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:1555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,555 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 886 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3F | 52.25 | -1.31 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3296,"numValue":52.25,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3297,"numValue":-1.31,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3298,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,556 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 3,001 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:I3F | 37.9 | -4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","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":"2LZM_A:I3F","type":"_PDB... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":10894,"numValue":37.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":10895,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMU... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,557 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 4,660 | ProTherm | 2 | CD | Thermal | Phosphate buffer | 50 mM | null | 2LZM_A:I3F | 37.9 | -4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:I3F","type... | [{"datasets":[],"id":17232,"numValue":37.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17233,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17234,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[]... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,558 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,987 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3F | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24620,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24621,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,559 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,332 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.56 | KCl | 25 mM | 2LZM_A:I3F | null | null | null | 0.53 | null | 2.64 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.56,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":25577,"numValue":2.64,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25578,"numValue":0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25579,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,560 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,850 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.16 | KCl | 25 mM | 2LZM_A:I3F | null | null | null | 1.09 | null | 2.64 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.16,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":26852,"numValue":2.64,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26853,"numValue":1.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26854,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,561 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,034 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3F | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27383,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27384,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,562 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,214 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.75 | KCl | 25 mM | 2LZM_A:I3F | null | null | null | 1.49 | null | 2.64 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":27822,"numValue":2.64,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":27823,"numValue":1.49,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27824,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,563 | train | mutant | 438 | 41 | 484 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3F | I3F | 1 | 1 | 0 | 0 | 3 | I | F | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 13,905 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:I3F | null | null | 16.8 | null | null | null | null | 2.61 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":51461,"numValue":16.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51462,"numValue":2.61,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51463,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":51464,"numValue":null,"references":[... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,564 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 714 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3L | 44.9 | 3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2767,"numValue":44.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2768,"numValue":3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2769,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,565 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 727 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3L | 65.6 | 0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2806,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2807,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2808,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,566 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 877 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3L | 41.41 | 2.66 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3269,"numValue":41.41,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3270,"numValue":2.66,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3271,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,567 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 882 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3L | 48.91 | 2.75 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3284,"numValue":48.91,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3285,"numValue":2.75,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3286,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,568 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 887 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3L | 56.4 | 2.84 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3299,"numValue":56.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3300,"numValue":2.84,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3301,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,569 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 902 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:I3L | 55.53 | 2.11 | null | null | null | 1.8 | 132 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3341,"numValue":55.53,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3342,"numValue":2.11,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3343,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1570 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,570 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 909 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:I3L | 67.2 | 1.69 | null | null | null | 2.5 | 147 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3376,"numValue":67.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3377,"numValue":1.69,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3378,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,571 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,724 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:I3L | null | null | null | -0.7 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23894,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":23895,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23896,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,572 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,988 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3L | null | null | null | -0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24622,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24623,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,573 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,333 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.56 | KCl | 25 mM | 2LZM_A:I3L | null | null | null | -1.16 | null | 2.36 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.56,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":25580,"numValue":2.36,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25581,"numValue":-1.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25582,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,574 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,339 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:I3L | null | null | null | -0.83 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":25598,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25599,"numValue":-0.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25600,"numValue":null,"references":[],"strValue":"Unknown","typ... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,575 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,851 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.16 | KCl | 25 mM | 2LZM_A:I3L | null | null | null | -1.01 | null | 2.36 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.16,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":26855,"numValue":2.36,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26856,"numValue":-1.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26857,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,576 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,035 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3L | null | null | null | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27385,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27386,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,577 | train | mutant | 439 | 41 | 485 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3L | I3L | 1 | 1 | 0 | 0 | 3 | I | L | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,215 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.75 | KCl | 25 mM | 2LZM_A:I3L | null | null | null | -0.85 | null | 2.36 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":27825,"numValue":2.36,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27826,"numValue":-0.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27827,"numValue":null,"references":[],"strValue":"yes","type":... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,578 | train | mutant | 440 | 41 | 486 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3V | I3V | 1 | 1 | 0 | 0 | 3 | I | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 715 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3V | 39.8 | -2.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|EASE-MM_S1676.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2770,"numValue":39.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2771,"numValue":-2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S1676.csv","PON-TStab_dataset.csv"],"id":2772,"numValue":null,"references":[],"strV... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,579 | train | mutant | 440 | 41 | 486 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3V | I3V | 1 | 1 | 0 | 0 | 3 | I | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 728 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3V | 63.5 | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2809,"numValue":63.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2810,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2811,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,580 | train | mutant | 440 | 41 | 486 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3V | I3V | 1 | 1 | 0 | 0 | 3 | I | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 3,000 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:I3V | 39.8 | -2.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|STRUM_Q306.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","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":"2LZM_A:I3V","type":"_PDB... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":10891,"numValue":39.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":10892,"numValue":-2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMU... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,582 | train | mutant | 440 | 41 | 486 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3V | I3V | 1 | 1 | 0 | 0 | 3 | I | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,989 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3V | null | null | null | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24624,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24625,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,583 | train | mutant | 440 | 41 | 486 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3V | I3V | 1 | 1 | 0 | 0 | 3 | I | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,036 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3V | null | null | null | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":27387,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27388,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,585 | train | mutant | 441 | 41 | 487 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3M | I3M | 1 | 1 | 0 | 0 | 3 | I | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 716 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3M | 41 | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2773,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2774,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2775,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,586 | train | mutant | 441 | 41 | 487 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3M | I3M | 1 | 1 | 0 | 0 | 3 | I | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 729 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3M | 62.4 | -2.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2812,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2813,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2814,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,587 | train | mutant | 441 | 41 | 487 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3M | I3M | 1 | 1 | 0 | 0 | 3 | I | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,990 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3M | null | null | null | 0.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":24626,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24627,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,588 | train | mutant | 441 | 41 | 487 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3M | I3M | 1 | 1 | 0 | 0 | 3 | I | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,037 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3M | null | null | null | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27389,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27390,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,589 | train | mutant | 442 | 41 | 488 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C | I3C | 1 | 1 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 717 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3C | 40 | -1.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2776,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2777,"numValue":-1.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2778,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,590 | train | mutant | 442 | 41 | 488 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C | I3C | 1 | 1 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 730 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3C | 61 | -3.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2815,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2816,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2817,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,591 | train | mutant | 442 | 41 | 488 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C | I3C | 1 | 1 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,991 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3C | null | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":24628,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24629,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,592 | train | mutant | 442 | 41 | 488 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C | I3C | 1 | 1 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,992 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3C | null | null | null | -1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":24630,"numValue":-1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24631,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,593 | train | mutant | 442 | 41 | 488 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C | I3C | 1 | 1 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,038 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3C | null | null | null | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":27391,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27392,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,595 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 718 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3A | 38.1 | -3.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2779,"numValue":38.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2780,"numValue":-3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2781,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,596 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 731 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3A | 68 | 3.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2818,"numValue":68.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2819,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2820,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,597 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 732 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3A | 62.9 | -1.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2821,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2822,"numValue":-1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2823,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,598 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 3,002 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:I3A | 38.1 | -3.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","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":"2LZM_A:I3A","type":"_PDB... | [{"datasets":[],"id":10897,"numValue":38.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10898,"numValue":-3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10899,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,599 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 4,661 | ProTherm | 2 | CD | Thermal | Phosphate buffer | 50 mM | null | 2LZM_A:I3A | 38.1 | -3.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:I3A","type... | [{"datasets":[],"id":17236,"numValue":38.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17237,"numValue":-3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17238,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[]... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,600 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,993 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3A | null | null | null | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24632,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24633,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,601 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,040 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3A | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":27395,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27396,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,602 | train | mutant | 443 | 41 | 489 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3A | I3A | 1 | 1 | 0 | 0 | 3 | I | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 13,906 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:I3A | null | null | 15.7 | null | null | null | null | 2.52 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":51465,"numValue":15.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51466,"numValue":2.52,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51467,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":51468,"numValue":null,"references":[... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1603 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,603 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 719 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3T | 35.8 | -6.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2782,"numValue":35.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2783,"numValue":-6.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2784,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,604 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 733 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3T | 58.7 | -6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2824,"numValue":58.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2825,"numValue":-6.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2826,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,605 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 879 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3T | 30.27 | -8.48 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3275,"numValue":30.27,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3276,"numValue":-8.48,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3277,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,606 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 884 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3T | 39.76 | -6.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3290,"numValue":39.76,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3291,"numValue":-6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3292,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,607 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 889 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3T | 49.24 | -4.32 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3305,"numValue":49.24,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3306,"numValue":-4.32,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3307,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,608 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,994 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3T | null | null | null | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24634,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24635,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,609 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,335 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.56 | KCl | 25 mM | 2LZM_A:I3T | null | null | null | 1.81 | null | 2.98 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.56,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":25586,"numValue":2.98,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25587,"numValue":1.81,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25588,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,610 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,853 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.16 | KCl | 25 mM | 2LZM_A:I3T | null | null | null | 2.28 | null | 2.98 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.16,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":26861,"numValue":2.98,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26862,"numValue":2.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26863,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,612 | train | mutant | 444 | 41 | 490 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3T | I3T | 1 | 1 | 0 | 0 | 3 | I | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,217 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.75 | KCl | 25 mM | 2LZM_A:I3T | null | null | null | 2.45 | null | 2.98 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":27831,"numValue":2.98,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":27832,"numValue":2.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27833,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,613 | train | mutant | 445 | 41 | 491 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3S | I3S | 1 | 1 | 0 | 0 | 3 | I | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 720 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3S | 34.9 | -7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2785,"numValue":34.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2786,"numValue":-7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2787,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,614 | train | mutant | 445 | 41 | 491 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3S | I3S | 1 | 1 | 0 | 0 | 3 | I | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 734 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3S | 60.1 | -4.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2827,"numValue":60.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2828,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2829,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,616 | train | mutant | 445 | 41 | 491 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3S | I3S | 1 | 1 | 0 | 0 | 3 | I | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,042 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3S | null | null | null | 1.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27399,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27400,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,617 | train | mutant | 446 | 41 | 492 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3G | I3G | 1 | 1 | 0 | 0 | 3 | I | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 721 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3G | 34.7 | -7.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2788,"numValue":34.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2789,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2790,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,618 | train | mutant | 446 | 41 | 492 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3G | I3G | 1 | 1 | 0 | 0 | 3 | I | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 735 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3G | 58.9 | -5.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|EASE-MM_S238.csv|PON-TStab_dataset.csv|Saraboji_S1791.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2830,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","EASE-MM_S238.csv","PON-TStab_dataset.csv","Saraboji_S1791.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":2831,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2832,"n... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,619 | train | mutant | 446 | 41 | 492 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3G | I3G | 1 | 1 | 0 | 0 | 3 | I | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 3,003 | ProTherm | 2 | CD | Thermal | phosphate | 50 mM | null | 2LZM_A:I3G | 34.7 | -7.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 267 | ARTICLE | Purification and molecular properties of rabbit lung indolamine N-methyltransferase. | 1,982 | 10.1021/bi00535a054 | 7074100 | Biochemistry;21;1464-70 | 4 | Irace G|Colonna G|Camardella M|Della Pietra G | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","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":"2LZM_A:I3G","type":"_PDB... | [{"datasets":[],"id":10900,"numValue":34.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10901,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10902,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,620 | train | mutant | 446 | 41 | 492 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3G | I3G | 1 | 1 | 0 | 0 | 3 | I | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 4,662 | ProTherm | 2 | CD | Thermal | Phosphate buffer | 50 mM | null | 2LZM_A:I3G | 34.7 | -7.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:I3G","type... | [{"datasets":[],"id":17240,"numValue":34.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17241,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17242,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[]... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,621 | train | mutant | 446 | 41 | 492 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3G | I3G | 1 | 1 | 0 | 0 | 3 | I | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,996 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3G | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24638,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24639,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,622 | train | mutant | 446 | 41 | 492 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3G | I3G | 1 | 1 | 0 | 0 | 3 | I | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,043 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3G | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27401,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27402,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,623 | train | mutant | 446 | 41 | 492 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3G | I3G | 1 | 1 | 0 | 0 | 3 | I | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 13,907 | ProTherm | 5.7 | CD | GdnHCl | Phosphate buffer | 50 mM | 12 | 2LZM_A:I3G | null | null | 15.9 | null | null | null | null | 2.34 | null | null | null | null | null | null | null | null | yes | 2.0 | DG|CM|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 457 | ARTICLE | Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. | 1,992 | 10.1021/bi00120a025 | 1737005 | Biochemistry;31;1464-76 | 4 | Nicholson H|Baase W A|Schellman J A|Chen B L | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":12.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Phosphate buffer","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BU... | [{"datasets":[],"id":51469,"numValue":15.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51470,"numValue":2.34,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":51471,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":51472,"numValue":null,"references":[... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,624 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 722 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3E | 37.8 | -4.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2791,"numValue":37.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2792,"numValue":-4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2793,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,625 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 736 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3E | 59 | -5.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2833,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2834,"numValue":-5.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2835,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,626 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 875 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3E | 33.06 | -5.69 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3263,"numValue":33.06,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3264,"numValue":-5.69,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3265,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,627 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 880 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3E | 41.48 | -4.68 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3278,"numValue":41.48,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3279,"numValue":-4.68,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3280,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,628 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 885 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3E | 49.9 | -3.66 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3293,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3294,"numValue":-3.66,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3295,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,629 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,997 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3E | null | null | null | 2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":24640,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24641,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,630 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,331 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.56 | KCl | 25 mM | 2LZM_A:I3E | null | null | null | 1.53 | null | 2.61 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.56,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":25574,"numValue":2.61,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25575,"numValue":1.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25576,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,631 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,849 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.16 | KCl | 25 mM | 2LZM_A:I3E | null | null | null | 1.71 | null | 2.61 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.16,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":26849,"numValue":2.61,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26850,"numValue":1.71,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26851,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,633 | train | mutant | 447 | 41 | 493 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3E | I3E | 1 | 1 | 0 | 0 | 3 | I | E | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,213 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.75 | KCl | 25 mM | 2LZM_A:I3E | null | null | null | 1.77 | null | 2.61 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":27819,"numValue":2.61,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":27820,"numValue":1.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27821,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,634 | train | mutant | 448 | 41 | 494 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3D | I3D | 1 | 1 | 0 | 0 | 3 | I | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 723 | ProTherm | 2 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3D | 35.4 | -6.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2794,"numValue":35.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2795,"numValue":-6.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2796,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,635 | train | mutant | 448 | 41 | 494 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3D | I3D | 1 | 1 | 0 | 0 | 3 | I | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 737 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:I3D | 56.2 | -8.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":2836,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2837,"numValue":-8.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2838,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,636 | train | mutant | 448 | 41 | 494 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3D | I3D | 1 | 1 | 0 | 0 | 3 | I | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 6,998 | ProTherm | 6.5 | CD | Thermal | Unknown | 64.7 | KCl | 0.2 M | 2LZM_A:I3D | null | null | null | 3.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv"],"id":24642,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24643,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,637 | train | mutant | 448 | 41 | 494 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3D | I3D | 1 | 1 | 0 | 0 | 3 | I | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,045 | ProTherm | 2 | CD | Thermal | Unknown | 41.9 | KCl | 0.2 M | 2LZM_A:I3D | null | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 80 | ARTICLE | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. | 1,988 | 10.1038/334406a0 | 3405287 | Nature;334;406-10 | 3 | Matthews B W|Matsumura M|Becktel W J | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27405,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27406,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,638 | train | mutant | 526 | 41 | 577 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3P | I3P | 1 | 1 | 0 | 0 | 3 | I | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 878 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3P | 26.76 | -11.99 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3272,"numValue":26.76,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3273,"numValue":-11.99,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3274,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,639 | train | mutant | 526 | 41 | 577 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3P | I3P | 1 | 1 | 0 | 0 | 3 | I | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 883 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3P | 36.96 | -9.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3287,"numValue":36.96,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3288,"numValue":-9.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3289,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,640 | train | mutant | 526 | 41 | 577 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3P | I3P | 1 | 1 | 0 | 0 | 3 | I | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 888 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I3P | 47.15 | -6.41 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3302,"numValue":47.15,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3303,"numValue":-6.41,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3304,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,641 | train | mutant | 526 | 41 | 577 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3P | I3P | 1 | 1 | 0 | 0 | 3 | I | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,334 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.56 | KCl | 25 mM | 2LZM_A:I3P | null | null | null | 2.53 | null | 3.7 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.56,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":25583,"numValue":3.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25584,"numValue":2.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25585,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1642 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,642 | train | mutant | 526 | 41 | 577 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3P | I3P | 1 | 1 | 0 | 0 | 3 | I | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 7,852 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.16 | KCl | 25 mM | 2LZM_A:I3P | null | null | null | 2.97 | null | 3.7 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":46.16,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":26858,"numValue":3.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26859,"numValue":2.97,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26860,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1643 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,643 | train | mutant | 526 | 41 | 577 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3P | I3P | 1 | 1 | 0 | 0 | 3 | I | P | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3 | A | H | false | false | 23.168173 | 12.4025 | 8,216 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.75 | KCl | 25 mM | 2LZM_A:I3P | null | null | null | 2.96 | null | 3.7 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 95 | ARTICLE | A differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00159a009 | 1420185 | Biochemistry;31;10699-702 | 3 | Sturtevant J M|Hu C Q|Ladbury J E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","typ... | [{"datasets":[],"id":27828,"numValue":3.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":27829,"numValue":2.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27830,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,645 | train | mutant | 6,774 | 41 | 7,416 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L | S38D|A82P|N144D|I3L | 4 | 4 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|82|144 | A | H|L|T | false | false | 65.83708 | 22.326677 | 14,567 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:N144D | 71.89 | 5.38 | null | null | null | 2.5 | 154 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53859,"numValue":71.89,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53860,"numValue":5.38,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53861,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53862,"numValue":154.0,"references":... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,646 | train | mutant | 6,774 | 41 | 7,416 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L | S38D|A82P|N144D|I3L | 4 | 4 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|82|144 | A | H|L|T | false | false | 65.83708 | 22.326677 | 14,898 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:N144D | null | null | null | -2.32 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54934,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54935,"numValue":-2.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54936,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,647 | train | mutant | 6,774 | 41 | 7,416 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L | S38D|A82P|N144D|I3L | 4 | 4 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|82|144 | A | H|L|T | false | false | 65.83708 | 22.326677 | 14,979 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:N144D | null | null | null | -1.95 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":55135,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55136,"numValue":-1.95,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55137,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,648 | train | mutant | 6,775 | 41 | 7,417 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A | S38D|A82P|N144D|I3L|V131A | 5 | 5 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|82|131|144 | A | H|L|T | true | false | 71.579245 | 21.77377 | 14,561 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | 58.98 | 5.56 | null | null | null | 1.8 | 140 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53829,"numValue":58.98,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53830,"numValue":5.56,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53831,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53832,"numValue":140.0,"references":... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1649 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,649 | train | mutant | 6,775 | 41 | 7,417 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A | S38D|A82P|N144D|I3L|V131A | 5 | 5 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|82|131|144 | A | H|L|T | true | false | 71.579245 | 21.77377 | 14,568 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | 72.57 | 6.06 | null | null | null | 2.5 | 150 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53864,"numValue":72.57,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53865,"numValue":6.06,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53866,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53867,"numValue":150.0,"references":... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1650 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,650 | train | mutant | 6,775 | 41 | 7,417 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A | S38D|A82P|N144D|I3L|V131A | 5 | 5 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|82|131|144 | A | H|L|T | true | false | 71.579245 | 21.77377 | 14,899 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | null | null | null | -2.57 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54937,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54938,"numValue":-2.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54939,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1651 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,651 | train | mutant | 6,775 | 41 | 7,417 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A | S38D|A82P|N144D|I3L|V131A | 5 | 5 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|82|131|144 | A | H|L|T | true | false | 71.579245 | 21.77377 | 14,980 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | null | null | null | -2.25 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":55138,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55139,"numValue":-2.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55140,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1652 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,652 | train | mutant | 6,776 | 41 | 7,418 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V | S38D|A82P|N144D|I3L|V131A|A41V | 6 | 6 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|131|144 | A | H|L|T | true | false | 66.106012 | 22.772642 | 14,562 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | 59.92 | 6.5 | null | null | null | 1.8 | 139 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53834,"numValue":59.92,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53835,"numValue":6.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53836,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53837,"numValue":139.0,"references":[... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1653 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,653 | train | mutant | 6,776 | 41 | 7,418 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V | S38D|A82P|N144D|I3L|V131A|A41V | 6 | 6 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|131|144 | A | H|L|T | true | false | 66.106012 | 22.772642 | 14,569 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | 73.42 | 6.91 | null | null | null | 2.5 | 145 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53869,"numValue":73.42,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53870,"numValue":6.91,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53871,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53872,"numValue":145.0,"references":... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1654 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,654 | train | mutant | 6,776 | 41 | 7,418 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V | S38D|A82P|N144D|I3L|V131A|A41V | 6 | 6 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|131|144 | A | H|L|T | true | false | 66.106012 | 22.772642 | 14,900 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | null | null | null | -2.87 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54940,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54941,"numValue":-2.87,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54942,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1655 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,655 | train | mutant | 6,776 | 41 | 7,418 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V | S38D|A82P|N144D|I3L|V131A|A41V | 6 | 6 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|131|144 | A | H|L|T | true | false | 66.106012 | 22.772642 | 14,981 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:V131A 2LZM_A:N144D | null | null | null | -2.62 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":55141,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55142,"numValue":-2.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55143,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,656 | train | mutant | 6,777 | 41 | 7,419 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V|N116D | S38D|A82P|N144D|I3L|V131A|A41V|N116D | 7 | 7 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|116|131|144 | A | H|L|T | true | false | 68.067731 | 23.040032 | 14,563 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:N116D 2LZM_A:V131A 2LZM_A:N144D | 60.68 | 7.26 | null | null | null | 1.8 | 139 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53839,"numValue":60.68,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53840,"numValue":7.26,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53841,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53842,"numValue":139.0,"references":... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,657 | train | mutant | 6,777 | 41 | 7,419 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V|N116D | S38D|A82P|N144D|I3L|V131A|A41V|N116D | 7 | 7 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|116|131|144 | A | H|L|T | true | false | 68.067731 | 23.040032 | 14,570 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:N116D 2LZM_A:V131A 2LZM_A:N144D | 74.83 | 8.32 | null | null | null | 2.5 | 156 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53874,"numValue":74.83,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53875,"numValue":8.32,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53876,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53877,"numValue":156.0,"references":... | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1658 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,658 | train | mutant | 6,777 | 41 | 7,419 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V|N116D | S38D|A82P|N144D|I3L|V131A|A41V|N116D | 7 | 7 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|116|131|144 | A | H|L|T | true | false | 68.067731 | 23.040032 | 14,901 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:N116D 2LZM_A:V131A 2LZM_A:N144D | null | null | null | -3.57 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54943,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54944,"numValue":-3.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54945,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,659 | train | mutant | 6,777 | 41 | 7,419 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S38D|A82P|N144D|I3L|V131A|A41V|N116D | S38D|A82P|N144D|I3L|V131A|A41V|N116D | 7 | 7 | 0 | 0 | 38 | S | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|38|41|82|116|131|144 | A | H|L|T | true | false | 68.067731 | 23.040032 | 14,982 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:I3L 2LZM_A:S38D 2LZM_A:A41V 2LZM_A:A82P 2LZM_A:N116D 2LZM_A:V131A 2LZM_A:N144D | null | null | null | -2.92 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":55144,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55145,"numValue":-2.92,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55146,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6829,"numValue":6.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6832,"numValue":4.0,"position":41,"positionArray":null,"positionRange":n... | |||||||||||
fireprotdb:1660 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,660 | train | mutant | 6,858 | 41 | 7,500 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C|C54V | I3C|C54V | 2 | 2 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|54 | A | H|L | true | false | 14.680993 | 20.872738 | 14,688 | ProTherm | 6.8 | Fluorescence | Thermal | cacodylate | 50 mM | null | NaCl | 0.2 M | 2LZM_A:I3C 2LZM_A:C54V | 41 | 2.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 906 | ARTICLE | Effect of an engineered disulfide bond on the folding of T4 lysozyme at low temperatures. | 1,990 | 10.1021/bi00465a026 | 2334694 | Biochemistry;29;3331-7 | 4 | Wetzel R|Perry L J|Fink A L|Anderson W D | [{"numValue":6.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"cacodylate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":... | [{"datasets":[],"id":54324,"numValue":41.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54325,"numValue":2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54326,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1661 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,661 | train | mutant | 7,102 | 41 | 7,755 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I3C|C54T | I3C|C54T | 2 | 2 | 0 | 0 | 3 | I | C | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 3|54 | A | H|L | true | false | 14.680993 | 20.872738 | 15,316 | ProTherm | 5 | CD | GdnHCl | Sodium phosphate | 2 mM | 25 | 2LZM_A:I3C 2LZM_A:C54T | null | null | 12.9 | null | null | null | null | 2.94 | null | null | null | null | null | null | null | null | yes | DG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 925 | ARTICLE | Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies. | 1,989 | 10.1021/bi00428a041 | 2653427 | Biochemistry;28;685-91 | 2 | Schellman J A|Chen B L | [{"numValue":5.0,"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":"2 mM","type":"BUF... | [{"datasets":[],"id":56210,"numValue":12.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":56211,"numValue":2.94,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56212,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6794,"numValue":7.0,"position":3,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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