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:2660 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,660 | 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 | 15,039 | ProTherm | 2.8 | CD | Thermal | Potassium phosphate | 20 mM | 50.9 | KCl | 25 mM | 2LZM_A:R119E 2LZM_A:K135E 2LZM_A:K147E | 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 | 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":55267,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55268,"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:2661 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,661 | train | mutant | 6,726 | 41 | 7,368 | 164 | 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|Q123A | R119A|Q123A | 2 | 2 | 0 | 0 | 119 | R | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|123 | A | H|T | false | false | 102.410167 | 38.959975 | 14,485 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:R119A 2LZM_A:Q123A | 51.14 | -0.51 | null | null | null | null | 110 | 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":53560,"numValue":51.14,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53561,"numValue":-0.51,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53562,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53563,"numValue":null,"reference... | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2662 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,662 | train | mutant | 6,726 | 41 | 7,368 | 164 | 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|Q123A | R119A|Q123A | 2 | 2 | 0 | 0 | 119 | R | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 119|123 | A | H|T | false | false | 102.410167 | 38.959975 | 15,025 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:R119A 2LZM_A:Q123A | null | null | null | 0.17 | 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":55233,"numValue":0.17,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55234,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6910,"numValue":4.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2663 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,663 | train | mutant | 184 | 41 | 212 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120A | M120A | 1 | 1 | 0 | 0 | 120 | M | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120 | A | H | true | false | 30.075331 | 22.774375 | 324 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:M120A | 51.07 | -0.58 | null | null | null | null | 112 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":1332,"numValue":51.07,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1333,"numValue":-0.58,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1334,"numValue":112.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2664 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,664 | train | mutant | 184 | 41 | 212 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120A | M120A | 1 | 1 | 0 | 0 | 120 | M | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120 | A | H | true | false | 30.075331 | 22.774375 | 7,554 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:M120A | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":26139,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26140,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,665 | train | mutant | 811 | 41 | 915 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120Y | M120Y | 1 | 1 | 0 | 0 | 120 | M | Y | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120 | A | H | true | false | 30.075331 | 22.774375 | 1,428 | ProTherm | 5.35 | CD | Thermal | sodium chloride, acetic acid, sodium acetate | 0.10 M, 1.4 mM, 8.6 mM | null | 2LZM_A:M120Y | 65.4 | -0.1 | null | null | null | null | 126 | 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":5215,"numValue":65.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":5216,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":5217,"numValue":126.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":5218,"numValue":null,"references":[],... | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2667 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,667 | train | mutant | 1,682 | 41 | 1,891 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120L | M120L | 1 | 1 | 0 | 0 | 120 | M | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120 | A | H | true | false | 30.075331 | 22.774375 | 3,148 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:M120L | 53.4 | 1.7 | null | null | null | null | 116 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":[],"id":11490,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11491,"numValue":1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11492,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,668 | train | mutant | 1,682 | 41 | 1,891 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120L | M120L | 1 | 1 | 0 | 0 | 120 | M | L | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120 | A | H | true | false | 30.075331 | 22.774375 | 7,813 | ProTherm | 3 | CD | Thermal | phosphoric acid, Potassium phosphate | 3 mM, 17 mM | 47 | KCl | 25 mM | 2LZM_A:M120L | null | null | null | -0.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes (>95%) | 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 | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid, Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValu... | [{"datasets":[],"id":26763,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26764,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26765,"numValue":null,"reference... | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2669 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,669 | train | mutant | 1,684 | 41 | 1,893 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120K | M120K | 1 | 1 | 0 | 0 | 120 | M | K | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120 | A | H | true | false | 30.075331 | 22.774375 | 3,150 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:M120K | 46.9 | -4.8 | null | null | null | null | 99 | null | null | null | null | null | null | null | null | null | yes (>95%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 291 | ARTICLE | Context-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme. | 1,998 | 10.1002/pro.5560070326 | 9541409 | Protein Sci;7;765-73 | 5 | Baase W A|Gassner N C|Lipscomb L A|Snow S D|Eldridge A M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":[],"id":11498,"numValue":46.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11499,"numValue":-4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11500,"numValue":99.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,671 | train | mutant | 6,723 | 41 | 7,365 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120A|Q122A | M120A|Q122A | 2 | 2 | 0 | 0 | 120 | M | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120|122 | A | H | true | false | 56.33212 | 29.173854 | 14,482 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:M120A 2LZM_A:Q122A | 50.9 | -0.75 | null | null | null | null | 108 | 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":53548,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53549,"numValue":-0.75,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53550,"numValue":108.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53551,"numValue":null,"references... | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2672 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,672 | train | mutant | 6,723 | 41 | 7,365 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | M120A|Q122A | M120A|Q122A | 2 | 2 | 0 | 0 | 120 | M | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 120|122 | A | H | true | false | 56.33212 | 29.173854 | 15,022 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:M120A 2LZM_A:Q122A | null | null | null | 0.25 | 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":55227,"numValue":0.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55228,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6911,"numValue":5.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2673 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,673 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 40 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 2LZM_A:L121A | 42.5 | -9.3 | null | null | null | 2.5 | 81 | 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":131,"numValue":42.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":132,"numValue":-9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":133,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":13... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,674 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 307 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 2LZM_A:L121A | 59.2 | -6.1 | null | null | null | 2.5 | 110 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"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":1260,"numValue":59.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1261,"numValue":-6.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1262,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2675 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,675 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 325 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:L121A | 42.5 | -9.15 | null | null | null | null | 81 | 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":1336,"numValue":42.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1337,"numValue":-9.15,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1338,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,676 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 2,034 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L121A | 59.1 | -6.2 | null | null | null | null | 108 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv"],"id":7612,"numValue":59.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S185... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,677 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 6,778 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.10 M | 2LZM_A:L121A | null | null | null | 2.3 | 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|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"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 mM... | [{"datasets":[],"id":24036,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24037,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24038,"numValue":null,"references":[],"strV... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2678 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,678 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 6,801 | 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:L121A | null | null | null | 2.2 | 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":24105,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24106,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24107,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2679 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,679 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 7,501 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | 51.8 | KCl | 0.025 M | 2LZM_A:L121A | null | null | null | 2.7 | null | 2.5 | 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 | 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":26000,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26001,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26002,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2680 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,680 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 7,555 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:L121A | null | null | null | 2.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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"],"id":26141,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26142,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,681 | train | mutant | 40 | 41 | 44 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A | L121A | 1 | 1 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 10,025 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:L121A | null | null | 10.7 | 4.2 | null | null | null | null | 2.6 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 664 | ARTICLE | Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. | 2,007 | 10.1110/ps.062632807 | 17400925 | Protein Sci;16;852-62 | 3 | Marqusee Susan|Cellitti Jason|Bernstein Rachel | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"B... | [{"datasets":[],"id":34437,"numValue":10.7,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34438,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34439,"numValue":2.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34440,"numValue":null,... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2682 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,682 | train | mutant | 167 | 41 | 195 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121M | L121M | 1 | 1 | 0 | 0 | 121 | L | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 304 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:L121M | 63.2 | -2.1 | null | null | null | 2.5 | 129 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Acetic acid,Sodium acetate,","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM,8.6 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValu... | [{"datasets":[],"id":1245,"numValue":63.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1246,"numValue":-2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1247,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,683 | train | mutant | 167 | 41 | 195 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121M | L121M | 1 | 1 | 0 | 0 | 121 | L | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121 | A | H | true | false | 1.074968 | 18.341875 | 6,775 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:L121M | null | null | null | 0.8 | 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":24027,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24028,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24029,"numValue":null,"references... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,684 | train | mutant | 6,718 | 41 | 7,360 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129L | L121A|A129L | 2 | 2 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129 | A | H | true | false | 0.705447 | 17.980937 | 14,477 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 2LZM_A:L121A 2LZM_A:A129L | 62.5 | -2.8 | null | null | null | 2.5 | 118 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"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":53525,"numValue":62.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53526,"numValue":-2.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53527,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53528,"numValue":118.0,"references":[... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,685 | train | mutant | 6,718 | 41 | 7,360 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129L | L121A|A129L | 2 | 2 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129 | A | H | true | false | 0.705447 | 17.980937 | 14,908 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.10 M | 2LZM_A:L121A 2LZM_A:A129L | null | null | null | 1.1 | null | 2.5 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"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 mM... | [{"datasets":[],"id":54960,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54961,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54962,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,686 | train | mutant | 6,719 | 41 | 7,361 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129M | L121A|A129M | 2 | 2 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129 | A | H | true | false | 0.705447 | 17.980937 | 14,478 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 2LZM_A:L121A 2LZM_A:A129M | 62.6 | -2.7 | null | null | null | 2.5 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"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":53530,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53531,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53532,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53533,"numValue":121.0,"references":[... | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2688 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,688 | train | mutant | 6,727 | 41 | 7,369 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121M|A129L|L133M|V149I|F153W | L121M|A129L|L133M|V149I|F153W | 5 | 5 | 0 | 0 | 121 | L | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|149|153 | A | H | true | false | 0.817885 | 16.293407 | 14,486 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 2LZM_A:L121M 2LZM_A:A129L 2LZM_A:L133M 2LZM_A:V149I 2LZM_A:F153W | 51.7 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53564,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53565,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,689 | train | mutant | 6,727 | 41 | 7,369 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121M|A129L|L133M|V149I|F153W | L121M|A129L|L133M|V149I|F153W | 5 | 5 | 0 | 0 | 121 | L | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|149|153 | A | H | true | false | 0.817885 | 16.293407 | 15,010 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121M 2LZM_A:A129L 2LZM_A:L133M 2LZM_A:V149I 2LZM_A:F153W | null | null | null | 1.3 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55203,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55204,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,690 | train | mutant | 6,728 | 41 | 7,370 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121I|A129L|L133M|F153W | L121I|A129L|L133M|F153W | 4 | 4 | 0 | 0 | 121 | L | I | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|153 | A | H | true | false | 0.955171 | 17.178366 | 14,487 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 2LZM_A:L121I 2LZM_A:A129L 2LZM_A:L133M 2LZM_A:F153W | 51.7 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53566,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53567,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,691 | train | mutant | 6,728 | 41 | 7,370 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121I|A129L|L133M|F153W | L121I|A129L|L133M|F153W | 4 | 4 | 0 | 0 | 121 | L | I | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|153 | A | H | true | false | 0.955171 | 17.178366 | 15,011 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121I 2LZM_A:A129L 2LZM_A:L133M 2LZM_A:F153W | null | null | null | 1.3 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55205,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55206,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,692 | train | mutant | 6,729 | 41 | 7,371 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129M|V149I | L121A|A129M|V149I | 3 | 3 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|149 | A | H | true | false | 0.559879 | 16.238482 | 14,488 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 2LZM_A:L121A 2LZM_A:A129M 2LZM_A:V149I | 51.7 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53568,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53569,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,693 | train | mutant | 6,729 | 41 | 7,371 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129M|V149I | L121A|A129M|V149I | 3 | 3 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|149 | A | H | true | false | 0.559879 | 16.238482 | 15,012 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121A 2LZM_A:A129M 2LZM_A:V149I | null | null | null | 1.4 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55207,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55208,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,694 | train | mutant | 6,730 | 41 | 7,372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121I|A129W|L133M | L121I|A129W|L133M | 3 | 3 | 0 | 0 | 121 | L | I | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133 | A | H | true | false | 1.030177 | 17.241458 | 14,489 | ProTherm | 3 | CD | Thermal | Potassium phosphate | null | KCl | 0.2 M | 2LZM_A:L121I 2LZM_A:A129W 2LZM_A:L133M | 51.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"... | [{"datasets":[],"id":53570,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53571,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | ||||||||||||
fireprotdb:2695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,695 | train | mutant | 6,730 | 41 | 7,372 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121I|A129W|L133M | L121I|A129W|L133M | 3 | 3 | 0 | 0 | 121 | L | I | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133 | A | H | true | false | 1.030177 | 17.241458 | 15,013 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121I 2LZM_A:A129W 2LZM_A:L133M | null | null | null | 1.4 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55209,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55210,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,696 | train | mutant | 6,731 | 41 | 7,373 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129V|L133M|F153L | L121A|A129V|L133M|F153L | 4 | 4 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|153 | A | H | true | false | 0.955171 | 17.178366 | 14,490 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 2LZM_A:L121A 2LZM_A:A129V 2LZM_A:L133M 2LZM_A:F153L | 51.7 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53572,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53573,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,697 | train | mutant | 6,731 | 41 | 7,373 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129V|L133M|F153L | L121A|A129V|L133M|F153L | 4 | 4 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|153 | A | H | true | false | 0.955171 | 17.178366 | 15,014 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121A 2LZM_A:A129V 2LZM_A:L133M 2LZM_A:F153L | null | null | null | 2.3 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55211,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55212,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,698 | train | mutant | 6,732 | 41 | 7,374 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121M|L133V|F153L | L121M|L133V|F153L | 3 | 3 | 0 | 0 | 121 | L | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|133|153 | A | H | true | false | 1.161585 | 17.031155 | 14,491 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 2LZM_A:L121M 2LZM_A:L133V 2LZM_A:F153L | 51.7 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53574,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53575,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,699 | train | mutant | 6,732 | 41 | 7,374 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121M|L133V|F153L | L121M|L133V|F153L | 3 | 3 | 0 | 0 | 121 | L | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|133|153 | A | H | true | false | 1.161585 | 17.031155 | 15,015 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121M 2LZM_A:L133V 2LZM_A:F153L | null | null | null | 2.5 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55213,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55214,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2700 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,700 | train | mutant | 6,733 | 41 | 7,375 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129L|L133A|F153L | L121A|A129L|L133A|F153L | 4 | 4 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|153 | A | H | true | false | 0.955171 | 17.178366 | 14,492 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 0.2 M | 2LZM_A:L121A 2LZM_A:A129L 2LZM_A:L133A 2LZM_A:F153L | 51.7 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53576,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53577,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2701 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,701 | train | mutant | 6,733 | 41 | 7,375 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129L|L133A|F153L | L121A|A129L|L133A|F153L | 4 | 4 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|133|153 | A | H | true | false | 0.955171 | 17.178366 | 15,016 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121A 2LZM_A:A129L 2LZM_A:L133A 2LZM_A:F153L | null | null | null | 3.5 | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55215,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55216,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6924,"numValue":7.0,"position":133,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2702 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,702 | train | mutant | 6,982 | 41 | 7,634 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L121A|A129M|F153L | L121A|A129M|F153L | 3 | 3 | 0 | 0 | 121 | L | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 121|129|153 | A | H | true | false | 0.713682 | 17.650322 | 15,009 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 0.2 M | 2LZM_A:L121A 2LZM_A:A129M 2LZM_A:F153L | 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 | 900 | ARTICLE | The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. | 1,993 | 10.1126/science.8259514 | 8259514 | Science;262;1715-8 | 4 | Hajiseyedjavadi O|Baase W A|Baldwin E P|Matthews B W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":55201,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55202,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6912,"numValue":6.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2703 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,703 | train | mutant | 185 | 41 | 213 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q122A | Q122A | 1 | 1 | 0 | 0 | 122 | Q | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 122 | A | H | false | false | 82.588909 | 35.573333 | 326 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:Q122A | 50.94 | -0.71 | null | null | null | null | 108 | 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":1340,"numValue":50.94,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1341,"numValue":-0.71,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1342,"numValue":108.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,704 | train | mutant | 185 | 41 | 213 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q122A | Q122A | 1 | 1 | 0 | 0 | 122 | Q | A | 3 | CONSERVATION | 1L63|2LZM | 49|80 | null | 122 | A | H | false | false | 82.588909 | 35.573333 | 7,556 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:Q122A | null | null | null | 0.24 | 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":26143,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26144,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6913,"numValue":3.0,"position":122,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,705 | train | mutant | 186 | 41 | 214 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q123A | Q123A | 1 | 1 | 0 | 0 | 123 | Q | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 123 | A | T|H | false | false | 86.108942 | 31.727222 | 327 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4, | 0.0029 M,0.017 M, | null | KCl | 0.025 M | 2LZM_A:Q123A | 51.01 | -0.64 | null | null | null | null | 111 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 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":1344,"numValue":51.01,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1345,"numValue":-0.64,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1346,"numValue":111.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,706 | train | mutant | 186 | 41 | 214 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q123A | Q123A | 1 | 1 | 0 | 0 | 123 | Q | A | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 123 | A | T|H | false | false | 86.108942 | 31.727222 | 7,557 | ProTherm | 3.01 | CD | Thermal | H3PO4,KH2PO4 | 0.0029 M, 0.017 M | 51.65 | KCl | 0.025 M | 2LZM_A:Q123A | null | null | null | 0.22 | 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":26145,"numValue":0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26146,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,707 | train | mutant | 1,773 | 41 | 1,986 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q123E | Q123E | 1 | 1 | 0 | 0 | 123 | Q | E | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 123 | A | T|H | false | false | 86.108942 | 31.727222 | 3,407 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:Q123E | 41.4 | 1 | null | null | null | null | 82 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S2204.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":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":12567,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12568,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":... | [{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,709 | train | mutant | 1,773 | 41 | 1,986 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q123E | Q123E | 1 | 1 | 0 | 0 | 123 | Q | E | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 123 | A | T|H | false | false | 86.108942 | 31.727222 | 3,409 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | null | KCl | 0.15 M | 2LZM_A:Q123E | 65.8 | 1.2 | null | null | null | null | 132 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":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":12575,"numValue":65.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12576,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12577,"numValue":132.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2710 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,710 | train | mutant | 1,773 | 41 | 1,986 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q123E | Q123E | 1 | 1 | 0 | 0 | 123 | Q | E | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 123 | A | T|H | false | false | 86.108942 | 31.727222 | 6,716 | ProTherm | 5.5 | CD | Thermal | acetate | 10 mM | 66.7 | KCl | 0.15 M | 2LZM_A:Q123E | null | null | null | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":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":23875,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23876,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2711 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,711 | train | mutant | 1,773 | 41 | 1,986 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q123E | Q123E | 1 | 1 | 0 | 0 | 123 | Q | E | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 123 | A | T|H | false | false | 86.108942 | 31.727222 | 7,021 | ProTherm | 6.5 | CD | Thermal | Potassium phosphate | 10 mM | 64.5 | KCl | 0.15 M | 2LZM_A:Q123E | null | null | null | -0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|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":6.5,"strValue":null,"type":"PH"},{"numValue":64.5,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24702,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24703,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2712 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,712 | train | mutant | 1,773 | 41 | 1,986 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | Q123E | Q123E | 1 | 1 | 0 | 0 | 123 | Q | E | 2 | CONSERVATION | 1L63|2LZM | 49|80 | null | 123 | A | T|H | false | false | 86.108942 | 31.727222 | 8,079 | ProTherm | 2 | CD | Thermal | HCl | 10 mM | 40.4 | KCl | 0.15 M | 2LZM_A:Q123E | 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 | 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"],"id":27476,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27477,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6914,"numValue":2.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,713 | train | mutant | 433 | 41 | 479 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K124G | K124G | 1 | 1 | 0 | 0 | 124 | K | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 124 | A | T | false | false | 100.672296 | 17.396667 | 704 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 2LZM_A:K124G | 41.9 | 0 | 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 | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":2735,"numValue":41.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":2736,"numValue":0.0,"references":[],"strValue":null,"type... | [{"id":6915,"numValue":4.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2714 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,714 | train | mutant | 433 | 41 | 479 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K124G | K124G | 1 | 1 | 0 | 0 | 124 | K | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 124 | A | T | false | false | 100.672296 | 17.396667 | 706 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | null | KCl | 100 mM | 2LZM_A:K124G | 64.5 | -0.2 | 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 | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":2741,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":2742,"numValue":-0.2,"references":[],"strValue":null,"typ... | [{"id":6915,"numValue":4.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,715 | train | mutant | 433 | 41 | 479 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K124G | K124G | 1 | 1 | 0 | 0 | 124 | K | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 124 | A | T | false | false | 100.672296 | 17.396667 | 6,984 | ProTherm | 6.5 | CD | Thermal | KH2PO4 | 100 mM | 64.7 | KCl | 100 mM | 2LZM_A:K124G | 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 | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":64.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24614,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24615,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6915,"numValue":4.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,716 | train | mutant | 433 | 41 | 479 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K124G | K124G | 1 | 1 | 0 | 0 | 124 | K | G | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 124 | A | T | false | false | 100.672296 | 17.396667 | 8,032 | ProTherm | 2 | CD | Thermal | KH2PO4 | 100 mM | 41.9 | KCl | 100 mM | 2LZM_A:K124G | null | null | null | 0 | 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 | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 78 | ARTICLE | Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme. | 1,989 | 10.1016/0022-2836(89)90299-4 | 2511328 | J Mol Biol;210;181-93 | 4 | Nicholson H|Matthews B W|S?derlind E|Tronrud D E | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":41.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv"],"id":27379,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":27380,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY... | [{"id":6915,"numValue":4.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,717 | train | mutant | 5,835 | 41 | 6,400 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W126R | W126R | 1 | 1 | 0 | 0 | 126 | W | R | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 126 | A | H | true | false | 48.863155 | 18.299286 | 12,617 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:W126R | null | null | null | 5.74 | null | null | null | 3.4 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 809 | ARTICLE | Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates. | 1,991 | 10.1021/bi00216a038 | 1988046 | Biochemistry;30;589-94 | 4 | Alber T|Wozniak J A|Goldenberg D P|Klemm J D | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":22.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Gel electrophoresis","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"imidazole,MOPS,","type":"BUFFER"},{"numValue":null,"strValue":"0.0... | [{"datasets":["SAAFEC_S1262.csv"],"id":45754,"numValue":5.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45755,"numValue":3.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45756,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6917,"numValue":5.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,718 | train | mutant | 6,713 | 41 | 7,355 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y|W126Y|W158Y | W138Y|W126Y|W158Y | 3 | 3 | 0 | 0 | 138 | W | Y | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 126|138|158 | A | H|S | true | true | 34.273639 | 18.085476 | 14,466 | ProTherm | 2 | CD | Thermal | Unknown | null | 2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y | 46.85 | null | null | null | null | 2.1 | 113 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":53479,"numValue":46.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53480,"numValue":2.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53481,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53482,"numValue":null,"references"... | [{"id":6917,"numValue":5.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6949,"numValue":5.0,"position":158,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:2719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,719 | train | mutant | 6,713 | 41 | 7,355 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y|W126Y|W158Y | W138Y|W126Y|W158Y | 3 | 3 | 0 | 0 | 138 | W | Y | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 126|138|158 | A | H|S | true | true | 34.273639 | 18.085476 | 14,467 | ProTherm | 2 | CD | Thermal | Unknown | null | 2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y | 30 | -7 | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":53483,"numValue":30.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53484,"numValue":-7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53485,"numValue":2.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53486,"numValue":null,"references":[]... | [{"id":6917,"numValue":5.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6949,"numValue":5.0,"position":158,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:2720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,720 | train | mutant | 6,713 | 41 | 7,355 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y|W126Y|W158Y | W138Y|W126Y|W158Y | 3 | 3 | 0 | 0 | 138 | W | Y | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 126|138|158 | A | H|S | true | true | 34.273639 | 18.085476 | 14,511 | ProTherm | 2.2 | CD | Thermal | Sodium phosphate | 0.2 M | null | NaCl | 0.5 M | 2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y | 36 | -6.6 | null | null | null | null | 85.3 | 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 | 59 | ARTICLE | Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. | 1,977 | 10.1016/0005-2795(77)90166-0 | 911878 | Biochim Biophys Acta;494;367-83 | 2 | Schellman J A|Elwell M L | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":53632,"numValue":36.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53633,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53634,"numValue":85.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53635,"numValue":null,"references":... | [{"id":6917,"numValue":5.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6949,"numValue":5.0,"position":158,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2721 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,721 | train | mutant | 6,713 | 41 | 7,355 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y|W126Y|W158Y | W138Y|W126Y|W158Y | 3 | 3 | 0 | 0 | 138 | W | Y | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 126|138|158 | A | H|S | true | true | 34.273639 | 18.085476 | 14,512 | ProTherm | 2.5 | CD | Thermal | Sodium phosphate | 0.2 M | null | NaCl | 0.5 M | 2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y | 40 | -6.2 | null | null | null | null | 89.2 | 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 | 59 | ARTICLE | Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. | 1,977 | 10.1016/0005-2795(77)90166-0 | 911878 | Biochim Biophys Acta;494;367-83 | 2 | Schellman J A|Elwell M L | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":53636,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53637,"numValue":-6.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53638,"numValue":89.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53639,"numValue":null,"references":... | [{"id":6917,"numValue":5.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6949,"numValue":5.0,"position":158,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,722 | train | mutant | 6,713 | 41 | 7,355 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y|W126Y|W158Y | W138Y|W126Y|W158Y | 3 | 3 | 0 | 0 | 138 | W | Y | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 126|138|158 | A | H|S | true | true | 34.273639 | 18.085476 | 14,513 | ProTherm | 2.2 | CD | Thermal | Sodium phosphate | 0.2 M | null | NaCl | 0.5 M | 2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y | 36 | -6.6 | null | 1.82 | null | null | 85.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|DDG|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 59 | ARTICLE | Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. | 1,977 | 10.1016/0005-2795(77)90166-0 | 911878 | Biochim Biophys Acta;494;367-83 | 2 | Schellman J A|Elwell M L | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":53640,"numValue":36.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53641,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53642,"numValue":85.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53643,"numValue":1.82,"references":... | [{"id":6917,"numValue":5.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6949,"numValue":5.0,"position":158,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,723 | train | mutant | 6,713 | 41 | 7,355 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | W138Y|W126Y|W158Y | W138Y|W126Y|W158Y | 3 | 3 | 0 | 0 | 138 | W | Y | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 126|138|158 | A | H|S | true | true | 34.273639 | 18.085476 | 14,514 | ProTherm | 2.5 | CD | Thermal | Sodium phosphate | 0.2 M | null | NaCl | 0.5 M | 2LZM_A:W126Y 2LZM_A:W138Y 2LZM_A:W158Y | 40 | -6.2 | null | 1.77 | null | null | 89.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|DDG|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 59 | ARTICLE | Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. | 1,977 | 10.1016/0005-2795(77)90166-0 | 911878 | Biochim Biophys Acta;494;367-83 | 2 | Schellman J A|Elwell M L | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":53645,"numValue":40.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53646,"numValue":-6.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53647,"numValue":89.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53648,"numValue":1.77,"references":... | [{"id":6917,"numValue":5.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6929,"numValue":9.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6949,"numValue":5.0,"position":158,"positionArray":null,"positionRang... | |||||||||||
fireprotdb:2724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,724 | train | mutant | 6,745 | 41 | 7,387 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A | D127A|E128A | 2 | 2 | 0 | 0 | 127 | D | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128 | A | H | false | false | 92.567478 | 31.960625 | 14,517 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:D127A 2LZM_A:E128A | 41.65 | 0.9 | null | null | null | 2.4 | 85.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53657,"numValue":41.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53658,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53659,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53660,"numValue":85.8,"references":[]... | [{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2725 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,725 | train | mutant | 6,745 | 41 | 7,387 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A | D127A|E128A | 2 | 2 | 0 | 0 | 127 | D | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128 | A | H | false | false | 92.567478 | 31.960625 | 15,102 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:D127A 2LZM_A:E128A | null | null | null | -0.24 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":55419,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55420,"numValue":-0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55421,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,726 | train | mutant | 6,749 | 41 | 7,391 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A | D127A|E128A|V131A|N132A | 4 | 4 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132 | A | H | true | false | 80.541743 | 25.290692 | 14,521 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | 44.75 | 4 | null | null | null | 2.4 | 86.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53677,"numValue":44.75,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53678,"numValue":4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53679,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53680,"numValue":86.3,"references":[]... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2727 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,727 | train | mutant | 6,749 | 41 | 7,391 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A | D127A|E128A|V131A|N132A | 4 | 4 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132 | A | H | true | false | 80.541743 | 25.290692 | 15,106 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -1.01 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":55431,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55432,"numValue":-1.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55433,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,728 | train | mutant | 6,749 | 41 | 7,391 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A | D127A|E128A|V131A|N132A | 4 | 4 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132 | A | H | true | false | 80.541743 | 25.290692 | 15,784 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | 55.8 | 2.4 | null | null | null | 1.8 | 129 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57948,"numValue":55.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57949,"numValue":2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57950,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57951,"numValue":129.0,"references":[]... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,729 | train | mutant | 6,749 | 41 | 7,391 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A | D127A|E128A|V131A|N132A | 4 | 4 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132 | A | H | true | false | 80.541743 | 25.290692 | 16,776 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -0.85 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61663,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61664,"numValue":-0.85,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61665,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2730 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,730 | train | mutant | 6,751 | 41 | 7,393 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A|L133A | D127A|E128A|V131A|N132A|L133A | 5 | 5 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132|133 | A | H | true | false | 64.769322 | 23.385053 | 14,523 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | 31.35 | -9.4 | null | null | null | 2.4 | 62.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53687,"numValue":31.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53688,"numValue":-9.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53689,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53690,"numValue":62.2,"references":[... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,731 | train | mutant | 6,751 | 41 | 7,393 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A|L133A | D127A|E128A|V131A|N132A|L133A | 5 | 5 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132|133 | A | H | true | false | 64.769322 | 23.385053 | 15,108 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | null | null | null | 2.27 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":55437,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55438,"numValue":2.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55439,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2732 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,732 | train | mutant | 6,751 | 41 | 7,393 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A|L133A | D127A|E128A|V131A|N132A|L133A | 5 | 5 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132|133 | A | H | true | false | 64.769322 | 23.385053 | 15,786 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | 46.4 | -7 | null | null | null | 1.8 | 103 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57958,"numValue":46.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57959,"numValue":-7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57960,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57961,"numValue":103.0,"references":[... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,733 | train | mutant | 6,751 | 41 | 7,393 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A|L133A | D127A|E128A|V131A|N132A|L133A | 5 | 5 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132|133 | A | H | true | false | 64.769322 | 23.385053 | 16,778 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | null | null | null | 2.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61669,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61670,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61671,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,734 | train | mutant | 7,393 | 41 | 8,076 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | D127A|E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | 9 | 9 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132|135|136|139|140|141 | A | H|S | true | true | 82.359145 | 24.304791 | 15,787 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:K135A 2LZM_A:S136A 2LZM_A:Y139A 2LZM_A:N140A 2LZM_A:Q141A | 52.6 | -0.8 | null | null | null | 1.8 | 103 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57963,"numValue":52.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57964,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57965,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57966,"numValue":103.0,"references":[... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2735 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,735 | train | mutant | 7,393 | 41 | 8,076 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | D127A|E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | 9 | 9 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132|135|136|139|140|141 | A | H|S | true | true | 82.359145 | 24.304791 | 16,780 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:K135A 2LZM_A:S136A 2LZM_A:Y139A 2LZM_A:N140A 2LZM_A:Q141A | null | null | null | 0.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61675,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61676,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61677,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,736 | train | mutant | 7,889 | 41 | 8,602 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D127A|E128A|V131A|N132A|K135A|S136A | D127A|E128A|V131A|N132A|K135A|S136A | 6 | 6 | 0 | 0 | 127 | D | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 127|128|131|132|135|136 | A | H|S | true | false | 81.700254 | 24.361109 | 16,779 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:D127A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:K135A 2LZM_A:S136A | null | null | null | 0.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61672,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61673,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61674,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6918,"numValue":1.0,"position":127,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,737 | train | mutant | 133 | 41 | 151 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128K | E128K | 1 | 1 | 0 | 0 | 128 | E | K | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 245 | ProTherm | 3 | CD | Thermal | Unknown | null | 2LZM_A:E128K | 46.85 | null | null | null | null | 2.25 | 78.5 | null | null | null | null | null | null | null | null | null | Unknown | TM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:E128K","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":1002,"numValue":46.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1003,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1004,"numValue":78.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1005,"numValue":null,"references":[],... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:2738 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,738 | train | mutant | 133 | 41 | 151 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128K | E128K | 1 | 1 | 0 | 0 | 128 | E | K | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 250 | ProTherm | 3 | CD | Thermal | Unknown | null | 2LZM_A:E128K | 54 | -5 | null | null | null | 2.25 | 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|_PDB_CHAIN_MUTATION | 22 | ARTICLE | Mutations and protein stability. | 1,981 | 10.1002/bip.1981.360200921 | 7306671 | Biopolymers;20;1989-99 | 4 | Lindorfer M|Hawkes R|Grutter M|Schellman J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:E128K","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":1022,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1023,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1024,"numValue":2.25,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,739 | train | mutant | 133 | 41 | 151 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128K | E128K | 1 | 1 | 0 | 0 | 128 | E | K | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 477 | ProTherm | 3 | CD | Thermal | Unknown | null | NaCl | 0.2 M | 2LZM_A:E128K | 51.5 | 5.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 51 | ARTICLE | Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. | 1,984 | 10.1016/0022-2836(84)90474-1 | 6726809 | J Mol Biol;175;195-212 | 3 | Hawkes R|Schellman J|Grutter M G | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":1916,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1917,"numValue":5.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1918,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2740 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,740 | train | mutant | 133 | 41 | 151 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128K | E128K | 1 | 1 | 0 | 0 | 128 | E | K | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 7,796 | ProTherm | 3 | CD | Thermal | Unknown | 47 | NaCl | 0.2 M | 2LZM_A:E128K | null | null | 1.19 | 1.16 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 51 | ARTICLE | Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. | 1,984 | 10.1016/0022-2836(84)90474-1 | 6726809 | J Mol Biol;175;195-212 | 3 | Hawkes R|Schellman J|Grutter M G | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"num... | [{"datasets":[],"id":26725,"numValue":1.19,"references":[],"strValue":null,"type":"DG"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26726,"numValue":1.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26727,"numValue":null,"reference... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2741 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,741 | train | mutant | 333 | 41 | 371 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A | E128A | 1 | 1 | 0 | 0 | 128 | E | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 582 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:E128A | 41.35 | 0.6 | null | null | null | 2.4 | 85 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":2315,"numValue":41.35,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2316,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2317,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,742 | train | mutant | 333 | 41 | 371 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A | E128A | 1 | 1 | 0 | 0 | 128 | E | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 3,498 | ProTherm | 2 | CD | Thermal | HCl | null | KCl | 0.20 M | 2LZM_A:E128A | 41.4 | 0.6 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"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":"KCl","type":"ION"},{"numValue":null,"strValue":"0.20 M","type":"ION_CONC"},{"numValue":n... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12873,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12874,"numValue":0.6,"references":[],"strValue":null... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,743 | train | mutant | 333 | 41 | 371 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A | E128A | 1 | 1 | 0 | 0 | 128 | E | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 8,068 | ProTherm | 2 | CD | Thermal | HCl | 40.8 | KCl | 0.20 M | 2LZM_A:E128A | null | null | null | -0.16 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":27451,"numValue":-0.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27452,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,744 | train | mutant | 333 | 41 | 371 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A | E128A | 1 | 1 | 0 | 0 | 128 | E | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128 | A | H | false | false | 91.299709 | 38.55 | 8,070 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:E128A | null | null | null | -0.16 | null | 2.4 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":27455,"numValue":2.4,"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":27456,"numValue":-0.16,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27457,"nu... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2745 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,745 | train | mutant | 6,746 | 41 | 7,388 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A | E128A|V131A | 2 | 2 | 0 | 0 | 128 | E | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131 | A | H | true | false | 92.923807 | 29.056071 | 14,518 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:E128A 2LZM_A:V131A | 42.25 | 1.5 | null | null | null | 2.4 | 93 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53662,"numValue":42.25,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53663,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53664,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53665,"numValue":93.0,"references":[]... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2746 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,746 | train | mutant | 6,746 | 41 | 7,388 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A | E128A|V131A | 2 | 2 | 0 | 0 | 128 | E | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131 | A | H | true | false | 92.923807 | 29.056071 | 14,718 | ProTherm | 2 | CD | Thermal | HCl | null | KCl | 0.20 M | 2LZM_A:E128A 2LZM_A:V131A | 42.3 | 1.5 | null | null | null | null | 93 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"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":"KCl","type":"ION"},{"numValue":null,"strValue":"0.20 M","type":"ION_CONC"},{"numValue":n... | [{"datasets":[],"id":54423,"numValue":42.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54424,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54425,"numValue":93.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54426,"numValue":null,"references":[... | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,747 | train | mutant | 6,746 | 41 | 7,388 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A | E128A|V131A | 2 | 2 | 0 | 0 | 128 | E | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131 | A | H | true | false | 92.923807 | 29.056071 | 15,099 | ProTherm | 2 | CD | Thermal | HCl | 40.8 | KCl | 0.20 M | 2LZM_A:E128A 2LZM_A:V131A | null | null | null | -0.41 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":55413,"numValue":-0.41,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55414,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2749 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,749 | train | mutant | 6,748 | 41 | 7,390 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A | E128A|V131A|N132A | 3 | 3 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132 | A | H | true | false | 76.110575 | 25.263839 | 14,520 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | 44.15 | 3.4 | null | null | null | 2.4 | 88.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53672,"numValue":44.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53673,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53674,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53675,"numValue":88.3,"references":[]... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2750 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,750 | train | mutant | 6,748 | 41 | 7,390 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A | E128A|V131A|N132A | 3 | 3 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132 | A | H | true | false | 76.110575 | 25.263839 | 14,720 | ProTherm | 2 | CD | Thermal | HCl | null | KCl | 0.20 M | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | 44.2 | 3.4 | null | null | null | null | 88.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"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":"KCl","type":"ION"},{"numValue":null,"strValue":"0.20 M","type":"ION_CONC"},{"numValue":n... | [{"datasets":[],"id":54431,"numValue":44.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54432,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54433,"numValue":88.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54434,"numValue":null,"references":[... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,751 | train | mutant | 6,748 | 41 | 7,390 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A | E128A|V131A|N132A | 3 | 3 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132 | A | H | true | false | 76.110575 | 25.263839 | 15,101 | ProTherm | 2 | CD | Thermal | HCl | 40.8 | KCl | 0.20 M | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -0.94 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 314 | ARTICLE | Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme. | 1,991 | 10.1021/bi00222a001 | 1998663 | Biochemistry;30;2012-7 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":40.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue... | [{"datasets":[],"id":55417,"numValue":-0.94,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55418,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,752 | train | mutant | 6,748 | 41 | 7,390 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A | E128A|V131A|N132A | 3 | 3 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132 | A | H | true | false | 76.110575 | 25.263839 | 15,105 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -0.91 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":55428,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55429,"numValue":-0.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55430,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,754 | train | mutant | 6,748 | 41 | 7,390 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A | E128A|V131A|N132A | 3 | 3 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132 | A | H | true | false | 76.110575 | 25.263839 | 16,775 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | -0.9 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61660,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61661,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61662,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2755 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,755 | train | mutant | 6,750 | 41 | 7,392 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A|L133A | E128A|V131A|N132A|L133A | 4 | 4 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132|133 | A | H | true | false | 57.50284 | 22.888504 | 14,522 | ProTherm | 2.02 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | 30.45 | -10.3 | null | null | null | 2.4 | 63.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValu... | [{"datasets":[],"id":53682,"numValue":30.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53683,"numValue":-10.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53684,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53685,"numValue":63.9,"references":... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2756 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,756 | train | mutant | 6,750 | 41 | 7,392 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A|L133A | E128A|V131A|N132A|L133A | 4 | 4 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132|133 | A | H | true | false | 57.50284 | 22.888504 | 15,107 | ProTherm | 2.02 | CD | Thermal | Unknown | 40.75 | KCl | 0.2 M | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | null | null | null | 2.59 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 63 | ARTICLE | Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. | 1,992 | 10.1002/pro.5560010608 | 1304917 | Protein Sci;1;761-76 | 3 | Baase W A|Zhang X J|Matthews B W | [{"numValue":2.02,"strValue":null,"type":"PH"},{"numValue":40.75,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":55434,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55435,"numValue":2.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55436,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | ||||||||||||
fireprotdb:2757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,757 | train | mutant | 6,750 | 41 | 7,392 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A|L133A | E128A|V131A|N132A|L133A | 4 | 4 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132|133 | A | H | true | false | 57.50284 | 22.888504 | 15,785 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | 46.4 | -7 | null | null | null | 1.8 | 102 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57953,"numValue":46.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57954,"numValue":-7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57955,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57956,"numValue":102.0,"references":[... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2758 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,758 | train | mutant | 6,750 | 41 | 7,392 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A|L133A | E128A|V131A|N132A|L133A | 4 | 4 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132|133 | A | H | true | false | 57.50284 | 22.888504 | 16,777 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:L133A | null | null | null | 2.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61666,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61667,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61668,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,759 | train | mutant | 7,394 | 41 | 8,077 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | 8 | 8 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132|135|136|139|140|141 | A | H|S | true | true | 80.924632 | 24.171483 | 15,788 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:K135A 2LZM_A:S136A 2LZM_A:Y139A 2LZM_A:N140A 2LZM_A:Q141A | 52.5 | -0.9 | null | null | null | 1.8 | 102 | null | null | null | null | null | null | null | null | null | yes(>90%) | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":57968,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57969,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57970,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":57971,"numValue":102.0,"references":[... | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,760 | train | mutant | 7,394 | 41 | 8,077 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | E128A|V131A|N132A|K135A|S136A|Y139A|N140A|Q141A | 8 | 8 | 0 | 0 | 128 | E | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 128|131|132|135|136|139|140|141 | A | H|S | true | true | 80.924632 | 24.171483 | 16,781 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A 2LZM_A:K135A 2LZM_A:S136A 2LZM_A:Y139A 2LZM_A:N140A 2LZM_A:Q141A | null | null | null | 0.5 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | yes(>90%) | DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 171 | ARTICLE | A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. | 2,002 | 10.1016/s0301-4622(02)00193-x | 12487988 | Biophys Chem;101-102;43-56 | 3 | Baase Walter A|Matthews Brian W|Zhang Xue-jun | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":53.4,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KPO4","type":"BUFFER"},{"numValue":null,"strValue":"20.0 mM","type":"BUFFER_CONC... | [{"datasets":[],"id":61678,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61679,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61680,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6919,"numValue":1.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6922,"numValue":2.0,"position":131,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2761 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,761 | train | mutant | 170 | 41 | 198 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129L | A129L | 1 | 1 | 0 | 0 | 129 | A | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 308 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 2LZM_A:A129L | 62.1 | -3.2 | null | null | null | 2.5 | 112 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"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":1265,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1266,"numValue":-3.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1267,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,763 | train | mutant | 170 | 41 | 198 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129L | A129L | 1 | 1 | 0 | 0 | 129 | A | L | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 6,779 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.10 M | 2LZM_A:A129L | null | null | null | 1.3 | null | 2.5 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"numValue":5.4,"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 mM... | [{"datasets":[],"id":24039,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24040,"numValue":1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24041,"numValue":null,"references... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2764 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,764 | train | mutant | 171 | 41 | 199 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129M | A129M | 1 | 1 | 0 | 0 | 129 | A | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 309 | ProTherm | 5.4 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.10 M | 2LZM_A:A129M | 60.1 | -5.2 | null | null | null | 2.5 | 110 | 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 | 34 | ARTICLE | Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme. | 1,996 | 10.1006/jmbi.1996.0338 | 8676387 | J Mol Biol;259;542-59 | 5 | Baldwin E|Xu J|Hajiseyedjavadi O|Baase W A|Matthews B W | [{"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":1270,"numValue":60.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1271,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1272,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,765 | train | mutant | 171 | 41 | 199 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129M | A129M | 1 | 1 | 0 | 0 | 129 | A | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 2,046 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:A129M | 60.1 | -5.2 | 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 | 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":[],"id":7672,"numValue":60.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7673,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":7674,"numValue":109.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":7675,"numValue":2.0,"references":[],"... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2766 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,766 | train | mutant | 171 | 41 | 199 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A129M | A129M | 1 | 1 | 0 | 0 | 129 | A | M | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 129 | A | H | true | false | 0.335927 | 17.62 | 3,785 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A129M | 46.2 | -5.5 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 350 | ARTICLE | The introduction of strain and its effects on the structure and stability of T4 lysozyme. | 2,000 | 10.1006/jmbi.1999.3300 | 10623513 | J Mol Biol;295;127-45 | 3 | Liu R|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphoric acid,Potassium phosphate,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"st... | [{"datasets":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":13974,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":13975,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S5... | [{"id":6920,"numValue":9.0,"position":129,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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