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:1988 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,988 | train | mutant | 6,770 | 41 | 7,412 | 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 | C54T|C97A | C54T|C97A | 2 | 2 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54|97 | A | L|H | true | false | 9.462741 | 20.324071 | 14,556 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:C54T 2LZM_A:C97A | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"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":53807,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53808,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6888,"numValue":5.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1989 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,989 | train | mutant | 6,770 | 41 | 7,412 | 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 | C54T|C97A | C54T|C97A | 2 | 2 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54|97 | A | L|H | true | false | 9.462741 | 20.324071 | 14,975 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:C54T 2LZM_A:C97A | null | null | null | 1.27 | null | 3.2 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.6,"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","type... | [{"datasets":[],"id":55123,"numValue":3.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55124,"numValue":1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55125,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6888,"numValue":5.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1991 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,991 | train | mutant | 6,770 | 41 | 7,412 | 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 | C54T|C97A | C54T|C97A | 2 | 2 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54|97 | A | L|H | true | false | 9.462741 | 20.324071 | 15,118 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:C54T 2LZM_A:C97A | null | null | null | 0.34 | null | 3.2 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.8,"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","type... | [{"datasets":[],"id":55467,"numValue":3.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55468,"numValue":0.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55469,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6888,"numValue":5.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1992 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,992 | train | mutant | 432 | 41 | 478 | 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 | N55G | N55G | 1 | 1 | 0 | 0 | 55 | N | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 55 | A | T | true | false | 117.271405 | 45.65125 | 703 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 2LZM_A:N55G | 40.2 | -1.7 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":2732,"numValue":40.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2733,"numValue":-1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2734,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1993 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,993 | train | mutant | 432 | 41 | 478 | 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 | N55G | N55G | 1 | 1 | 0 | 0 | 55 | N | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 55 | A | T | true | false | 117.271405 | 45.65125 | 705 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 2LZM_A:N55G | 63.1 | -1.6 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":2738,"numValue":63.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2739,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2740,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1994 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,994 | train | mutant | 432 | 41 | 478 | 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 | N55G | N55G | 1 | 1 | 0 | 0 | 55 | N | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 55 | A | T | true | false | 117.271405 | 45.65125 | 6,983 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | 64.7 | KCl | 100 mM | 2LZM_A:N55G | null | null | null | 0.6 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"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":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24612,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24613,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1995 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,995 | train | mutant | 432 | 41 | 478 | 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 | N55G | N55G | 1 | 1 | 0 | 0 | 55 | N | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 55 | A | T | true | false | 117.271405 | 45.65125 | 8,031 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | 41.9 | KCl | 100 mM | 2LZM_A:N55G | null | null | null | 0.5 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"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":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27377,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27378,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1996 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,996 | train | mutant | 1,879 | 41 | 2,107 | 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 | N55C | N55C | 1 | 1 | 0 | 0 | 55 | N | C | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 55 | A | T | true | false | 117.271405 | 45.65125 | 3,623 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:N55C | 32.8 | -3.6 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 338 | ARTICLE | Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. | 1,992 | 10.1021/bi00149a004 | 1510962 | Biochemistry;31;7765-72 | 4 | Lu J|Baase W A|Dahlquist F W|Muchmore D C | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13320,"numValue":32.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":13321,"numValue":-3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMU... | [{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1997 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,997 | train | mutant | 203 | 41 | 232 | 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 | I58T | I58T | 1 | 1 | 0 | 0 | 58 | I | T | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 58 | A | L | false | false | 4.479108 | 21.615625 | 384 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | null | NaCl | 0.10 M | 2LZM_A:I58T | 55.2 | -10.1 | null | null | null | null | 84 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.010 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":1579,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1580,"numValue":-10.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1581,"numValue":84.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6849,"numValue":8.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1998 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,998 | train | mutant | 203 | 41 | 232 | 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 | I58T | I58T | 1 | 1 | 0 | 0 | 58 | I | T | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 58 | A | L | false | false | 4.479108 | 21.615625 | 7,117 | ProTherm | 5.4 | CD | Thermal | sodium acetate | 0.010 M | 59 | NaCl | 0.10 M | 2LZM_A:I58T | null | null | null | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 41 | ARTICLE | Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme. | 2,001 | 10.1110/ps.02101 | 11316887 | Protein Sci;10;1067-78 | 5 | Xu J|Baase W A|Baldwin E P|Matthews B W|Quillin M L | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":59.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.010 M","type":"B... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24967,"numValue":3.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24968,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6849,"numValue":8.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1999 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,999 | train | mutant | 1,676 | 41 | 1,885 | 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 | I58A | I58A | 1 | 1 | 0 | 0 | 58 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 58 | A | L | false | false | 4.479108 | 21.615625 | 3,128 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I58A | 41.3 | -10.4 | null | null | null | 1.8 | 80 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11392,"numValue":41.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11393,"numValue":-10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.c... | [{"id":6849,"numValue":8.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2000 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,000 | train | mutant | 1,676 | 41 | 1,885 | 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 | I58A | I58A | 1 | 1 | 0 | 0 | 58 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 58 | A | L | false | false | 4.479108 | 21.615625 | 7,562 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:I58A | null | null | null | 3.2 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26159,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26160,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26161,"numV... | [{"id":6849,"numValue":8.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2002 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,002 | train | mutant | 578 | 41 | 629 | 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 | T59N | T59N | 1 | 1 | 0 | 0 | 59 | T | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 978 | ProTherm | 2 | CD | Thermal | KCl-HCl | null | KCl | 15 mM | 2LZM_A:T59N | 38.9 | -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 | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KCl-HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"15 mM","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3673,"numValue":38.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3674,"numValue":-2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3675,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2003 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,003 | train | mutant | 578 | 41 | 629 | 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 | T59N | T59N | 1 | 1 | 0 | 0 | 59 | T | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 984 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 15 mM | 2LZM_A:T59N | 60.2 | -2.8 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3691,"numValue":60.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3692,"numValue":-2.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3693,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2004 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,004 | train | mutant | 578 | 41 | 629 | 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 | T59N | T59N | 1 | 1 | 0 | 0 | 59 | T | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 7,041 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 15 mM | 2LZM_A:T59N | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":24749,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24750,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2005 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,005 | train | mutant | 578 | 41 | 629 | 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 | T59N | T59N | 1 | 1 | 0 | 0 | 59 | T | N | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 8,057 | ProTherm | 2 | CD | Thermal | HCl | 41 | KCl | 15 mM | 2LZM_A:T59N | null | null | null | 0.6 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27429,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27430,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2007 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,007 | train | mutant | 579 | 41 | 630 | 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 | T59S | T59S | 1 | 1 | 0 | 0 | 59 | T | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 985 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 15 mM | 2LZM_A:T59S | 62.6 | -0.4 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3694,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3695,"numValue":-0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3696,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2008 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,008 | train | mutant | 579 | 41 | 630 | 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 | T59S | T59S | 1 | 1 | 0 | 0 | 59 | T | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 7,042 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 15 mM | 2LZM_A:T59S | null | null | null | 0.2 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24751,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24752,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2009 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,009 | train | mutant | 579 | 41 | 630 | 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 | T59S | T59S | 1 | 1 | 0 | 0 | 59 | T | S | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 8,058 | ProTherm | 2 | CD | Thermal | HCl | 41 | KCl | 15 mM | 2LZM_A:T59S | null | null | null | 0.7 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv"],"id":27431,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27432,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2011 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,011 | train | mutant | 580 | 41 | 631 | 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 | T59D | T59D | 1 | 1 | 0 | 0 | 59 | T | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 986 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 15 mM | 2LZM_A:T59D | 59.9 | -3.1 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3697,"numValue":59.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3698,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3699,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2012 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,012 | train | mutant | 580 | 41 | 631 | 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 | T59D | T59D | 1 | 1 | 0 | 0 | 59 | T | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 7,043 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 15 mM | 2LZM_A:T59D | null | null | null | 1.2 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":24753,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24754,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2013 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,013 | train | mutant | 580 | 41 | 631 | 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 | T59D | T59D | 1 | 1 | 0 | 0 | 59 | T | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 8,059 | ProTherm | 2 | CD | Thermal | HCl | 41 | KCl | 15 mM | 2LZM_A:T59D | null | null | null | 0.9 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27433,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27434,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2015 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,015 | train | mutant | 581 | 41 | 632 | 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 | T59G | T59G | 1 | 1 | 0 | 0 | 59 | T | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 987 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 15 mM | 2LZM_A:T59G | 58.9 | -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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3700,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3701,"numValue":-4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3702,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2017 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,017 | train | mutant | 581 | 41 | 632 | 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 | T59G | T59G | 1 | 1 | 0 | 0 | 59 | T | G | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 8,060 | ProTherm | 2 | CD | Thermal | HCl | 41 | KCl | 15 mM | 2LZM_A:T59G | null | null | null | 2.2 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv"],"id":27435,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27436,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2018 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,018 | train | mutant | 582 | 41 | 633 | 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 | T59V | T59V | 1 | 1 | 0 | 0 | 59 | T | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 982 | ProTherm | 2 | CD | Thermal | KCl-HCl | null | KCl | 15 mM | 2LZM_A:T59V | 31 | -10 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KCl-HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"15 mM","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3685,"numValue":31.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3686,"numValue":-10.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":3687,"numValue":null,"ref... | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2020 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,020 | train | mutant | 582 | 41 | 633 | 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 | T59V | T59V | 1 | 1 | 0 | 0 | 59 | T | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 7,045 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 15 mM | 2LZM_A:T59V | null | null | null | 1.5 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24757,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24758,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2021 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,021 | train | mutant | 582 | 41 | 633 | 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 | T59V | T59V | 1 | 1 | 0 | 0 | 59 | T | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 8,061 | ProTherm | 2 | CD | Thermal | HCl | 41 | KCl | 15 mM | 2LZM_A:T59V | null | null | null | 2.8 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv"],"id":27437,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27438,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2022 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,022 | train | mutant | 583 | 41 | 634 | 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 | T59A | T59A | 1 | 1 | 0 | 0 | 59 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 983 | ProTherm | 2 | CD | Thermal | KCl-HCl | null | KCl | 15 mM | 2LZM_A:T59A | 30.9 | -10.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KCl-HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"15 mM","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3688,"numValue":30.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3689,"numValue":-10.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":3690,"numValue":null,"ref... | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2023 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,023 | train | mutant | 583 | 41 | 634 | 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 | T59A | T59A | 1 | 1 | 0 | 0 | 59 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 989 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 15 mM | 2LZM_A:T59A | 59 | -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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3706,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3707,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3708,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2024 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,024 | train | mutant | 583 | 41 | 634 | 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 | T59A | T59A | 1 | 1 | 0 | 0 | 59 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 7,046 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 15 mM | 2LZM_A:T59A | null | null | null | 1.5 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24759,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24760,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2025 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,025 | train | mutant | 583 | 41 | 634 | 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 | T59A | T59A | 1 | 1 | 0 | 0 | 59 | T | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 59 | A | L | false | false | 68.273436 | 24.805714 | 8,062 | ProTherm | 2 | CD | Thermal | HCl | 41 | KCl | 15 mM | 2LZM_A:T59A | null | null | null | 2.8 | 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 | 101 | ARTICLE | Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. | 1,992 | 10.1021/bi00129a006 | 1567817 | Biochemistry;31;3590-6 | 5 | Baase W A|Matthews B W|Sauer U|Becktel W J|Bell J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv"],"id":27439,"numValue":2.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27440,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6850,"numValue":7.0,"position":59,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2026 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,026 | train | mutant | 479 | 41 | 528 | 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 | K60P | K60P | 1 | 1 | 0 | 0 | 60 | K | P | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 60 | A | H | false | false | 105.094917 | 38.103889 | 785 | ProTherm | 2 | CD | Thermal | H3PO4,HCl, | 10 mM,10 mM, | null | KCl | 0.2 M | 2LZM_A:K60P | 42.2 | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,HCl,","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":2994,"numValue":42.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":2995,"numValue":0.3,"references":[],"strValue":null,"type... | [{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2027 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,027 | train | mutant | 479 | 41 | 528 | 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 | K60P | K60P | 1 | 1 | 0 | 0 | 60 | K | P | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 60 | A | H | false | false | 105.094917 | 38.103889 | 790 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:K60P | 64.6 | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":3013,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":3014,"numValue":-0.1,"references":[],"strValue":null,"typ... | [{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2029 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,029 | train | mutant | 479 | 41 | 528 | 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 | K60P | K60P | 1 | 1 | 0 | 0 | 60 | K | P | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 60 | A | H | false | false | 105.094917 | 38.103889 | 8,046 | ProTherm | 2 | CD | Thermal | H3PO4,HCl | 10 mM,10 mM | 41.9 | KCl | 0.2 M | 2LZM_A:K60P | null | null | null | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"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":"H3PO4,HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27407,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27408,"numValue":null,"references":[],"strValue":"yes","type":... | [{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2030 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,030 | train | mutant | 1,775 | 41 | 1,988 | 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 | K60H | K60H | 1 | 1 | 0 | 0 | 60 | K | H | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 60 | A | H | false | false | 105.094917 | 38.103889 | 3,413 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:K60H | 35.1 | -3.4 | null | null | null | null | 75 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":12591,"numValue":35.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12592,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12593,"numValue":75.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2031 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,031 | train | mutant | 1,775 | 41 | 1,988 | 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 | K60H | K60H | 1 | 1 | 0 | 0 | 60 | K | H | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 60 | A | H | false | false | 105.094917 | 38.103889 | 3,414 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:K60H | 62.6 | -0.4 | null | null | null | null | 115 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | Broom_S605.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["Broom_S605.csv"],"id":12595,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Broom_S605.csv","Saraboji_S1791.csv"],"id":12596,"numValue":-0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv"],"id":12597,"numValue":115.0,"references... | [{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2032 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,032 | train | mutant | 1,775 | 41 | 1,988 | 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 | K60H | K60H | 1 | 1 | 0 | 0 | 60 | K | H | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 60 | A | H | false | false | 105.094917 | 38.103889 | 7,038 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63 | KCl | 0.15 M | 2LZM_A:K60H | null | null | null | 0.1 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24743,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24744,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2033 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,033 | train | mutant | 1,775 | 41 | 1,988 | 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 | K60H | K60H | 1 | 1 | 0 | 0 | 60 | K | H | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 60 | A | H | false | false | 105.094917 | 38.103889 | 8,425 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 28.5 | KCl | 0.15 M | 2LZM_A:K60H | null | null | null | 0.8 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":28.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":["capriotti_S1615_map.csv"],"id":28652,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":28653,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6851,"numValue":1.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2034 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,034 | train | mutant | 1,127 | 41 | 1,271 | 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 | L66A | L66A | 1 | 1 | 0 | 0 | 66 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 2,021 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L66A | 55.2 | -10.1 | null | null | null | null | 84 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv|STRUM_Q3421.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","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":... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7547,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2035 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,035 | train | mutant | 1,127 | 41 | 1,271 | 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 | L66A | L66A | 1 | 1 | 0 | 0 | 66 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 3,143 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L66A | 38.3 | -13.4 | null | null | null | 1.8 | 69 | 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 | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11467,"numValue":38.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11468,"numValue":-13.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11469,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2036 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,036 | train | mutant | 1,127 | 41 | 1,271 | 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 | L66A | L66A | 1 | 1 | 0 | 0 | 66 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 6,788 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:L66A | null | null | null | 3.3 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24066,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24067,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24068,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2037 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,037 | train | mutant | 1,127 | 41 | 1,271 | 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 | L66A | L66A | 1 | 1 | 0 | 0 | 66 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 7,577 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:L66A | null | null | null | 3.9 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26204,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26205,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26206,"numV... | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2038 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,038 | train | mutant | 1,141 | 41 | 1,285 | 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 | L66M | L66M | 1 | 1 | 0 | 0 | 66 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 2,041 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L66M | 62.6 | -2.5 | null | null | null | null | 122 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","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":... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q306.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":7647,"numValue":62.6,"references":[],"strValue":null,"ty... | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2039 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,039 | train | mutant | 1,141 | 41 | 1,285 | 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 | L66M | L66M | 1 | 1 | 0 | 0 | 66 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 6,808 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:L66M | null | null | null | 1 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24126,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24127,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24128,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2040 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,040 | train | mutant | 2,067 | 41 | 2,307 | 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 | L66P | L66P | 1 | 1 | 0 | 0 | 66 | L | P | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 4,056 | ProTherm | 7 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:L66P | 26.8 | -38.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 374 | ARTICLE | Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. | 1,996 | 10.1002/pro.5560050419 | 8845764 | Protein Sci;5;742-51 | 5 | Blankespoor S|Born T|Jagar R|Gray T M|Arnoys E J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":14985,"numValue":26.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14986,"numValue":-38.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14987,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2041 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,041 | train | mutant | 2,067 | 41 | 2,307 | 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 | L66P | L66P | 1 | 1 | 0 | 0 | 66 | L | P | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 66 | A | H | false | true | 4.09387 | 15.363125 | 11,100 | ProTherm | 7 | CD | Urea | Potassium phosphate | 10 mM | 25 | KCl | 0.15 M | 2LZM_A:L66P | null | null | 4.32 | 12.23 | null | null | null | 2.53 | 1.71 | null | null | null | null | null | null | null | no | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 374 | ARTICLE | Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: leucine 66 to proline and leucine 91 to proline. | 1,996 | 10.1002/pro.5560050419 | 8845764 | Protein Sci;5;742-51 | 5 | Blankespoor S|Born T|Jagar R|Gray T M|Arnoys E J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"B... | [{"datasets":[],"id":38219,"numValue":4.32,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38220,"numValue":12.23,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38221,"numValue":1.71,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38222,"numValue":2.53,"references":[]... | [{"id":6857,"numValue":8.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2042 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,042 | train | mutant | 1,679 | 41 | 1,888 | 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 | F67A | F67A | 1 | 1 | 0 | 0 | 67 | F | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 67 | A | H | true | false | 12.938596 | 15.351818 | 3,139 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:F67A | 46 | -5.7 | null | null | null | 1.8 | 101 | 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 | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11447,"numValue":46.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11448,"numValue":-5.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11449,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6858,"numValue":8.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2043 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,043 | train | mutant | 1,679 | 41 | 1,888 | 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 | F67A | F67A | 1 | 1 | 0 | 0 | 67 | F | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 67 | A | H | true | false | 12.938596 | 15.351818 | 7,573 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:F67A | null | null | null | 1.9 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26192,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26193,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26194,"numV... | [{"id":6858,"numValue":8.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2044 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,044 | train | mutant | 1,841 | 41 | 2,062 | 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 | N68A | N68A | 1 | 1 | 0 | 0 | 68 | N | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 68 | A | H | true | false | 81.739845 | 20.58125 | 3,546 | ProTherm | 2.5 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:N68A | 48 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 325 | ARTICLE | Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices. | 1,994 | 10.1021/bi00206a003 | 7918421 | Biochemistry;33;12022-31 | 5 | Cornish V W|Kaplan M I|Veenstra D L|Kollman P A|Schultz P G | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13064,"numValue":48.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13065,"numValue":-0.2,"references":[],"strValue":nul... | [{"id":6859,"numValue":2.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2046 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,046 | train | mutant | 252 | 41 | 283 | 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 | Q69P | Q69P | 1 | 1 | 0 | 0 | 69 | Q | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 69 | A | H | false | true | 90.30185 | 15.321667 | 450 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 150 mM | 2LZM_A:Q69P | 25.6 | -12.9 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":1820,"numValue":25.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1821,"numValue":-12.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1822,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6860,"numValue":4.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2047 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,047 | train | mutant | 252 | 41 | 283 | 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 | Q69P | Q69P | 1 | 1 | 0 | 0 | 69 | Q | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 69 | A | H | false | true | 90.30185 | 15.321667 | 452 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:Q69P | 55.6 | -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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1826,"numValue":55.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1827,"numValue":-7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1828,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6860,"numValue":4.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2048 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,048 | train | mutant | 252 | 41 | 283 | 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 | Q69P | Q69P | 1 | 1 | 0 | 0 | 69 | Q | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 69 | A | H | false | true | 90.30185 | 15.321667 | 7,037 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63.2 | KCl | 150 mM | 2LZM_A:Q69P | null | null | null | 2.9 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24741,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24742,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6860,"numValue":4.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2049 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,049 | train | mutant | 252 | 41 | 283 | 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 | Q69P | Q69P | 1 | 1 | 0 | 0 | 69 | Q | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 69 | A | H | false | true | 90.30185 | 15.321667 | 8,222 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 38.5 | KCl | 150 mM | 2LZM_A:Q69P | null | null | null | 3.3 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":38.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},... | [{"datasets":["capriotti_S1615_map.csv"],"id":27846,"numValue":3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27847,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6860,"numValue":4.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2050 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,050 | train | mutant | 1,677 | 41 | 1,886 | 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 | V71A | V71A | 1 | 1 | 0 | 0 | 71 | V | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 71 | A | H | false | true | 6.718547 | 11.179286 | 3,131 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V71A | 47 | -4.7 | null | null | null | 1.8 | 108 | 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 | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11407,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11408,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11409,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6862,"numValue":7.0,"position":71,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2051 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,051 | train | mutant | 1,677 | 41 | 1,886 | 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 | V71A | V71A | 1 | 1 | 0 | 0 | 71 | V | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 71 | A | H | false | true | 6.718547 | 11.179286 | 7,565 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:V71A | null | null | null | 1.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26168,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26169,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26170,"numV... | [{"id":6862,"numValue":7.0,"position":71,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2052 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,052 | train | mutant | 253 | 41 | 284 | 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 | D72P | D72P | 1 | 1 | 0 | 0 | 72 | D | P | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 72 | A | H | false | true | 72.044259 | 21.818125 | 451 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 150 mM | 2LZM_A:D72P | 28.3 | -10.2 | 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 | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":1823,"numValue":28.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1824,"numValue":-10.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1825,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6863,"numValue":3.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2053 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,053 | train | mutant | 253 | 41 | 284 | 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 | D72P | D72P | 1 | 1 | 0 | 0 | 72 | D | P | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 72 | A | H | false | true | 72.044259 | 21.818125 | 453 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:D72P | 56.3 | -6.9 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1829,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1830,"numValue":-6.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1831,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6863,"numValue":3.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2054 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,054 | train | mutant | 253 | 41 | 284 | 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 | D72P | D72P | 1 | 1 | 0 | 0 | 72 | D | P | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 72 | A | H | false | true | 72.044259 | 21.818125 | 7,035 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 63.4 | KCl | 150 mM | 2LZM_A:D72P | null | null | null | 2.7 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":63.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24736,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24737,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6863,"numValue":3.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2056 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,056 | train | mutant | 232 | 41 | 262 | 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 | A73S | A73S | 1 | 1 | 0 | 0 | 73 | A | S | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 73 | A | H | true | true | 48.489833 | 17.66 | 418 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A73S | 50.28 | -1.27 | null | null | null | null | 111 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1723,"numValue":50.28,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1724,"numValue":-1.27,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1725,"numValue":111.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6864,"numValue":2.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2057 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,057 | train | mutant | 232 | 41 | 262 | 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 | A73S | A73S | 1 | 1 | 0 | 0 | 73 | A | S | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 73 | A | H | true | true | 48.489833 | 17.66 | 7,587 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A73S | 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|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26231,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26232,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6864,"numValue":2.0,"position":73,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2058 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,058 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 454 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:A74P | 50.8 | -12.4 | 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 | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1832,"numValue":50.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1833,"numValue":-12.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1834,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2059 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,059 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 455 | ProTherm | 3.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:A74P | 39.3 | -18.2 | 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 | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1835,"numValue":39.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1836,"numValue":-18.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1837,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2060 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,060 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 456 | ProTherm | 4 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:A74P | 46.9 | -15.3 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1838,"numValue":46.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1839,"numValue":-15.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1840,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2061 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,061 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 457 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:A74P | 53.3 | -12.4 | 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 | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1841,"numValue":53.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1842,"numValue":-12.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1843,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2062 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,062 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 6,757 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 10 mM | 65.7 | KCl | 150 mM | 2LZM_A:A74P | null | null | null | 4.5 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":65.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23984,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23985,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2063 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,063 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 7,059 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 62.9 | KCl | 150 mM | 2LZM_A:A74P | null | null | null | 4.6 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":62.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":24790,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24791,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2064 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,064 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 7,074 | ProTherm | 4 | CD | Thermal | Potassium phosphate | 10 mM | 62.2 | KCl | 150 mM | 2LZM_A:A74P | null | null | null | 5 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24822,"numValue":5.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24823,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2065 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,065 | train | mutant | 254 | 41 | 285 | 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 | A74P | A74P | 1 | 1 | 0 | 0 | 74 | A | P | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 74 | A | H | true | true | 8.278582 | 17.91 | 7,161 | ProTherm | 3.5 | CD | Thermal | Potassium phosphate | 10 mM | 57.5 | KCl | 150 mM | 2LZM_A:A74P | null | null | null | 5.7 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 47 | ARTICLE | Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. | 1,992 | 1733941 | J Biol Chem;267;2393-9 | 3 | Matthews B W|Sauer U H|San D P | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":57.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv"],"id":25080,"numValue":5.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25081,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6865,"numValue":5.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2066 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,066 | train | mutant | 238 | 41 | 268 | 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 | V75T | V75T | 1 | 1 | 0 | 0 | 75 | V | T | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 75 | A | H | false | false | 37.086381 | 21.545 | 424 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V75T | 47.85 | -3.7 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1747,"numValue":47.85,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1748,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1749,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6866,"numValue":3.0,"position":75,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2067 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,067 | train | mutant | 238 | 41 | 268 | 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 | V75T | V75T | 1 | 1 | 0 | 0 | 75 | V | T | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 75 | A | H | false | false | 37.086381 | 21.545 | 7,593 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:V75T | null | null | null | 1.3 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26243,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26244,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6866,"numValue":3.0,"position":75,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2068 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,068 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 574 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 2LZM_A:G77A | 40.5 | -1.4 | null | null | null | 2 | 85 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|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":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":2281,"numValue":40.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","potapov_with_uniprot_mapping.csv","Saraboji_S1791.csv"],"id":2282,"numValue":-1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_m... | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2069 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,069 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 576 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 2LZM_A:G77A | 65.6 | 0.94 | null | null | null | 2 | 125 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|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":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":2291,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","potapov_with_uniprot_mapping.csv","Saraboji_S1791.csv"],"id":2292,"numValue":0.94,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_m... | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2070 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,070 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 786 | ProTherm | 2 | CD | Thermal | H3PO4,HCl, | 10 mM,10 mM, | null | KCl | 0.2 M | 2LZM_A:G77A | 40.5 | -1.4 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,HCl,","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":2997,"numValue":40.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","potapov_with_uniprot_mapping.csv","Saraboji_S1791.csv"],"id":2998,"numValue":-1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_m... | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2071 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,071 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 791 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:G77A | 65.6 | 0.9 | null | null | null | null | 125 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":3016,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","potapov_with_uniprot_mapping.csv","Saraboji_S1791.csv"],"id":3017,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_ma... | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2072 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,072 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 6,981 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | 64.7 | KCl | 100 mM | 2LZM_A:G77A | null | null | null | -0.4 | null | 2 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv|capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|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":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":24606,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24607,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":["pota... | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2073 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,073 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 7,000 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 64.7 | KCl | 0.15 M | 2LZM_A:G77A | 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|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24646,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":24647,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2074 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,074 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 8,029 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | 41.9 | KCl | 100 mM | 2LZM_A:G77A | null | null | null | 0.4 | null | 2 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | potapov_with_uniprot_mapping.csv|capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|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":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":27371,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27372,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"i... | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2075 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,075 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 8,047 | ProTherm | 2 | CD | Thermal | H3PO4,HCl | 10 mM,10 mM | 41.9 | KCl | 0.2 M | 2LZM_A:G77A | null | null | null | 0.4 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"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":"H3PO4,HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM","type":"BU... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27409,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":27410,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2076 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,076 | train | mutant | 327 | 41 | 363 | 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 | G77A | G77A | 1 | 1 | 0 | 0 | 77 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 77 | A | H | true | false | 4.232685 | 21.82625 | 12,609 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:G77A | null | null | null | 1.2 | null | null | null | 5.65 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":45730,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":45731,"numValue":5.65,"references":[],"strValue":null,"type":"CM"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":4573... | [{"id":6868,"numValue":3.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2077 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,077 | train | mutant | 160 | 41 | 188 | 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 | I78M | I78M | 1 | 1 | 0 | 0 | 78 | I | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 78 | A | H | true | false | 0 | 20.37125 | 297 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:I78M | 61.6 | -3.7 | null | null | null | 2.5 | 117 | 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 | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"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,"strValu... | [{"datasets":[],"id":1210,"numValue":61.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1211,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1212,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6869,"numValue":8.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2078 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,078 | train | mutant | 160 | 41 | 188 | 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 | I78M | I78M | 1 | 1 | 0 | 0 | 78 | I | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 78 | A | H | true | false | 0 | 20.37125 | 6,768 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:I78M | null | null | null | 1.5 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":65.3,"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 m... | [{"datasets":[],"id":24006,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24007,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24008,"numValue":null,"references... | [{"id":6869,"numValue":8.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2080 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,080 | train | mutant | 804 | 41 | 908 | 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 | I78V | I78V | 1 | 1 | 0 | 0 | 78 | I | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 78 | A | H | true | false | 0 | 20.37125 | 7,076 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:I78V | null | null | null | 0.8 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 151 | ARTICLE | Repacking the Core of T4 lysozyme by automated design. | 2,003 | 10.1016/s0022-2836(03)00856-8 | 12963380 | J Mol Biol;332;741-56 | 6 | Mooers Blaine H M|Datta Deepshikha|Baase Walter A|Zollars Eric S|Mayo Stephen L|Matthews Brian W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":61.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":24827,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24828,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24829,"numValue":null,"references":[],"strValue":"Unknown",... | [{"id":6869,"numValue":8.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2081 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,081 | train | mutant | 1,128 | 41 | 1,272 | 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 | I78A | I78A | 1 | 1 | 0 | 0 | 78 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 78 | A | H | true | false | 0 | 20.37125 | 2,022 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I78A | 61.8 | -3.5 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","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":... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7552,"numValue":61.8,"references":[],"strValue":null,"type":"TM"... | [{"id":6869,"numValue":8.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2082 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,082 | train | mutant | 1,128 | 41 | 1,272 | 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 | I78A | I78A | 1 | 1 | 0 | 0 | 78 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 78 | A | H | true | false | 0 | 20.37125 | 3,129 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I78A | 47 | -4.7 | null | null | null | 1.8 | 105 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11397,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv"],"id":11398,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11399,"numValue":1.8,"references":[],"s... | [{"id":6869,"numValue":8.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2083 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,083 | train | mutant | 1,128 | 41 | 1,272 | 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 | I78A | I78A | 1 | 1 | 0 | 0 | 78 | I | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 78 | A | H | true | false | 0 | 20.37125 | 6,789 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | 65.3 | Sodium Chloride | 0.10 M | 1L63_A:I78A | null | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.3,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"st... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24069,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24070,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24071,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6869,"numValue":8.0,"position":78,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2085 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,085 | train | mutant | 1,880 | 41 | 2,108 | 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 | L79C | L79C | 1 | 1 | 0 | 0 | 79 | L | C | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 79 | A | H | false | false | 70.986674 | 25.1375 | 3,625 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L79C | 31.3 | -5.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 338 | ARTICLE | Protein folding: assignment of the energetic changes of reversible chemical modifications to the folded or unfolded states. | 1,992 | 10.1021/bi00149a004 | 1510962 | Biochemistry;31;7765-72 | 4 | Lu J|Baase W A|Dahlquist F W|Muchmore D C | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13326,"numValue":31.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":1332... | [{"id":6870,"numValue":1.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2086 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,086 | train | mutant | 100 | 41 | 110 | 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 | R80K | R80K | 1 | 1 | 0 | 0 | 80 | R | K | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 80 | A | H|T | true | true | 177.947781 | 50.361818 | 194 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:R80K | 64.72 | -0.43 | null | null | null | 3.5 | 136 | 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 | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":797,"numValue":64.72,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":798,"numValue":-0.43,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":799,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":6871,"numValue":2.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2087 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,087 | train | mutant | 100 | 41 | 110 | 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 | R80K | R80K | 1 | 1 | 0 | 0 | 80 | R | K | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 80 | A | H|T | true | true | 177.947781 | 50.361818 | 206 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:R80K | 61.85 | -0.34 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":852,"numValue":61.85,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":853,"numValue":-0.34,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":854,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":6871,"numValue":2.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2089 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,089 | train | mutant | 6,710 | 41 | 7,352 | 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 | R80K|R119H | R80K|R119H | 2 | 2 | 0 | 0 | 80 | R | K | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 80|119 | A | H|T | true | true | 148.329586 | 48.277273 | 14,460 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:R80K 2LZM_A:R119H | 63.95 | -1.2 | null | null | null | 3.5 | 133 | 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 | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":53450,"numValue":63.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53451,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53452,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53453,"numValue":133.0,"references":... | [{"id":6871,"numValue":2.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2090 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,090 | train | mutant | 6,710 | 41 | 7,352 | 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 | R80K|R119H | R80K|R119H | 2 | 2 | 0 | 0 | 80 | R | K | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 80|119 | A | H|T | true | true | 148.329586 | 48.277273 | 14,461 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:R80K 2LZM_A:R119H | 60.94 | -1.25 | null | null | null | 3.5 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":6.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":... | [{"datasets":[],"id":53455,"numValue":60.94,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53456,"numValue":-1.25,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53457,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53458,"numValue":null,"references":... | [{"id":6871,"numValue":2.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2091 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,091 | train | mutant | 6,710 | 41 | 7,352 | 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 | R80K|R119H | R80K|R119H | 2 | 2 | 0 | 0 | 80 | R | K | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 80|119 | A | H|T | true | true | 148.329586 | 48.277273 | 14,915 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:R80K 2LZM_A:R119H | null | null | null | 0.47 | null | 3.5 | 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 | 15 | ARTICLE | Development of an in vivo method to identify mutants of phage T4 lysozyme of enhanced thermostability. | 1,993 | 10.1002/pro.5560021221 | 7507755 | Protein Sci;2;2217-25 | 4 | Baase W A|Matthews B W|Pjura P|Matsumura M | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.15,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BU... | [{"datasets":[],"id":54979,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54980,"numValue":0.47,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54981,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6871,"numValue":2.0,"position":80,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2092 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,092 | train | mutant | 233 | 41 | 263 | 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 | A82S | A82S | 1 | 1 | 0 | 0 | 82 | A | S | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 419 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A82S | 50.56 | -0.99 | null | null | null | null | 112 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1727,"numValue":50.56,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1728,"numValue":-0.99,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1729,"numValue":112.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2093 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,093 | train | mutant | 233 | 41 | 263 | 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 | A82S | A82S | 1 | 1 | 0 | 0 | 82 | A | S | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 7,588 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A82S | 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|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26233,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26234,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2095 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,095 | train | mutant | 328 | 41 | 364 | 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 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 577 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 2LZM_A:A82P | 66.8 | 2.1 | null | null | null | 2 | 126 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 60 | ARTICLE | Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. | 1,987 | 10.1073/pnas.84.19.6663 | 3477797 | Proc Natl Acad Sci U S A;84;6663-7 | 3 | Nicholson H|Matthews B W|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":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":2296,"numValue":66.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2297,"numValue":2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2298,"numValue":2.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2096 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,096 | train | mutant | 328 | 41 | 364 | 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 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 787 | ProTherm | 2 | CD | Thermal | H3PO4,HCl, | 10 mM,10 mM, | null | KCl | 0.2 M | 2LZM_A:A82P | 42.7 | 0.8 | null | null | null | null | 90 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,HCl,","type":"BUFFER"},{"numValue":null,"strValue":"10 mM,10 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION... | [{"datasets":[],"id":3001,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3002,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3003,"numValue":90.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2097 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,097 | train | mutant | 328 | 41 | 364 | 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 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 792 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:A82P | 66.8 | 2.1 | null | null | null | null | 126 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 86 | ARTICLE | Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme. | 1,992 | 10.1002/bip.360321103 | 1457724 | Biopolymers;32;1431-41 | 4 | Nicholson H|Matthews B W|Becktel W J|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":3020,"numValue":66.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3021,"numValue":2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3022,"numValue":126.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2098 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,098 | train | mutant | 328 | 41 | 364 | 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 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 890 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A82P | 38.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"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":3308,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3309,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2099 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,099 | train | mutant | 328 | 41 | 364 | 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 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 893 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A82P | 46.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"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":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":3314,"numValue":46.2,"references":[],"strValue":null,"type"... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2100 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,100 | train | mutant | 328 | 41 | 364 | 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 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 896 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A82P | 53.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"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":3320,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3321,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2101 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,101 | train | mutant | 328 | 41 | 364 | 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 | A82P | A82P | 1 | 1 | 0 | 0 | 82 | A | P | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 82 | A | T | false | false | 88.988662 | 25.384 | 900 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:A82P | 54.5 | 1.08 | null | null | null | 1.8 | 125 | 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":3331,"numValue":54.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3332,"numValue":1.08,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3333,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6873,"numValue":4.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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