S | 72.29 | null | null | null | 84.83 | 2.43 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 910 | ARTICLE | Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry. | 1,994 | 10.1021/bi00178a027 | 8142367 | Biochemistry;33;3688-92 | 5 | Wynn R|Kishore N|Sturtevant J M|Ladbury J E|Hellinga H W | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54452,"numValue":72.29,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54453,"numValue":84.83,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54454,"numValue":2.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54455,"numValue":null,"references":... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,806 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,839 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 65.24 | null | null | null | 62.6 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54768,"numValue":65.24,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54769,"numValue":62.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54770,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7807 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,807 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,840 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 65.2 | null | null | null | 84.6 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54771,"numValue":65.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54772,"numValue":84.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54773,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,808 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,841 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 66.91 | null | null | null | 86.7 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54774,"numValue":66.91,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54775,"numValue":86.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54776,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,809 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,842 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 66.3 | null | null | null | 74.1 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54777,"numValue":66.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54778,"numValue":74.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54779,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,810 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,843 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.33 | null | null | null | 100.5 | 1.87 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54780,"numValue":69.33,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54781,"numValue":100.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54782,"numValue":1.87,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54783,"numValue":null,"references":... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,811 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,844 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.36 | null | null | null | 106.9 | 1.86 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54784,"numValue":69.36,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54785,"numValue":106.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54786,"numValue":1.86,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54787,"numValue":null,"references":... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,812 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,845 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.74 | null | null | null | 94.5 | 0.96 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54788,"numValue":69.74,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54789,"numValue":94.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54790,"numValue":0.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54791,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,813 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,846 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.34 | null | null | null | 94 | 1.45 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54792,"numValue":69.34,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54793,"numValue":94.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54794,"numValue":1.45,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54795,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7814 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,814 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,847 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.65 | null | null | null | 97.6 | 1.24 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54796,"numValue":69.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54797,"numValue":97.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54798,"numValue":1.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54799,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7815 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,815 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,848 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.69 | null | null | null | 97.1 | 1.48 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54800,"numValue":69.69,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54801,"numValue":97.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54802,"numValue":1.48,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54803,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7816 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,816 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,849 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.8 | null | null | null | 96.8 | 1.55 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54804,"numValue":69.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54805,"numValue":96.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54806,"numValue":1.55,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54807,"numValue":null,"references":[]... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7817 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,817 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,850 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 67.3 | null | null | null | 67 | 3.06 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54808,"numValue":67.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54809,"numValue":67.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54810,"numValue":3.06,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54811,"numValue":null,"references":[]... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7819 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,819 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,852 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 70.34 | null | null | null | 102 | 0.41 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54816,"numValue":70.34,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54817,"numValue":102.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54818,"numValue":0.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54819,"numValue":null,"references":... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7820 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,820 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,853 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 63.07 | null | null | null | 53.5 | 1.87 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54820,"numValue":63.07,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54821,"numValue":53.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54822,"numValue":1.87,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54823,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7821 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,821 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,854 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 63.72 | null | null | null | 52.9 | 2.19 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54824,"numValue":63.72,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54825,"numValue":52.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54826,"numValue":2.19,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54827,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7822 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,822 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,855 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 65.49 | null | null | null | 56.5 | 2.18 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54828,"numValue":65.49,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54829,"numValue":56.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54830,"numValue":2.18,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54831,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7823 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,823 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,856 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 62.63 | null | null | null | 71.8 | 2.8 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54832,"numValue":62.63,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54833,"numValue":71.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54834,"numValue":2.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54835,"numValue":null,"references":[]... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7824 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,824 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,857 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 63.43 | null | null | null | 51 | 2.45 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54836,"numValue":63.43,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54837,"numValue":51.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54838,"numValue":2.45,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54839,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7825 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,825 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,858 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.59 | null | null | null | 84.6 | 0.85 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54840,"numValue":69.59,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54841,"numValue":84.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54842,"numValue":0.85,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54843,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7826 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,826 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 14,859 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | 69.56 | null | null | null | 81.1 | 1.54 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 920 | ARTICLE | The adaptability of Escherichia coli thioredoxin to non-conservative amino acid substitutions. | 1,997 | 10.1002/pro.5560060621 | 9194193 | Protein Sci;6;1325-32 | 4 | Wynn R|O'Brien R|Davis B|Driscoll P C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C32S 2TRX... | [{"datasets":[],"id":54844,"numValue":69.56,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54845,"numValue":81.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54846,"numValue":1.54,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54847,"numValue":null,"references":[... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7827 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,827 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 15,343 | ProTherm | 8 | Refraction | Urea | Tris | 50 mM | 25 | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | null | null | 5.14 | null | null | null | null | 3 | 1.72 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 927 | ARTICLE | Partitioning the effects of changes in a protein to the folded or unfolded forms by using a thermodynamic cycle: a change in Escherichia coli thioredoxin does not affect the unfolded state. | 1,993 | 10.1021/bi00210a046 | 8251515 | Biochemistry;32;12922-7 | 2 | Wynn R|Richards F M | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Refraction","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":56312,"numValue":5.14,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56313,"numValue":1.72,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56314,"numValue":3.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56315,"numValue":null,"references":[],"s... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7828 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,828 | train | mutant | 6,976 | 126 | 7,627 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C33S|C36S|L79C | C33S|C36S|L79C | 3 | 3 | 0 | 0 | 33 | C | S | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 33|36|79 | A | L|H|E | true | true | 3.055444 | 25.689097 | 15,344 | ProTherm | 8 | Refraction | Urea | Tris | 50 mM | 25 | 2TRX_A:C32S 2TRX_A:C35S 2TRX_A:L78C | null | null | 5.95 | null | null | null | null | 3.49 | 1.71 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 927 | ARTICLE | Partitioning the effects of changes in a protein to the folded or unfolded forms by using a thermodynamic cycle: a change in Escherichia coli thioredoxin does not affect the unfolded state. | 1,993 | 10.1021/bi00210a046 | 8251515 | Biochemistry;32;12922-7 | 2 | Wynn R|Richards F M | [{"numValue":8.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Refraction","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":56316,"numValue":5.95,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56317,"numValue":1.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56318,"numValue":3.49,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56319,"numValue":null,"references":[],"... | [{"id":37,"numValue":null,"position":33,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8034,"numValue":9.0,"position":33,"positionArray":null,"p... | ||||||||||||||
fireprotdb:7829 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,829 | train | mutant | 4,565 | 126 | 5,085 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | P35S | P35S | 1 | 1 | 0 | 0 | 35 | P | S | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 35 | A | H | false | false | 61.918797 | 27.711428 | 10,742 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 50 mM | 25 | 2TRX_A:P34S | null | null | 8.8 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 703 | ARTICLE | Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding. | 1,987 | 10.1021/bi00395a028 | 3322388 | Biochemistry;26;6765-74 | 2 | Kelley R F|Richards F M | [{"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":"50 mM","type":... | [{"datasets":[],"id":36942,"numValue":8.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":36943,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36944,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8036,"numValue":9.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7830 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,830 | train | mutant | 4,565 | 126 | 5,085 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | P35S | P35S | 1 | 1 | 0 | 0 | 35 | P | S | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 35 | A | H | false | false | 61.918797 | 27.711428 | 12,550 | ProTherm | 8.7 | Absorbance | Urea | Tris | 0.1 M | 23 | KCl | 0.2 M | 2TRX_A:P34S | null | null | 8.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 796 | ARTICLE | Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein. | 1,991 | 10.1073/pnas.88.23.10573 | 1961723 | Proc Natl Acad Sci U S A;88;10573-7 | 2 | Kim P S|Lin T Y | [{"numValue":8.7,"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":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_C... | [{"datasets":[],"id":45531,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45532,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8036,"numValue":9.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7831 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,831 | train | mutant | 4,565 | 126 | 5,085 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | P35S | P35S | 1 | 1 | 0 | 0 | 35 | P | S | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 35 | A | H | false | false | 61.918797 | 27.711428 | 12,551 | ProTherm | 8.7 | Absorbance | Urea | Tris | 0.1 M | 23 | KCl | 0.2 M | 2TRX_A:P34S | null | null | 9.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 796 | ARTICLE | Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein. | 1,991 | 10.1073/pnas.88.23.10573 | 1961723 | Proc Natl Acad Sci U S A;88;10573-7 | 2 | Kim P S|Lin T Y | [{"numValue":8.7,"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":"Tris","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_C... | [{"datasets":[],"id":45533,"numValue":9.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":45534,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8036,"numValue":9.0,"position":35,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:7832 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,832 | train | mutant | 258 | 126 | 289 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C36A | C36A | 1 | 1 | 0 | 0 | 36 | C | A | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 36 | A | H | true | true | 2.422929 | 28.384167 | 464 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 2TRX_A:C35A | 73 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:C35A","typ... | [{"datasets":[],"id":1860,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1861,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8037,"numValue":9.0,"position":36,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7833 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,833 | train | mutant | 258 | 126 | 289 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | C36A | C36A | 1 | 1 | 0 | 0 | 36 | C | A | 9 | ACTIVE_SITE|CONSERVATION | 2TRX|2H6X | 371|416 | null | 36 | A | H | true | true | 2.422929 | 28.384167 | 8,759 | ProTherm | 7 | CD | GdnHCl | sodium phosphate | 50 mM | 25 | 2TRX_A:C35A | null | null | null | -5.9 | null | null | null | 1.7 | 3.5 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":29587,"numValue":-5.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29588,"numValue":3.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":29589,"numValue":1.7,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":29590,"numValue":null,"references":[],"s... | [{"id":38,"numValue":null,"position":36,"positionArray":null,"positionRange":null,"strValue":"Nucleophile","type":"ACTIVE_SITE"},{"id":8037,"numValue":9.0,"position":36,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7835 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,835 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 7,112 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 60 | 2TRX_A:M37L | null | null | 2.9 | null | null | null | null | 1.4 | 2 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":60.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":24945,"numValue":2.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":24946,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":24947,"numValue":1.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":24948,"numValue":null,"references":[],"str... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,836 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 7,307 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 55 | 2TRX_A:M37L | null | null | 5.3 | null | null | null | null | 2.29 | 2.1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":25508,"numValue":5.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":25509,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":25510,"numValue":2.29,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":25511,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7837 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,837 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 7,879 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 45 | 2TRX_A:M37L | null | null | 7.6 | null | null | null | null | 2.45 | 3.1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":26942,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":26943,"numValue":3.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":26944,"numValue":2.45,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":26945,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,838 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 8,149 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 40 | 2TRX_A:M37L | null | null | 6.1 | null | null | null | null | 2.74 | 2.2 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":40.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":27686,"numValue":6.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":27687,"numValue":2.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":27688,"numValue":2.74,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":27689,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,839 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 11,046 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 25 | 2TRX_A:M37L | null | null | 9.1 | null | null | null | null | 2.58 | 3.7 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":38004,"numValue":9.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38005,"numValue":3.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38006,"numValue":2.58,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38007,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7840 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,840 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 13,883 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 15 | 2TRX_A:M37L | null | null | 8 | null | null | null | null | 2.34 | 3.4 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":15.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":51369,"numValue":8.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51370,"numValue":3.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":51371,"numValue":2.34,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51372,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,841 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 14,088 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 10 | 2TRX_A:M37L | null | null | 5.9 | null | null | null | null | 2.47 | 2.4 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":52114,"numValue":5.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52115,"numValue":2.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":52116,"numValue":2.47,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":52117,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,842 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 14,184 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 8 | 2TRX_A:M37L | null | null | 6.2 | null | null | null | null | 2.15 | 2.9 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":8.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":52520,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52521,"numValue":2.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":52522,"numValue":2.15,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":52523,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7843 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,843 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 14,185 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 6 | 2TRX_A:M37L | null | null | 8 | null | null | null | null | 2.11 | 3.9 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":6.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":52524,"numValue":8.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52525,"numValue":3.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":52526,"numValue":2.11,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":52527,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,844 | train | mutant | 2,029 | 126 | 2,266 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L | M38L | 1 | 1 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38 | A | H | false | true | 135.527832 | 35.780625 | 14,328 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 4 | 2TRX_A:M37L | null | null | 8 | null | null | null | null | 2.09 | 3.8 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":4.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":53016,"numValue":8.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":53017,"numValue":3.8,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":53018,"numValue":2.09,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":53019,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,845 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 14,775 | ProTherm | 7 | DSC | Thermal | phosphate | 50 mM | null | 2TRX_A:M37L 2TRX_A:P40S | 83.7 | null | null | null | 96.4 | 2.45 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:M37L 2TRX_A:P40S... | [{"datasets":[],"id":54590,"numValue":83.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54591,"numValue":96.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54592,"numValue":2.45,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54593,"numValue":null,"references":[]... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7847 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,847 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 14,955 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 60 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 3.4 | null | null | null | null | 2.1 | 1.6 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":60.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":55067,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55068,"numValue":1.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55069,"numValue":2.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":55070,"numValue":null,"references":[],"str... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7848 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,848 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 14,973 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 55 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 6.6 | null | null | null | null | 2.1 | 3.1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":55.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":55117,"numValue":6.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55118,"numValue":3.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55119,"numValue":2.1,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":55120,"numValue":null,"references":[],"str... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,849 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 15,051 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 50 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 5 | null | null | null | null | 2.41 | 2.1 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":55291,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55292,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55293,"numValue":2.41,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":55294,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,850 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 15,094 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 45 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 8.6 | null | null | null | null | 2.53 | 3.4 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":45.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":55400,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55401,"numValue":3.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55402,"numValue":2.53,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":55403,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7852 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,852 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 15,129 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 37 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 8.1 | null | null | null | null | 2.73 | 3 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":37.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":55501,"numValue":8.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55502,"numValue":3.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55503,"numValue":2.73,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":55504,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7854 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,854 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 15,389 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 25 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 11.5 | null | null | null | null | 2.87 | 4 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":56484,"numValue":11.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56485,"numValue":4.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":56486,"numValue":2.87,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56487,"numValue":null,"references":[],"s... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7855 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,855 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 15,598 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 20 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 10.4 | null | null | null | null | 2.85 | 3.6 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":57230,"numValue":10.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57231,"numValue":3.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57232,"numValue":2.85,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":57233,"numValue":null,"references":[],"s... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7857 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,857 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 15,618 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 10 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 9.2 | null | null | null | null | 2.71 | 3.4 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_C... | [{"datasets":[],"id":57308,"numValue":9.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57309,"numValue":3.4,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57310,"numValue":2.71,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":57311,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7858 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,858 | train | mutant | 6,926 | 126 | 7,568 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | M38L|P41S | M38L|P41S | 2 | 2 | 0 | 0 | 38 | M | L | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 38|41 | A | H | false | true | 105.914398 | 31.485669 | 15,627 | ProTherm | 7 | DSC | GdnHCl | phosphate | 50 mM | 5 | 2TRX_A:M37L 2TRX_A:P40S | null | null | 8.6 | null | null | null | null | 2.47 | 3.5 | null | null | null | null | null | null | null | yes | DG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 364 | ARTICLE | Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. | 1,999 | 10.1110/ps.8.11.2455 | 10595549 | Protein Sci;8;2455-9 | 3 | Chakrabarti A|Srivastava S|Swaminathan C P | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":5.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CO... | [{"datasets":[],"id":57343,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57344,"numValue":3.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57345,"numValue":2.47,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":57346,"numValue":null,"references":[],"st... | [{"id":8039,"numValue":7.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8042,"numValue":9.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,859 | train | mutant | 4,960 | 126 | 5,511 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | I39V | I39V | 1 | 1 | 0 | 0 | 39 | I | V | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 39 | A | H | true | true | 3.628015 | 28.239375 | 11,544 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:I38V | null | null | null | 4 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39863,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39864,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39865,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8040,"numValue":7.0,"position":39,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7860 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,860 | train | mutant | 4,961 | 126 | 5,512 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | I42V | I42V | 1 | 1 | 0 | 0 | 42 | I | V | 5 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 42 | A | H | false | false | 30.233462 | 26.400625 | 11,545 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:I41V | null | null | null | 2.7 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39866,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39867,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39868,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8043,"numValue":5.0,"position":42,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7861 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,861 | train | mutant | 4,949 | 126 | 5,500 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D44E | D44E | 1 | 1 | 0 | 0 | 44 | D | E | 4 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 44 | A | H | true | false | 57.683087 | 29.23625 | 11,532 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:D43E | null | null | null | -2.4 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39825,"numValue":-2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39826,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39827,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8045,"numValue":4.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,864 | train | mutant | 4,950 | 126 | 5,501 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D48E | D48E | 1 | 1 | 0 | 0 | 48 | D | E | 1 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 48 | A | H | false | false | 77.553672 | 40.18125 | 11,533 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:D47E | null | null | null | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39828,"numValue":-1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39829,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39830,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8049,"numValue":1.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,865 | train | mutant | 4,955 | 126 | 5,506 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | E49D | E49D | 1 | 1 | 0 | 0 | 49 | E | D | 5 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 49 | A | H | false | false | 84.027002 | 40.41 | 11,538 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:E48D | null | null | null | 4.5 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39843,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39844,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39845,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8050,"numValue":5.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,866 | train | mutant | 4,968 | 126 | 5,519 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | V56I | V56I | 1 | 1 | 0 | 0 | 56 | V | I | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 56 | A | E | true | false | 1.496178 | 22.484286 | 11,552 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:V55I | null | null | null | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39891,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39892,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39893,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8057,"numValue":7.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7867 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,867 | train | mutant | 4,963 | 126 | 5,514 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | I61V | I61V | 1 | 1 | 0 | 0 | 61 | I | V | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 61 | A | T | false | false | 36.515982 | 27.5625 | 11,547 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:I60V | null | null | null | 0.8 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39874,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39875,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39876,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8062,"numValue":7.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,868 | train | mutant | 4,951 | 126 | 5,502 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D62E | D62E | 1 | 1 | 0 | 0 | 62 | D | E | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 62 | A | T | false | false | 85.235628 | 29.8625 | 11,534 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:D61E | null | null | null | 2.6 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39831,"numValue":2.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39832,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39833,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8063,"numValue":9.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7869 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,869 | train | mutant | 259 | 126 | 290 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T67L | T67L | 1 | 1 | 0 | 0 | 67 | T | L | 6 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 67 | A | H|S | false | false | 3.135001 | 28.302857 | 465 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 2TRX_A:T66L | 85 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:T66L","typ... | [{"datasets":[],"id":1862,"numValue":85.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1863,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8068,"numValue":6.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7870 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,870 | train | mutant | 259 | 126 | 290 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T67L | T67L | 1 | 1 | 0 | 0 | 67 | T | L | 6 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 67 | A | H|S | false | false | 3.135001 | 28.302857 | 8,760 | ProTherm | 7 | CD | GdnHCl | sodium phosphate | 50 mM | 25 | 2TRX_A:T66L | null | null | null | -7.6 | null | null | null | 2.4 | 3.1 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":29591,"numValue":-7.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29592,"numValue":3.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":29593,"numValue":2.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":29594,"numValue":null,"references":[],"s... | [{"id":8068,"numValue":6.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7871 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,871 | train | mutant | 4,964 | 126 | 5,515 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | I73V | I73V | 1 | 1 | 0 | 0 | 73 | I | V | 8 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 73 | A | L | false | false | 27.251854 | 31.629375 | 11,548 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:I72V | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39877,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39878,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39879,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8074,"numValue":8.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7872 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,872 | train | mutant | 4,965 | 126 | 5,516 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | I76V | I76V | 1 | 1 | 0 | 0 | 76 | I | V | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 76 | A | S | false | false | 30.962104 | 26.98875 | 11,549 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:I75V | null | null | null | 3 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39880,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39881,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39882,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8077,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7873 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,873 | train | mutant | 4,564 | 126 | 5,084 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | P77A | P77A | 1 | 1 | 0 | 0 | 77 | P | A | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 77 | A | S | true | true | 1.531934 | 23.702143 | 10,741 | ProTherm | 7 | CD | GdnHCl | Potassium phosphate | 50 mM | 25 | 2TRX_A:P76A | null | null | 5 | 3.9 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|DDG|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 703 | ARTICLE | Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding. | 1,987 | 10.1021/bi00395a028 | 3322388 | Biochemistry;26;6765-74 | 2 | Kelley R F|Richards F M | [{"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":"50 mM","type":... | [{"datasets":[],"id":36939,"numValue":5.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":36940,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36941,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8078,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7874 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,874 | train | mutant | 260 | 126 | 291 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T78V | T78V | 1 | 1 | 0 | 0 | 78 | T | V | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 78 | A | E | false | false | 4.760999 | 21.603572 | 466 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 2TRX_A:T77V | 82 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:T77V","typ... | [{"datasets":[],"id":1864,"numValue":82.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1865,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8079,"numValue":9.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7875 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,875 | train | mutant | 260 | 126 | 291 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T78V | T78V | 1 | 1 | 0 | 0 | 78 | T | V | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 78 | A | E | false | false | 4.760999 | 21.603572 | 8,761 | ProTherm | 7 | CD | GdnHCl | sodium phosphate | 50 mM | 25 | 2TRX_A:T77V | null | null | null | -7.9 | null | null | null | 2.5 | 3.2 | null | null | null | null | null | null | null | Unknown | DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 49 | ARTICLE | Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. | 2,001 | 10.1021/bi010427y | 11513583 | Biochemistry;40;10047-53 | 2 | Bolon D N|Mayo S L | [{"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":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":29595,"numValue":-7.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29596,"numValue":3.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":29597,"numValue":2.5,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":29598,"numValue":null,"references":[],"s... | [{"id":8079,"numValue":9.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,876 | train | mutant | 7,486 | 126 | 8,169 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T78C|V92C | T78C|V92C | 2 | 2 | 0 | 0 | 78 | T | C | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 78|92 | A | E | false | false | 49.567885 | 23.009286 | 15,910 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 2TRX_A:T77C 2TRX_A:V91C | 96.8 | 7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":58441,"numValue":96.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58442,"numValue":7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58443,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8079,"numValue":9.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8093,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,877 | train | mutant | 7,486 | 126 | 8,169 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T78C|V92C | T78C|V92C | 2 | 2 | 0 | 0 | 78 | T | C | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 78|92 | A | E | false | false | 49.567885 | 23.009286 | 15,913 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 2TRX_A:T77C 2TRX_A:V91C | 75 | -0.3 | 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 | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":58450,"numValue":75.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58451,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58452,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8079,"numValue":9.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8093,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7878 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,878 | train | mutant | 7,486 | 126 | 8,169 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T78C|V92C | T78C|V92C | 2 | 2 | 0 | 0 | 78 | T | C | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 78|92 | A | E | false | false | 49.567885 | 23.009286 | 16,687 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | 89.8 | 2TRX_A:T77C 2TRX_A:V91C | null | null | null | -2.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":89.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 1... | [{"datasets":[],"id":61418,"numValue":-2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61419,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8079,"numValue":9.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8093,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7880 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,880 | train | mutant | 7,486 | 126 | 8,169 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | T78C|V92C | T78C|V92C | 2 | 2 | 0 | 0 | 78 | T | C | 9 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 78|92 | A | E | false | false | 49.567885 | 23.009286 | 16,965 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 10 mM | 25 | 2TRX_A:T77C 2TRX_A:V91C | null | null | 6.4 | -0.2 | null | null | null | 1.72 | 3.6 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":62365,"numValue":6.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62366,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":62367,"numValue":3.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62368,"numValue":1.72,"references":[],"s... | [{"id":8079,"numValue":9.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8093,"numValue":7.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7881 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,881 | train | mutant | 1,657 | 126 | 1,866 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79K | L79K | 1 | 1 | 0 | 0 | 79 | L | K | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79 | A | E | false | false | 0.595933 | 19.065625 | 3,106 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:L78K | 71.6 | -13.7 | null | null | null | 0.94 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 283 | ARTICLE | Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. | 1,995 | 10.1021/bi00007a007 | 7857925 | Biochemistry;34;2148-52 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Thomson J A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:L78K","ty... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv"],"id":11302,"numValue":71.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1791.csv"],"id":11303,"numValue":-13.7,"references":[],"strValue":null,"type":"D... | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7882 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,882 | train | mutant | 1,657 | 126 | 1,866 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79K | L79K | 1 | 1 | 0 | 0 | 79 | L | K | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79 | A | E | false | false | 0.595933 | 19.065625 | 6,478 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | 85.32 | 2TRX_A:L78K | null | null | null | 3.9 | null | 0.94 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 283 | ARTICLE | Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. | 1,995 | 10.1021/bi00007a007 | 7857925 | Biochemistry;34;2148-52 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Thomson J A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":85.32,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":23234,"numValue":0.94,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23235,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23236,"numValue":null,"reference... | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7883 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,883 | train | mutant | 1,658 | 126 | 1,867 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79R | L79R | 1 | 1 | 0 | 0 | 79 | L | R | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79 | A | E | false | false | 0.595933 | 19.065625 | 3,107 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | null | 2TRX_A:L78R | 69.2 | -16.1 | null | null | null | 1.09 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 283 | ARTICLE | Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. | 1,995 | 10.1021/bi00007a007 | 7857925 | Biochemistry;34;2148-52 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Thomson J A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:L78R","ty... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv"],"id":11306,"numValue":69.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1791.csv"],"id":11307,"numValue":-16.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["M47an... | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7884 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,884 | train | mutant | 1,658 | 126 | 1,867 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79R | L79R | 1 | 1 | 0 | 0 | 79 | L | R | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79 | A | E | false | false | 0.595933 | 19.065625 | 6,479 | ProTherm | 7 | DSC | Thermal | Sodium phosphate | 50 mM | 85.32 | 2TRX_A:L78R | null | null | null | 4 | null | 1.09 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 283 | ARTICLE | Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. | 1,995 | 10.1021/bi00007a007 | 7857925 | Biochemistry;34;2148-52 | 4 | Wynn R|Sturtevant J M|Ladbury J E|Thomson J A | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":85.32,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":... | [{"datasets":[],"id":23237,"numValue":1.09,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23238,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23239,"numValue":null,"reference... | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7885 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,885 | train | mutant | 7,487 | 126 | 8,170 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79C|K91C | L79C|K91C | 2 | 2 | 0 | 0 | 79 | L | C | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79|91 | A | E | false | false | 35.06384 | 21.682535 | 15,911 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 2TRX_A:L78C 2TRX_A:K90C | 81.6 | -7.2 | 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 | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":58444,"numValue":81.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58445,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58446,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8092,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,886 | train | mutant | 7,487 | 126 | 8,170 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79C|K91C | L79C|K91C | 2 | 2 | 0 | 0 | 79 | L | C | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79|91 | A | E | false | false | 35.06384 | 21.682535 | 15,914 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 2TRX_A:L78C 2TRX_A:K90C | 75.5 | 0.2 | 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 | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":58453,"numValue":75.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58454,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58455,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8092,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7887 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,887 | train | mutant | 7,487 | 126 | 8,170 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79C|K91C | L79C|K91C | 2 | 2 | 0 | 0 | 79 | L | C | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79|91 | A | E | false | false | 35.06384 | 21.682535 | 16,688 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | 89.8 | 2TRX_A:L78C 2TRX_A:K90C | null | null | null | 2.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":89.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 1... | [{"datasets":[],"id":61420,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61421,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8092,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7888 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,888 | train | mutant | 7,487 | 126 | 8,170 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79C|K91C | L79C|K91C | 2 | 2 | 0 | 0 | 79 | L | C | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79|91 | A | E | false | false | 35.06384 | 21.682535 | 16,963 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 10 mM | 25 | 2TRX_A:L78C 2TRX_A:K90C | null | null | 6.7 | 2.9 | null | null | null | 1.85 | 3.7 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":62355,"numValue":6.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62356,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":62357,"numValue":3.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62358,"numValue":1.85,"references":[],"st... | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8092,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7889 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,889 | train | mutant | 7,487 | 126 | 8,170 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L79C|K91C | L79C|K91C | 2 | 2 | 0 | 0 | 79 | L | C | 7 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 79|91 | A | E | false | false | 35.06384 | 21.682535 | 16,966 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 10 mM | 25 | 2TRX_A:L78C 2TRX_A:K90C | null | null | 6.3 | -0.1 | null | null | null | 1.71 | 3.6 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":62370,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62371,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":62372,"numValue":3.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62373,"numValue":1.71,"references":[],"s... | [{"id":8080,"numValue":7.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8092,"numValue":4.0,"position":91,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,890 | train | mutant | 7,488 | 126 | 8,171 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L80C|T90C | L80C|T90C | 2 | 2 | 0 | 0 | 80 | L | C | 5 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 80|90 | A | E | false | false | 40.150925 | 20.997455 | 15,912 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 2TRX_A:L79C 2TRX_A:T89C | 99.6 | 9.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":58447,"numValue":99.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58448,"numValue":9.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58449,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8081,"numValue":5.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8091,"numValue":5.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,891 | train | mutant | 7,488 | 126 | 8,171 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L80C|T90C | L80C|T90C | 2 | 2 | 0 | 0 | 80 | L | C | 5 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 80|90 | A | E | false | false | 40.150925 | 20.997455 | 15,915 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | null | 2TRX_A:L79C 2TRX_A:T89C | 75.7 | 0.4 | 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 | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 10mM, 10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":58456,"numValue":75.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58457,"numValue":0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58458,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8081,"numValue":5.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8091,"numValue":5.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,892 | train | mutant | 7,488 | 126 | 8,171 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L80C|T90C | L80C|T90C | 2 | 2 | 0 | 0 | 80 | L | C | 5 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 80|90 | A | E | false | false | 40.150925 | 20.997455 | 16,689 | ProTherm | 7 | DSC | Thermal | citrate, glycine, HEPES | 10 mM, 10mM, 10 mM | 89.8 | 2TRX_A:L79C 2TRX_A:T89C | null | null | null | -2.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":89.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"citrate, glycine, HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM, 1... | [{"datasets":[],"id":61422,"numValue":-2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61423,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8081,"numValue":5.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8091,"numValue":5.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,893 | train | mutant | 7,488 | 126 | 8,171 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L80C|T90C | L80C|T90C | 2 | 2 | 0 | 0 | 80 | L | C | 5 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 80|90 | A | E | false | false | 40.150925 | 20.997455 | 16,964 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 10 mM | 25 | 2TRX_A:L79C 2TRX_A:T89C | null | null | 11.8 | -2.2 | null | null | null | 3.2 | 3.7 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":62360,"numValue":11.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62361,"numValue":-2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":62362,"numValue":3.7,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62363,"numValue":3.2,"references":[],"s... | [{"id":8081,"numValue":5.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8091,"numValue":5.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7894 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,894 | train | mutant | 7,488 | 126 | 8,171 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | L80C|T90C | L80C|T90C | 2 | 2 | 0 | 0 | 80 | L | C | 5 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 80|90 | A | E | false | false | 40.150925 | 20.997455 | 16,967 | ProTherm | 7 | Fluorescence | GdnHCl | phosphate | 10 mM | 25 | 2TRX_A:L79C 2TRX_A:T89C | null | null | 6.3 | -0.1 | null | null | null | 1.7 | 3.6 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 950 | ARTICLE | Protein stabilization by introduction of cross-strand disulfides. | 2,005 | 10.1021/bi050921s | 16262263 | Biochemistry;44;14638-46 | 7 | Indu S|Ramakrishnan C|Varadarajan Raghavan|Chakraborty Kausik|Thakurela Sudhir|Prajapati Ravindra Singh|Ali P Shaik Syed | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":... | [{"datasets":[],"id":62375,"numValue":6.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":62376,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":62377,"numValue":3.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":62378,"numValue":1.7,"references":[],"st... | [{"id":8081,"numValue":5.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8091,"numValue":5.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7895 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,895 | train | mutant | 113 | 126 | 127 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | E86R | E86R | 1 | 1 | 0 | 0 | 86 | E | R | 4 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 86 | A | E | false | false | 123.529972 | 30.865556 | 225 | ProTherm | 7 | CD | Thermal | sodium phosphate | 10 mM | null | 2TRX_A:E85R | 90 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 17 | ARTICLE | A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli. | 2,001 | 10.1093/protein/14.4.255 | 11391017 | Protein Eng;14;255-60 | 4 | Pedone E|Saviano M|Rossi M|Bartolucci S | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2TRX_A:E85R","typ... | [{"datasets":[],"id":941,"numValue":90.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":942,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":8087,"numValue":4.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:7899 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,899 | train | mutant | 4,957 | 126 | 5,508 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | E102D | E102D | 1 | 1 | 0 | 0 | 102 | E | D | 1 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 102 | A | H | false | false | 109.073371 | 32.666945 | 11,540 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:E101D | null | null | null | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39851,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39852,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39853,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8103,"numValue":1.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7900 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,900 | train | mutant | 4,952 | 126 | 5,503 | 109 | 109 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | 14 | Thioredoxin 1 | Escherichia coli (strain K12) | 1 | P0AA25 | IPR005746|IPR036249|IPR017937|IPR013766 | D105E | D105E | 1 | 1 | 0 | 0 | 105 | D | E | 3 | CONSERVATION | 2TRX|2H6X | 371|416 | null | 105 | A | H | false | false | 74.692886 | 31.97625 | 11,535 | ProTherm | 7 | fluorescence | Urea | Hepes | 5 mM | 25 | 2H6X_A:D104E | null | null | null | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 774 | ARTICLE | Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. | 2,006 | 10.1016/j.jmb.2006.07.065 | 16935299 | J Mol Biol;362;966-78 | 6 | Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Hepes","type":"BUFFER"},{"numValue":null,"strValue":"5 mM","type":"BUFFER... | [{"datasets":[],"id":39834,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39835,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39836,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":8106,"numValue":3.0,"position":105,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:7901 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,901 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 18,389 | ProTherm | 7 | CD | Thermal | Sodium phosphate | 50 mM | null | NaCl | 150 mM | 45 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 908 | ARTICLE | Surface salt bridges stabilize the GCN4 leucine zipper. | 1,998 | 10.1002/pro.5560071121 | 9828010 | Protein Sci;7;2431-7 | 4 | Lu M|Kallenbach N R|Spek E J|Bui A H | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":67845,"numValue":45.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":67846,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:7902 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,902 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 19,742 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 10 mM | null | 56.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(>95%) | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 919 | ARTICLE | The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil. | 2,000 | 10.1006/jmbi.2000.3936 | 10903875 | J Mol Biol;300;1377-87 | 4 | Zhu H|Scholtz J M|Celinski S A|Hu J C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":72579,"numValue":56.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":72580,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7903 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,903 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 20,141 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 10 mM | 60 | null | null | 6.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes(>95%) | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 919 | ARTICLE | The contribution of buried polar groups to the conformational stability of the GCN4 coiled coil. | 2,000 | 10.1006/jmbi.2000.3936 | 10903875 | J Mol Biol;300;1377-87 | 4 | Zhu H|Scholtz J M|Celinski S A|Hu J C | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":60.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":[],"id":73818,"numValue":6.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":73819,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7904 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,904 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,959 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 8.35 | null | null | null | null | null | 1.88 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79544,"numValue":8.35,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79545,"numValue":1.88,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79546,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7905 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,905 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,960 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 6.5 | null | null | null | null | null | 1.59 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79547,"numValue":6.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79548,"numValue":1.59,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79549,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7906 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,906 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,961 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 9 | null | null | null | null | null | 2 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79550,"numValue":9.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79551,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79552,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7907 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,907 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,962 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 10.4 | null | null | null | null | null | 2.09 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79553,"numValue":10.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79554,"numValue":2.09,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79555,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7908 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,908 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,963 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 9.2 | null | null | null | null | null | 2.1 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79556,"numValue":9.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79557,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79558,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7909 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,909 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,964 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 8.4 | null | null | null | null | null | 1.5 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79559,"numValue":8.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79560,"numValue":1.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79561,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7910 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,910 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,965 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 6.07 | null | null | null | null | null | 1.57 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79562,"numValue":6.07,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79563,"numValue":1.57,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79564,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7911 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,911 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,966 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 11.45 | null | null | null | null | null | 2.01 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79565,"numValue":11.45,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79566,"numValue":2.01,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79567,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7912 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,912 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,967 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 8.76 | null | null | null | null | null | 1.93 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79568,"numValue":8.76,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79569,"numValue":1.93,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79570,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7913 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,913 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,968 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 10.37 | null | null | null | null | null | 2.06 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79571,"numValue":10.37,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79572,"numValue":2.06,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79573,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:7914 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 7,914 | train | sequence | 128 | 128 | -1 | 281 | -1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | 15 | General control transcription factor GCN4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 1 | P03069 | IPR050946|IPR004827|IPR046347 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,969 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 10 | null | null | 9.22 | null | null | null | null | null | 2.03 | null | null | null | null | null | null | null | Unknown | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1551 | ARTICLE | Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. | 1,999 | 10.1021/bi982209j | 10029555 | Biochemistry;38;2601-9 | 2 | Sosnick T R|Bhattacharyya R P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":79574,"numValue":9.22,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79575,"numValue":2.03,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":79576,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] |
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