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:2548 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,548 | train | mutant | 810 | 41 | 914 | 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 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 6,799 | 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:V111A | 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 | 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":24099,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24100,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24101,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,549 | train | mutant | 810 | 41 | 914 | 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 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 7,083 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | 61 | 2LZM_A:V111A | null | null | null | 1.1 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.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":24848,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv"],"id":24849,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24850,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,550 | train | mutant | 810 | 41 | 914 | 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 | V111A | V111A | 1 | 1 | 0 | 0 | 111 | V | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 7,569 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:V111A | null | null | null | 1.3 | 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|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":26180,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":26181,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26182,"numValue":null,"references":[],"strV... | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,551 | train | mutant | 1,144 | 41 | 1,288 | 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 | V111M | V111M | 1 | 1 | 0 | 0 | 111 | V | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 2,045 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:V111M | 63.3 | -2 | null | null | null | null | 127 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.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":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":7667,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMu... | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2552 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,552 | train | mutant | 1,144 | 41 | 1,288 | 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 | V111M | V111M | 1 | 1 | 0 | 0 | 111 | V | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111 | A | H | false | false | 0.201556 | 19.4 | 6,812 | 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:V111M | null | null | null | 0.7 | 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":24138,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24139,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24140,"numValue":null,"references":[],"strValue":"Yes(80%... | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,553 | train | mutant | 6,738 | 41 | 7,380 | 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 | V111I|F153L | V111I|F153L | 2 | 2 | 0 | 0 | 111 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111|153 | A | H | true | false | 0.465854 | 18.194545 | 14,497 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:V111I 2LZM_A:F153L | 48.24 | -3.52 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53590,"numValue":48.24,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53591,"numValue":-3.52,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53592,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,554 | train | mutant | 6,738 | 41 | 7,380 | 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 | V111I|F153L | V111I|F153L | 2 | 2 | 0 | 0 | 111 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111|153 | A | H | true | false | 0.465854 | 18.194545 | 14,506 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:V111I 2LZM_A:F153L | 61.65 | -3.24 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":[],"id":53617,"numValue":61.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53618,"numValue":-3.24,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53619,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,556 | train | mutant | 6,738 | 41 | 7,380 | 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 | V111I|F153L | V111I|F153L | 2 | 2 | 0 | 0 | 111 | V | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 111|153 | A | H | true | false | 0.465854 | 18.194545 | 15,003 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:V111I 2LZM_A:F153L | null | null | null | 1.09 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":[],"id":55188,"numValue":1.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55189,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,557 | train | mutant | 102 | 41 | 112 | 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 | G113E | G113E | 1 | 1 | 0 | 0 | 113 | G | E | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 196 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:G113E | 65.94 | 0.79 | null | null | null | 3.5 | 126 | 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":807,"numValue":65.94,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":808,"numValue":0.79,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":809,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":8... | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,558 | train | mutant | 102 | 41 | 112 | 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 | G113E | G113E | 1 | 1 | 0 | 0 | 113 | G | E | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 208 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:G113E | 63.22 | 1.03 | 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":861,"numValue":63.22,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":862,"numValue":1.03,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":863,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":8... | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,559 | train | mutant | 102 | 41 | 112 | 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 | G113E | G113E | 1 | 1 | 0 | 0 | 113 | G | E | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 6,825 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:G113E | null | null | null | -0.3 | null | 3.5 | 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 | 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":24174,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24175,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24176,"numValue":null,"reference... | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,560 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 789 | ProTherm | 2 | CD | Thermal | H3PO4,HCl, | 10 mM,10 mM, | null | KCl | 0.2 M | 2LZM_A:G113A | 42.3 | 0.4 | null | null | null | null | 99 | 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":3009,"numValue":42.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3010,"numValue":0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3011,"numValue":99.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,561 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 794 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:G113A | 65.3 | 0.8 | null | null | null | null | 120 | 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":3028,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3029,"numValue":0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3030,"numValue":120.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,562 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 892 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:G113A | 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":3312,"numValue":38.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3313,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,563 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 895 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:G113A | 46.2 | 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":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3318,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3319,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,564 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 898 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:G113A | 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":3324,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":3325,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,565 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 7,003 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 64.7 | KCl | 0.15 M | 2LZM_A:G113A | null | null | null | -0.3 | 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 | 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"],"id":24652,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24653,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,566 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 7,330 | ProTherm | 3 | DSC | Thermal | Potassium phosphate | 20 mM | 53.6 | KCl | 25 mM | 2LZM_A:G113A | null | null | null | -0.54 | null | 2.52 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":25571,"numValue":2.52,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25572,"numValue":-0.54,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25573,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,567 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 7,848 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | 46.2 | KCl | 25 mM | 2LZM_A:G113A | null | null | null | -0.54 | null | 2.52 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":46.2,"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":26846,"numValue":2.52,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26847,"numValue":-0.54,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26848,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,568 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 8,050 | ProTherm | 2 | CD | Thermal | H3PO4,HCl | 10 mM,10 mM | 41.9 | KCl | 0.2 M | 2LZM_A:G113A | 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 | 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"],"id":27415,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27416,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,569 | train | mutant | 481 | 41 | 530 | 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 | G113A | G113A | 1 | 1 | 0 | 0 | 113 | G | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 113 | A | T | true | false | 55.568371 | 32.785 | 8,212 | ProTherm | 2 | DSC | Thermal | Potassium phosphate | 20 mM | 38.8 | KCl | 25 mM | 2LZM_A:G113A | null | null | null | -0.5 | null | 2.52 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":27816,"numValue":2.52,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27817,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27818,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6904,"numValue":3.0,"position":113,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,571 | train | mutant | 180 | 41 | 208 | 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 | T115A | T115A | 1 | 1 | 0 | 0 | 115 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 7,549 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:T115A | null | null | null | 0.14 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26129,"numValue":0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26130,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,572 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 3,295 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:T115E | 39.2 | -1.7 | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"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":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":12129,"numValue":39.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":12130,"numValue":-1.7,"references":[],"strValue":null,"t... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,573 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 3,300 | ProTherm | 6.5 | CD | Thermal | phosphate | 10 mM | null | KCl | 150 mM | 2LZM_A:T115E | 66.8 | 0.7 | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"num... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":12144,"numValue":66.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":12145,"numValue":0.7,"references":[],"strValue":null,"ty... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,574 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 3,402 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:T115E | 38.7 | -1.7 | null | null | null | null | 84 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|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 | 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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":12547,"numValue":38.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":12548,"numValue":-1.7,"references":[],"strValue":null,"t... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,576 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 3,404 | ProTherm | 4 | CD | Thermal | acetate | 10 mM | null | KCl | 0.15 M | 2LZM_A:T115E | 63.3 | -0.3 | null | null | null | null | 131 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|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 | 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":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":12555,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":12556,"numValue":-0.3,"references":[],"strValue":null,"t... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,577 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 3,405 | ProTherm | 5.5 | CD | Thermal | acetate | 10 mM | null | KCl | 0.15 M | 2LZM_A:T115E | 66.8 | 0.1 | null | null | null | null | 126 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|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 | 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":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":12559,"numValue":66.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":12560,"numValue":0.1,"references":[],"strValue":null,"ty... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,578 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 3,406 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:T115E | 65.3 | 0.7 | null | null | null | null | 125 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1791.csv|SVM-WIN31_SVM-3D12_S499.csv|STRUM_Q3421.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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S2204.csv"],"id":12563,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","khan_protherm_data_ma... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,579 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 6,715 | ProTherm | 5.5 | CD | Thermal | acetate | 10 mM | 66.7 | KCl | 0.15 M | 2LZM_A:T115E | null | null | null | 0 | 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":5.5,"strValue":null,"type":"PH"},{"numValue":66.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23873,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23874,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,580 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 6,750 | ProTherm | 6.5 | CD | Thermal | phosphate | 10 mM | 66.1 | KCl | 150 mM | 2LZM_A:T115E | null | null | null | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":66.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23970,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23971,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,581 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 7,006 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 64.6 | KCl | 0.15 M | 2LZM_A:T115E | null | null | null | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|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":64.6,"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":24659,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24660,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,582 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 7,034 | ProTherm | 4 | CD | Thermal | acetate | 10 mM | 63.6 | KCl | 0.15 M | 2LZM_A:T115E | 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 | 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":4.0,"strValue":null,"type":"PH"},{"numValue":63.6,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24734,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24735,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,583 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 7,430 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 10 mM | 52.6 | KCl | 0.15 M | 2LZM_A:T115E | null | null | null | 0.2 | 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":3.0,"strValue":null,"type":"PH"},{"numValue":52.6,"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":25829,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":25830,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,584 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 8,064 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 40.9 | KCl | 200 mM | 2LZM_A:T115E | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.9,"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":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27443,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27444,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,585 | train | mutant | 1,738 | 41 | 1,948 | 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 | T115E | T115E | 1 | 1 | 0 | 0 | 115 | T | E | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115 | A | H | true | false | 86.677669 | 24.525714 | 8,078 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 40.4 | KCl | 0.15 M | 2LZM_A:T115E | 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 | 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":40.4,"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","khan_protherm_data_mapped.csv"],"id":27474,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27475,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,587 | train | mutant | 6,721 | 41 | 7,363 | 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 | T115A|S117A | T115A|S117A | 2 | 2 | 0 | 0 | 115 | T | A | 5 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 115|117 | A | H | true | false | 43.94163 | 21.59869 | 15,020 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:T115A 2LZM_A:S117A | null | null | null | -0.95 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":[],"id":55223,"numValue":-0.95,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55224,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,588 | train | mutant | 6,724 | 41 | 7,366 | 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 | T115A|R119A | T115A|R119A | 2 | 2 | 0 | 0 | 115 | T | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 115|119 | A | H | true | false | 102.69453 | 35.359221 | 14,483 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:T115A 2LZM_A:R119A | 51.13 | -0.52 | null | null | null | null | 106 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":53552,"numValue":51.13,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53553,"numValue":-0.52,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53554,"numValue":106.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53555,"numValue":null,"reference... | [{"id":6906,"numValue":5.0,"position":115,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,590 | train | mutant | 181 | 41 | 209 | 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 | N116A | N116A | 1 | 1 | 0 | 0 | 116 | N | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 320 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:N116A | 52.14 | 0.49 | null | null | null | null | 109 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":1316,"numValue":52.14,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1317,"numValue":0.49,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1318,"numValue":109.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,591 | train | mutant | 181 | 41 | 209 | 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 | N116A | N116A | 1 | 1 | 0 | 0 | 116 | N | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 7,550 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:N116A | null | null | null | -0.17 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26131,"numValue":-0.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26132,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,592 | train | mutant | 530 | 41 | 581 | 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 | N116D | N116D | 1 | 1 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 905 | ProTherm | 3 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:N116D | 54.32 | 0.9 | null | null | null | 1.8 | 131 | 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":3356,"numValue":54.32,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3357,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3358,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,593 | train | mutant | 530 | 41 | 581 | 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 | N116D | N116D | 1 | 1 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 912 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:N116D | 67.87 | 1.36 | null | null | null | 2.5 | 139 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3391,"numValue":67.87,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3392,"numValue":1.36,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3393,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,594 | train | mutant | 530 | 41 | 581 | 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 | N116D | N116D | 1 | 1 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 3,296 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:N116D | 40.7 | -0.2 | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"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":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":12132,"numValue":40.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12133,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12134,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,596 | train | mutant | 530 | 41 | 581 | 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 | N116D | N116D | 1 | 1 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 6,727 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.51 | NaCl | 100 mM | 2LZM_A:N116D | null | null | null | -0.6 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|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 | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.51,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23903,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":23904,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23905,"numValue":null,"references":[],"str... | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,597 | train | mutant | 530 | 41 | 581 | 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 | N116D | N116D | 1 | 1 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 6,751 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 66.1 | KCl | 150 mM | 2LZM_A:N116D | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":66.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":23972,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23973,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,598 | train | mutant | 530 | 41 | 581 | 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 | N116D | N116D | 1 | 1 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 7,342 | ProTherm | 3 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 53.42 | KCl | 25 mM | 2LZM_A:N116D | null | null | null | -0.34 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 97 | ARTICLE | Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. | 1,995 | 10.1093/protein/8.10.1017 | 8771182 | Protein Eng;8;1017-22 | 5 | Baase W A|Zhang X J|Matthews B W|Shoichet B K|Wilson K P | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.42,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","type... | [{"datasets":[],"id":25607,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25608,"numValue":-0.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25609,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,599 | train | mutant | 530 | 41 | 581 | 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 | N116D | N116D | 1 | 1 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116 | A | H | true | false | 79.838049 | 24.644375 | 8,065 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 40.9 | KCl | 200 mM | 2LZM_A:N116D | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.9,"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":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27445,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27446,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,600 | train | mutant | 6,725 | 41 | 7,367 | 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 | N116A|M120A | N116A|M120A | 2 | 2 | 0 | 0 | 116 | N | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116|120 | A | H | true | false | 54.95669 | 23.709375 | 14,484 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:N116A 2LZM_A:M120A | 52.23 | 0.58 | null | null | null | null | 116 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":53556,"numValue":52.23,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53557,"numValue":0.58,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53558,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53559,"numValue":null,"references... | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,601 | train | mutant | 6,725 | 41 | 7,367 | 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 | N116A|M120A | N116A|M120A | 2 | 2 | 0 | 0 | 116 | N | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116|120 | A | H | true | false | 54.95669 | 23.709375 | 15,024 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:N116A 2LZM_A:M120A | null | null | null | -0.21 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":[],"id":55231,"numValue":-0.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55232,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,602 | train | mutant | 6,765 | 41 | 7,407 | 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 | N116D|R119M | N116D|R119M | 2 | 2 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116|119 | A | H | true | false | 99.27472 | 35.418551 | 14,537 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:N116D 2LZM_A:R119M | 40.1 | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"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":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":53740,"numValue":40.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53741,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53742,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,604 | train | mutant | 6,765 | 41 | 7,407 | 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 | N116D|R119M | N116D|R119M | 2 | 2 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116|119 | A | H | true | false | 99.27472 | 35.418551 | 14,904 | ProTherm | 5.7 | CD | Thermal | HCl | 0.01 N | 66.1 | KCl | 200 mM | 2LZM_A:N116D 2LZM_A:R119M | null | null | null | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":66.1,"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":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":[],"id":54952,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54953,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,605 | train | mutant | 6,765 | 41 | 7,407 | 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 | N116D|R119M | N116D|R119M | 2 | 2 | 0 | 0 | 116 | N | D | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 116|119 | A | H | true | false | 99.27472 | 35.418551 | 15,098 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 40.9 | KCl | 200 mM | 2LZM_A:N116D 2LZM_A:R119M | null | null | null | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.9,"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":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":[],"id":55411,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55412,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6907,"numValue":7.0,"position":116,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,606 | train | mutant | 182 | 41 | 210 | 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 | S117A | S117A | 1 | 1 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 321 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:S117A | 55.29 | 3.64 | null | null | null | null | 115 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":1320,"numValue":55.29,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1321,"numValue":3.64,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1322,"numValue":115.0,"references":[],"strValue":null,"type":"DH... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,607 | train | mutant | 182 | 41 | 210 | 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 | S117A | S117A | 1 | 1 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 7,551 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:S117A | null | null | null | -1.27 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":26133,"numValue":-1.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26134,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,608 | train | mutant | 228 | 41 | 258 | 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 | S117F | S117F | 1 | 1 | 0 | 0 | 117 | S | F | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 413 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 M,17 M, | null | KCl | 25 mM | 2LZM_A:S117F | 56.48 | 4.8 | null | null | null | null | 104 | 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 | 43 | ARTICLE | Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe. | 1,993 | 10.1002/pro.5560020811 | 8401213 | Protein Sci;2;1285-90 | 5 | Nicholson H|Baase W A|Matthews B W|Anderson D E|Hurley J H | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 M,17 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION... | [{"datasets":[],"id":1703,"numValue":56.48,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1704,"numValue":4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1705,"numValue":104.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,610 | train | mutant | 228 | 41 | 258 | 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 | S117F | S117F | 1 | 1 | 0 | 0 | 117 | S | F | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 920 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S117F | 68.28 | 2.8 | null | null | null | 3.5 | 132 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3431,"numValue":68.28,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3432,"numValue":2.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3433,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,611 | train | mutant | 228 | 41 | 258 | 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 | S117F | S117F | 1 | 1 | 0 | 0 | 117 | S | F | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 6,735 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:S117F | null | null | null | -1.1 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23927,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23928,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23929,"numValue":null,"reference... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,612 | train | mutant | 228 | 41 | 258 | 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 | S117F | S117F | 1 | 1 | 0 | 0 | 117 | S | F | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 6,836 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.09 | NaCl | 0.10 M | 2LZM_A:S117F | null | null | null | -1.1 | 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 | 43 | ARTICLE | Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe. | 1,993 | 10.1002/pro.5560020811 | 8401213 | Protein Sci;2;1285-90 | 5 | Nicholson H|Baase W A|Matthews B W|Anderson D E|Hurley J H | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.09,"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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24207,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24208,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,613 | train | mutant | 228 | 41 | 258 | 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 | S117F | S117F | 1 | 1 | 0 | 0 | 117 | S | F | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 7,519 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 M,17 M | 51.7 | KCl | 25 mM | 2LZM_A:S117F | null | null | null | -1.4 | 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 | 43 | ARTICLE | Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe. | 1,993 | 10.1002/pro.5560020811 | 8401213 | Protein Sci;2;1285-90 | 5 | Nicholson H|Baase W A|Matthews B W|Anderson D E|Hurley J H | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 M,17 M","type":"BU... | [{"datasets":["capriotti_S1615_map.csv"],"id":26050,"numValue":-1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26051,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,614 | train | mutant | 536 | 41 | 587 | 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 | S117V | S117V | 1 | 1 | 0 | 0 | 117 | S | V | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 918 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S117V | 71.58 | 5.1 | null | null | null | 3.5 | 133 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3421,"numValue":71.58,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3422,"numValue":5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3423,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,615 | train | mutant | 536 | 41 | 587 | 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 | S117V | S117V | 1 | 1 | 0 | 0 | 117 | S | V | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 6,733 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:S117V | null | null | null | -2 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23921,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23922,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23923,"numValue":null,"reference... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,616 | train | mutant | 537 | 41 | 588 | 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 | S117I | S117I | 1 | 1 | 0 | 0 | 117 | S | I | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 919 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S117I | 70.68 | 4.2 | null | null | null | 3.5 | 140 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":3426,"numValue":70.68,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3427,"numValue":4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3428,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,617 | train | mutant | 537 | 41 | 588 | 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 | S117I | S117I | 1 | 1 | 0 | 0 | 117 | S | I | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117 | A | H | true | false | 1.205591 | 18.671667 | 6,734 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:S117I | null | null | null | -1.7 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":23924,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":23925,"numValue":-1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23926,"numValue":null,"references":[],"strValue":"yes","type":"R... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,618 | train | mutant | 6,722 | 41 | 7,364 | 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 | S117A|R119A | S117A|R119A | 2 | 2 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|119 | A | H | true | false | 59.958491 | 32.432197 | 14,481 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:S117A 2LZM_A:R119A | 55.02 | 3.37 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":53544,"numValue":55.02,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53545,"numValue":3.37,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53546,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53547,"numValue":null,"references... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,619 | train | mutant | 6,722 | 41 | 7,364 | 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 | S117A|R119A | S117A|R119A | 2 | 2 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|119 | A | H | true | false | 59.958491 | 32.432197 | 15,021 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:S117A 2LZM_A:R119A | null | null | null | -1.16 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":[],"id":55225,"numValue":-1.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55226,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,620 | train | mutant | 6,778 | 41 | 7,420 | 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 | S117I|N132M | S117I|N132M | 2 | 2 | 0 | 0 | 117 | S | I | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|132 | A | H | true | false | 21.844851 | 18.175521 | 14,571 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S117I 2LZM_A:N132M | 71.98 | 5.5 | null | null | null | 3.5 | 123 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53879,"numValue":71.98,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53880,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53881,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53882,"numValue":123.0,"references":[... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:2621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,621 | train | mutant | 6,778 | 41 | 7,420 | 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 | S117I|N132M | S117I|N132M | 2 | 2 | 0 | 0 | 117 | S | I | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|132 | A | H | true | false | 21.844851 | 18.175521 | 14,902 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:S117I 2LZM_A:N132M | null | null | null | -2 | null | 3.5 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54946,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54947,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54948,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:2623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,623 | train | mutant | 6,779 | 41 | 7,421 | 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 | S117I|N132I | S117I|N132I | 2 | 2 | 0 | 0 | 117 | S | I | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|132 | A | H | true | false | 21.844851 | 18.175521 | 14,903 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 66.48 | NaCl | 100 mM | 2LZM_A:S117I 2LZM_A:N132I | null | null | null | -1.4 | null | 3.5 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":66.48,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 ... | [{"datasets":[],"id":54949,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54950,"numValue":-1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54951,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:2624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,624 | train | mutant | 6,780 | 41 | 7,422 | 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 | S117A|N132I | S117A|N132I | 2 | 2 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|132 | A | H | true | false | 21.844851 | 18.175521 | 14,573 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S117A 2LZM_A:N132I | 70.4 | 5.3 | null | null | null | 3.5 | 121 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53889,"numValue":70.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53890,"numValue":5.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53891,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53892,"numValue":121.0,"references":[]... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:2625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,625 | train | mutant | 6,780 | 41 | 7,422 | 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 | S117A|N132I | S117A|N132I | 2 | 2 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|132 | A | H | true | false | 21.844851 | 18.175521 | 14,916 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:S117A 2LZM_A:N132I | null | null | null | -2 | null | 3.5 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.1,"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":54982,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54983,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54984,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:2626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,626 | train | mutant | 6,781 | 41 | 7,423 | 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 | S117A|N132M | S117A|N132M | 2 | 2 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|132 | A | H | true | false | 21.844851 | 18.175521 | 14,574 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 100 mM | 2LZM_A:S117A 2LZM_A:N132M | 69.8 | 4.7 | null | null | null | 3.5 | 120 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue... | [{"datasets":[],"id":53894,"numValue":69.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53895,"numValue":4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53896,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53897,"numValue":120.0,"references":[]... | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:2627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,627 | train | mutant | 6,781 | 41 | 7,423 | 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 | S117A|N132M | S117A|N132M | 2 | 2 | 0 | 0 | 117 | S | A | 8 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 117|132 | A | H | true | false | 21.844851 | 18.175521 | 14,917 | ProTherm | 5.4 | CD | Thermal | Acetic acid, Sodium acetate | 1.4 mM, 8.6 mM | 65.1 | NaCl | 100 mM | 2LZM_A:S117A 2LZM_A:N132M | null | null | null | -1.8 | null | 3.5 | 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 | 98 | ARTICLE | A relationship between protein stability and protein function. | 1,995 | 10.1073/pnas.92.2.452 | 7831309 | Proc Natl Acad Sci U S A;92;452-6 | 4 | Kuroki R|Baase W A|Matthews B W|Shoichet B K | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.1,"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":54985,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54986,"numValue":-1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54987,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":22,"numValue":null,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6908,"numValue":8.0,"position":117,"positionArray":null,"positionRange"... | |||||||||||
fireprotdb:2628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,628 | train | mutant | 39 | 41 | 43 | 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 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 39 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 2LZM_A:L118A | 39.6 | -12.2 | null | null | null | 2.5 | 75.5 | 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 | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"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":"0.020 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type"... | [{"datasets":[],"id":126,"numValue":39.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":127,"numValue":-12.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":128,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1... | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,629 | train | mutant | 39 | 41 | 43 | 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 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 322 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:L118A | 39.6 | -12.05 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":1324,"numValue":39.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1325,"numValue":-12.05,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1326,"numValue":75.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,630 | train | mutant | 39 | 41 | 43 | 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 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 2,033 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L118A | 56.3 | -0.9 | null | null | null | null | 109 | 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|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","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7607,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,631 | train | mutant | 39 | 41 | 43 | 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 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 6,800 | 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:L118A | null | null | null | 3.2 | 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":24102,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24103,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24104,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2632 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,632 | train | mutant | 39 | 41 | 43 | 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 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 7,500 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | 51.8 | KCl | 0.025 M | 2LZM_A:L118A | null | null | null | 3.5 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.8,"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":"0.020 M","ty... | [{"datasets":[],"id":25997,"numValue":2.5,"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":25998,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25999,"numV... | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,633 | train | mutant | 39 | 41 | 43 | 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 | L118A | L118A | 1 | 1 | 0 | 0 | 118 | L | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 7,552 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:L118A | null | null | null | 3.5 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26135,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26136,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,635 | train | mutant | 166 | 41 | 194 | 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 | L118M | L118M | 1 | 1 | 0 | 0 | 118 | L | M | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 6,774 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:L118M | null | null | null | 0.7 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|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":24024,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24025,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24026,"numValue":null,"references... | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,636 | train | mutant | 805 | 41 | 909 | 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 | L118I | L118I | 1 | 1 | 0 | 0 | 118 | L | I | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 118 | A | H | false | false | 12.474277 | 19.780625 | 1,421 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:L118I | 62.4 | -3.1 | null | null | null | null | 123 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | PH|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":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium chloride, acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.10 M, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":5187,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5188,"numValue":-3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5189,"numValue":123.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5190,"numValue":null,"references":[],... | [{"id":6909,"numValue":7.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,638 | train | mutant | 56 | 41 | 62 | 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 | R119E | R119E | 1 | 1 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 70 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R119E | 50.3 | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"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":["khan_protherm_data_mapped.csv"],"id":239,"numValue":50.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":240,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,639 | train | mutant | 56 | 41 | 62 | 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 | R119E | R119E | 1 | 1 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 75 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R119E | 66.6 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | khan_protherm_data_mapped.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"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":["khan_protherm_data_mapped.csv"],"id":254,"numValue":66.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":255,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"]... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,640 | train | mutant | 56 | 41 | 62 | 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 | R119E | R119E | 1 | 1 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 6,711 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:R119E | null | null | null | 0.04 | 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 | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":66.7,"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":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23865,"numValue":0.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":23866,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,641 | train | mutant | 56 | 41 | 62 | 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 | R119E | R119E | 1 | 1 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 7,615 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:R119E | null | null | null | 0.2 | 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 | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":50.9,"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":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26295,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":26296,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2642 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,642 | train | mutant | 56 | 41 | 62 | 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 | R119E | R119E | 1 | 1 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 11,153 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 25 | KCl | 25 mM | 2LZM_A:R119E | null | null | null | 0 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 750 | ARTICLE | Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. | 2,000 | 10.1110/ps.9.7.1395 | 10933506 | Protein Sci;9;1395-8 | 3 | Pace C N|Shaw K L|Alston R W | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":38360,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":38361,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2643 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,643 | train | mutant | 103 | 41 | 113 | 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 | R119H | R119H | 1 | 1 | 0 | 0 | 119 | R | H | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 197 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:R119H | 64.41 | -0.74 | null | null | null | 3.5 | 132 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":812,"numValue":64.41,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":813,"numValue":-0.74,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":814,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2644 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,644 | train | mutant | 103 | 41 | 113 | 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 | R119H | R119H | 1 | 1 | 0 | 0 | 119 | R | H | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 209 | ProTherm | 6.78 | CD | Thermal | Potassium phosphate | 0.01 M | null | KCl | 0.15 M | 2LZM_A:R119H | 61.36 | -0.83 | 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":865,"numValue":61.36,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":866,"numValue":-0.83,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":867,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,645 | train | mutant | 103 | 41 | 113 | 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 | R119H | R119H | 1 | 1 | 0 | 0 | 119 | R | H | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 6,826 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.15 | NaCl | 0.10 M | 2LZM_A:R119H | null | null | null | 0.29 | null | 3.5 | 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 | 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":24177,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24178,"numValue":0.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24179,"numValue":null,"reference... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,646 | train | mutant | 183 | 41 | 211 | 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 | R119A | R119A | 1 | 1 | 0 | 0 | 119 | R | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 323 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:R119A | 51.12 | -0.53 | null | null | null | null | 107 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M,0.017 M,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","t... | [{"datasets":[],"id":1328,"numValue":51.12,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1329,"numValue":-0.53,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1330,"numValue":107.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,647 | train | mutant | 183 | 41 | 211 | 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 | R119A | R119A | 1 | 1 | 0 | 0 | 119 | R | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 7,553 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:R119A | null | null | null | 0.18 | 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 | 36 | ARTICLE | Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent. | 1,995 | 10.1006/jmbi.1994.0087 | 7869383 | J Mol Biol;246;317-30 | 4 | Blaber M|Gassner N|Baase W A|Matthews B W | [{"numValue":3.01,"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":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.0029 M, 0.017 M"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26137,"numValue":0.18,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26138,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,648 | train | mutant | 1,739 | 41 | 1,949 | 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 | R119M | R119M | 1 | 1 | 0 | 0 | 119 | R | M | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 3,297 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | null | KCl | 200 mM | 2LZM_A:R119M | 40 | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"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":"0.01 N","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":12135,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12136,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12137,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2650 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,650 | train | mutant | 1,739 | 41 | 1,949 | 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 | R119M | R119M | 1 | 1 | 0 | 0 | 119 | R | M | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 6,752 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 66.1 | KCl | 150 mM | 2LZM_A:R119M | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":66.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23974,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23975,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2651 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,651 | train | mutant | 1,739 | 41 | 1,949 | 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 | R119M | R119M | 1 | 1 | 0 | 0 | 119 | R | M | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 8,066 | ProTherm | 2 | CD | Thermal | HCl | 0.01 N | 40.9 | KCl | 200 mM | 2LZM_A:R119M | null | null | null | 0.3 | 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 | 89 | ARTICLE | Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. | 1,991 | 10.1021/bi00105a002 | 1911773 | Biochemistry;30;9816-28 | 4 | Nicholson H|Matthews B W|Dao-pin S|Anderson D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.9,"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":"0.01 N","type":"BUFFER_CONC"}... | [{"datasets":["capriotti_S1615_map.csv"],"id":27447,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27448,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2652 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,652 | train | mutant | 1,881 | 41 | 2,109 | 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 | R119C | R119C | 1 | 1 | 0 | 0 | 119 | R | C | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119 | A | H | false | false | 118.711391 | 46.192727 | 3,626 | ProTherm | 2.4 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R119C | 33.4 | -3 | 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|Broom_S605.csv|Saraboji_S1791.csv|STRUM_Q3421.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":13329,"numValue":33.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13330,"numValue":-3.0,"references":[],"strValue":null... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2653 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,653 | train | mutant | 6,703 | 41 | 7,345 | 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 | R119E|K135E | R119E|K135E | 2 | 2 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|135 | A | H|S | true | false | 132.70535 | 38.384975 | 14,444 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E | 49.4 | -1.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"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":53400,"numValue":49.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53401,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53402,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2654 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,654 | train | mutant | 6,703 | 41 | 7,345 | 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 | R119E|K135E | R119E|K135E | 2 | 2 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|135 | A | H|S | true | false | 132.70535 | 38.384975 | 14,452 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E | 64.1 | -2.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"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":53424,"numValue":64.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53425,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53426,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2655 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,655 | train | mutant | 6,703 | 41 | 7,345 | 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 | R119E|K135E | R119E|K135E | 2 | 2 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|135 | A | H|S | true | false | 132.70535 | 38.384975 | 14,889 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":66.7,"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":"20 mM","type"... | [{"datasets":[],"id":54913,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54914,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,656 | train | mutant | 6,703 | 41 | 7,345 | 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 | R119E|K135E | R119E|K135E | 2 | 2 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|135 | A | H|S | true | false | 132.70535 | 38.384975 | 15,036 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E | null | null | null | 0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":50.9,"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":"20 mM","type"... | [{"datasets":[],"id":55261,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55262,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,657 | train | mutant | 6,706 | 41 | 7,348 | 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 | R119E|K135E|K147E | R119E|K135E|K147E | 3 | 3 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|135|147 | A | H|S | true | false | 119.003919 | 35.950724 | 14,447 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | 50 | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":2.8,"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":53409,"numValue":50.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53410,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53411,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2658 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,658 | train | mutant | 6,706 | 41 | 7,348 | 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 | R119E|K135E|K147E | R119E|K135E|K147E | 3 | 3 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|135|147 | A | H|S | true | false | 119.003919 | 35.950724 | 14,455 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | 62.9 | -3.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"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":53433,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53434,"numValue":-3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53435,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,659 | train | mutant | 6,706 | 41 | 7,348 | 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 | R119E|K135E|K147E | R119E|K135E|K147E | 3 | 3 | 0 | 0 | 119 | R | E | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|135|147 | A | H|S | true | false | 119.003919 | 35.950724 | 14,892 | ProTherm | 5.3 | CD | Thermal | Potassium phosphate | 20 mM | 66.7 | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 8 | ARTICLE | Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability. | 1,991 | 10.1016/0022-2836(91)80181-s | 1942034 | J Mol Biol;221;873-87 | 5 | Baase W A|Dao-pin S|S?derlind E|Wozniak J A|Sauer U | [{"numValue":5.3,"strValue":null,"type":"PH"},{"numValue":66.7,"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":"20 mM","type"... | [{"datasets":[],"id":54919,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54920,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6926,"numValue":5.0,"position":135,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6938,"numValue":3.0,"position":147,"positionArray":null,"positionRang... |
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