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:1878 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,878 | train | mutant | 89 | 41 | 99 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K43A | K43A | 1 | 1 | 0 | 0 | 43 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 43 | A | H | true | false | 50.074322 | 37.580556 | 7,416 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | 53 | NaCl | 0.1 M | 2LZM_A:K43A | null | null | null | 1.1 | null | 4.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"B... | [{"datasets":[],"id":25797,"numValue":4.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25798,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25799,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6834,"numValue":5.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1879 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,879 | train | mutant | 89 | 41 | 99 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K43A | K43A | 1 | 1 | 0 | 0 | 43 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 43 | A | H | true | false | 50.074322 | 37.580556 | 7,543 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:K43A | null | null | null | 0.96 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26117,"numValue":0.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26118,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6834,"numValue":5.0,"position":43,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1880 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,880 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 149 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:S44A | 52.75 | 1.2 | null | null | null | null | 122 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|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":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":584,"numValue":52.75,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":585,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":586,"numValue":122.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id"... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1881 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,881 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 156 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 2LZM_A:S44A | 63.18 | 0.98 | null | null | null | null | 119 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"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":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":612,"numValue":63.18,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":613,"numValue":0.98,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":614,"numValue":119.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1882 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,882 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 930 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44A | 52.89 | 1.21 | null | null | null | null | 117 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3481,"numValue":52.89,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3482,"numValue":1.21,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3483,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1883 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,883 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 3,545 | ProTherm | 2.5 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:S44A | 49.4 | -1.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 325 | ARTICLE | Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices. | 1,994 | 10.1021/bi00206a003 | 7918421 | Biochemistry;33;12022-31 | 5 | Cornish V W|Kaplan M I|Veenstra D L|Kollman P A|Schultz P G | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13061,"numValue":49.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13062,"numValue":-1.6,"references":[],"strValue":nul... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1884 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,884 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 4,058 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:S44A | 38.4 | -15.7 | null | null | 72.18 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:S44A","type":"... | [{"datasets":[],"id":14993,"numValue":38.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14994,"numValue":-15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14995,"numValue":72.18,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1885 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,885 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 4,059 | ProTherm | 3.2 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:S44A | 44.1 | null | null | null | 89.15 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:S44A","type":"... | [{"datasets":[],"id":14997,"numValue":44.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14998,"numValue":89.15,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14999,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,886 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 4,060 | ProTherm | 3.3 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:S44A | 45.1 | -14.3 | null | null | 89.87 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:S44A","type":"... | [{"datasets":[],"id":15000,"numValue":45.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15001,"numValue":-14.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15002,"numValue":89.87,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1887 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,887 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 4,061 | ProTherm | 3.6 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:S44A | 49.8 | null | null | null | 95.6 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:S44A","type":"... | [{"datasets":[],"id":15004,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15005,"numValue":95.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15006,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1888 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,888 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 4,062 | ProTherm | 3.7 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:S44A | 50.9 | -13.7 | null | null | 90.46 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:S44A","type":"... | [{"datasets":[],"id":15007,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15008,"numValue":-13.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15009,"numValue":90.46,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1889 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,889 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 4,063 | ProTherm | 4 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:S44A | 54.3 | null | null | null | 105.64 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:S44A","type":"... | [{"datasets":[],"id":15011,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15012,"numValue":105.64,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15013,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,890 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,069 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:S44A | null | null | null | -0.34 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24812,"numValue":-0.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24813,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,891 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,523 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44A | null | null | null | -0.43 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26058,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26059,"numValue":-0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26060,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,892 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,544 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:S44A | null | null | null | -0.44 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":["capriotti_S1615_map.csv"],"id":26119,"numValue":-0.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26120,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,893 | train | mutant | 90 | 41 | 100 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44A | S44A | 1 | 1 | 0 | 0 | 44 | S | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,785 | ProTherm | 2.5 | CD | Thermal | Potassium phosphate | 20 mM | 47.8 | KCl | 25 mM | 2LZM_A:S44A | null | null | null | 0.44 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 325 | ARTICLE | Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices. | 1,994 | 10.1021/bi00206a003 | 7918421 | Biochemistry;33;12022-31 | 5 | Cornish V W|Kaplan M I|Veenstra D L|Kollman P A|Schultz P G | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":47.8,"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":"20 mM","type"... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv"],"id":26696,"numValue":0.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26697,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1894 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,894 | train | mutant | 547 | 41 | 598 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44L | S44L | 1 | 1 | 0 | 0 | 44 | S | L | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 931 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44L | 52.77 | 1.09 | null | null | null | null | 117 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3485,"numValue":52.77,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3486,"numValue":1.09,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3487,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1895 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,895 | train | mutant | 547 | 41 | 598 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44L | S44L | 1 | 1 | 0 | 0 | 44 | S | L | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,524 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44L | null | null | null | -0.39 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26061,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26062,"numValue":-0.39,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26063,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1896 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,896 | train | mutant | 548 | 41 | 599 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44M | S44M | 1 | 1 | 0 | 0 | 44 | S | M | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 932 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44M | 52.6 | 0.92 | null | null | null | null | 115 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3489,"numValue":52.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3490,"numValue":0.92,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3491,"numValue":115.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1897 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,897 | train | mutant | 548 | 41 | 599 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44M | S44M | 1 | 1 | 0 | 0 | 44 | S | M | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,525 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44M | null | null | null | -0.33 | null | 2.4 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26064,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26065,"numValue":-0.33,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26066,"numValue":null,"references":[],"strValue":"yes","type":"... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1898 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,898 | train | mutant | 549 | 41 | 600 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44I | S44I | 1 | 1 | 0 | 0 | 44 | S | I | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 933 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44I | 52.59 | 0.91 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3493,"numValue":52.59,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3494,"numValue":0.91,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3495,"numValue":112.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1899 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,899 | train | mutant | 549 | 41 | 600 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44I | S44I | 1 | 1 | 0 | 0 | 44 | S | I | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,526 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44I | null | null | null | -0.31 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26067,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26068,"numValue":-0.31,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26069,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1900 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,900 | train | mutant | 550 | 41 | 601 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44Q | S44Q | 1 | 1 | 0 | 0 | 44 | S | Q | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 934 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44Q | 52.43 | 0.75 | null | null | null | null | 116 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3497,"numValue":52.43,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3498,"numValue":0.75,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3499,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1901 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,901 | train | mutant | 550 | 41 | 601 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44Q | S44Q | 1 | 1 | 0 | 0 | 44 | S | Q | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,527 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44Q | null | null | null | -0.27 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26070,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26071,"numValue":-0.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26072,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1902 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,902 | train | mutant | 551 | 41 | 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 | S44R | S44R | 1 | 1 | 0 | 0 | 44 | S | R | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 935 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44R | 52.36 | 0.68 | null | null | null | null | 116 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3501,"numValue":52.36,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3502,"numValue":0.68,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3503,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1903 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,903 | train | mutant | 551 | 41 | 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 | S44R | S44R | 1 | 1 | 0 | 0 | 44 | S | R | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,528 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44R | null | null | null | -0.24 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26073,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26074,"numValue":-0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26075,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1904 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,904 | train | mutant | 552 | 41 | 603 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44K | S44K | 1 | 1 | 0 | 0 | 44 | S | K | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 936 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44K | 52.25 | 0.57 | null | null | null | null | 116 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3505,"numValue":52.25,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3506,"numValue":0.57,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3507,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1905 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,905 | train | mutant | 552 | 41 | 603 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44K | S44K | 1 | 1 | 0 | 0 | 44 | S | K | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,529 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44K | null | null | null | -0.2 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26076,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26077,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26078,"numValue":null,"reference... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1907 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,907 | train | mutant | 553 | 41 | 604 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44Y | S44Y | 1 | 1 | 0 | 0 | 44 | S | Y | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,530 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44Y | null | null | null | -0.19 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26079,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26080,"numValue":-0.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26081,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1908 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,908 | train | mutant | 554 | 41 | 605 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44V | S44V | 1 | 1 | 0 | 0 | 44 | S | V | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 938 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44V | 51.97 | 0.29 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3513,"numValue":51.97,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3514,"numValue":0.29,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3515,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1911 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,911 | train | mutant | 555 | 41 | 606 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44F | S44F | 1 | 1 | 0 | 0 | 44 | S | F | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,532 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44F | null | null | null | -0.06 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26085,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26086,"numValue":-0.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26087,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1912 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,912 | train | mutant | 556 | 41 | 607 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44W | S44W | 1 | 1 | 0 | 0 | 44 | S | W | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 940 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44W | 51.83 | 0.15 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3521,"numValue":51.83,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3522,"numValue":0.15,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3523,"numValue":112.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1913 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,913 | train | mutant | 556 | 41 | 607 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44W | S44W | 1 | 1 | 0 | 0 | 44 | S | W | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,533 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44W | null | null | null | -0.05 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26088,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26089,"numValue":-0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26090,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1914 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,914 | train | mutant | 557 | 41 | 608 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44H | S44H | 1 | 1 | 0 | 0 | 44 | S | H | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 941 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44H | 51.8 | 0.12 | null | null | null | null | 117 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3525,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3526,"numValue":0.12,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3527,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1915 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,915 | train | mutant | 557 | 41 | 608 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44H | S44H | 1 | 1 | 0 | 0 | 44 | S | H | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,534 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44H | null | null | null | -0.04 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26091,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26092,"numValue":-0.04,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26093,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1916 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,916 | train | mutant | 558 | 41 | 609 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44T | S44T | 1 | 1 | 0 | 0 | 44 | S | T | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 942 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44T | 51.71 | 0.03 | null | null | null | null | 113 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3529,"numValue":51.71,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3530,"numValue":0.03,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3531,"numValue":113.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1917 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,917 | train | mutant | 558 | 41 | 609 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44T | S44T | 1 | 1 | 0 | 0 | 44 | S | T | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,535 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44T | null | null | null | -0.01 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26094,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26095,"numValue":-0.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26096,"numValue":null,"referenc... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1918 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,918 | train | mutant | 559 | 41 | 610 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44E | S44E | 1 | 1 | 0 | 0 | 44 | S | E | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 943 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44E | 51.68 | 0 | null | null | null | null | 111 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":3533,"numValue":51.68,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv","Saraboji_S17... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1919 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,919 | train | mutant | 559 | 41 | 610 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44E | S44E | 1 | 1 | 0 | 0 | 44 | S | E | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,536 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44E | null | null | null | 0 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26097,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26098,"numValue":0.0,"refere... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1920 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,920 | train | mutant | 560 | 41 | 611 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44D | S44D | 1 | 1 | 0 | 0 | 44 | S | D | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 944 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44D | 51.36 | -0.32 | null | null | null | null | 110 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3537,"numValue":51.36,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3538,"numValue":-0.32,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3539,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1922 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,922 | train | mutant | 561 | 41 | 612 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44C | S44C | 1 | 1 | 0 | 0 | 44 | S | C | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 945 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44C | 51.33 | -0.35 | null | null | null | null | 117 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3541,"numValue":51.33,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3542,"numValue":-0.35,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3543,"numValue":117.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1923 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,923 | train | mutant | 561 | 41 | 612 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44C | S44C | 1 | 1 | 0 | 0 | 44 | S | C | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,538 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44C | null | null | null | 0.11 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26103,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26104,"numValue":0.11,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26105,"numValue":null,"reference... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1924 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,924 | train | mutant | 562 | 41 | 613 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44N | S44N | 1 | 1 | 0 | 0 | 44 | S | N | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 946 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44N | 51.28 | -0.4 | null | null | null | null | 110 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3545,"numValue":51.28,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3546,"numValue":-0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3547,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1925 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,925 | train | mutant | 562 | 41 | 613 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44N | S44N | 1 | 1 | 0 | 0 | 44 | S | N | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,539 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44N | null | null | null | 0.14 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26106,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26107,"numValue":0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26108,"numValue":null,"reference... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1926 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,926 | train | mutant | 563 | 41 | 614 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44G | S44G | 1 | 1 | 0 | 0 | 44 | S | G | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 947 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44G | 50.13 | -1.55 | null | null | null | null | 110 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3549,"numValue":50.13,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3550,"numValue":-1.55,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3551,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1927 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,927 | train | mutant | 563 | 41 | 614 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44G | S44G | 1 | 1 | 0 | 0 | 44 | S | G | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,540 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44G | null | null | null | 0.53 | 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|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26109,"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":26110,"numValue":0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26111,"num... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1928 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,928 | train | mutant | 564 | 41 | 615 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44P | S44P | 1 | 1 | 0 | 0 | 44 | S | P | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 948 | ProTherm | 3.01 | CD | Thermal | KH2PO4,H3PO4, | 17 mM,3 mM, | null | KCl | 25 mM | 2LZM_A:S44P | 41.36 | -10.32 | null | null | null | null | 74 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4,H3PO4,","type":"BUFFER"},{"numValue":null,"strValue":"17 mM,3 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":3553,"numValue":41.36,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3554,"numValue":-10.32,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3555,"numValue":74.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1929 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,929 | train | mutant | 564 | 41 | 615 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | S44P | S44P | 1 | 1 | 0 | 0 | 44 | S | P | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 44 | A | H | true | false | 68.371141 | 28.9025 | 7,541 | ProTherm | 3.01 | CD | Thermal | KH2PO4, H3PO4 | 17 mM, 3 mM | 51.68 | KCl | 25 mM | 2LZM_A:S44P | null | null | null | 3.03 | null | 2.4 | 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 | 99 | ARTICLE | Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. | 1,994 | 10.1006/jmbi.1994.1016 | 8289284 | J Mol Biol;235;600-24 | 6 | Blaber M|Baase W A|Zhang X J|Matthews B W|Lindstrom J D|Pepiot S D | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.68,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4, H3PO4","type":"BUFFER"},{"numValue":null,"strValue":"17 mM, 3 mM","typ... | [{"datasets":[],"id":26112,"numValue":2.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26113,"numValue":3.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26114,"numValue":null,"reference... | [{"id":6835,"numValue":1.0,"position":44,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1930 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,930 | train | mutant | 91 | 41 | 101 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A | E45A | 1 | 1 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45 | A | H | false | true | 57.738572 | 22.751667 | 150 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:E45A | 53.12 | 1.47 | null | null | null | null | 125 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|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":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":588,"numValue":53.12,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":589,"numValue":1.47,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":590,"numValue":125.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1931 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,931 | train | mutant | 91 | 41 | 101 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A | E45A | 1 | 1 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45 | A | H | false | true | 57.738572 | 22.751667 | 157 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 2LZM_A:E45A | 62.24 | 0.04 | null | null | null | null | 124 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"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":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":616,"numValue":62.24,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":617,"numValue":0.04,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":618,"numValue":124.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1932 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,932 | train | mutant | 91 | 41 | 101 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A | E45A | 1 | 1 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45 | A | H | false | true | 57.738572 | 22.751667 | 7,070 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:E45A | null | null | null | -0.01 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24814,"numValue":-0.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24815,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1933 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,933 | train | mutant | 91 | 41 | 101 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A | E45A | 1 | 1 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45 | A | H | false | true | 57.738572 | 22.751667 | 7,545 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:E45A | null | null | null | -0.55 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":["capriotti_S1615_map.csv"],"id":26121,"numValue":-0.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26122,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1934 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,934 | train | mutant | 6,708 | 41 | 7,350 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A|K48A | E45A|K48A | 2 | 2 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45|48 | A | H | false | true | 101.186463 | 20.673056 | 14,457 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:E45A 2LZM_A:K48A | 52.69 | 1.04 | null | null | null | null | 121 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|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":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":53439,"numValue":52.69,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53440,"numValue":1.04,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53441,"numValue":121.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53442,"numValue":null,"references... | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1935 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,935 | train | mutant | 6,708 | 41 | 7,350 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A|K48A | E45A|K48A | 2 | 2 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45|48 | A | H | false | true | 101.186463 | 20.673056 | 14,458 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 2LZM_A:E45A 2LZM_A:K48A | 62.23 | 0.03 | null | null | null | null | 127 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"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":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":53443,"numValue":62.23,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53444,"numValue":0.03,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53445,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53446,"numValue":null,"references... | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1936 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,936 | train | mutant | 6,708 | 41 | 7,350 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A|K48A | E45A|K48A | 2 | 2 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45|48 | A | H | false | true | 101.186463 | 20.673056 | 14,949 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:E45A 2LZM_A:K48A | null | null | null | -0.01 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":[],"id":55053,"numValue":-0.01,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55054,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1937 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,937 | train | mutant | 6,708 | 41 | 7,350 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | E45A|K48A | E45A|K48A | 2 | 2 | 0 | 0 | 45 | E | A | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 45|48 | A | H | false | true | 101.186463 | 20.673056 | 15,019 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:E45A 2LZM_A:K48A | null | null | null | -0.38 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":[],"id":55221,"numValue":-0.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55222,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6836,"numValue":4.0,"position":45,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1938 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,938 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 38 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 2LZM_A:L46A | 43.2 | -8.6 | null | null | null | 2.5 | 89.8 | 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":121,"numValue":43.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":122,"numValue":-8.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":123,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12... | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1939 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,939 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 151 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:L46A | 43.26 | -8.39 | null | null | null | null | 89 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|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":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":592,"numValue":43.26,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":593,"numValue":-8.39,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":594,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1940 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,940 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 158 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 2LZM_A:L46A | 55.8 | -6.4 | null | null | null | null | 88 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"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":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":620,"numValue":55.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":621,"numValue":-6.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":622,"numValue":88.0,"references":[],"strValue":null,"type":"DHVH"},... | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1941 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,941 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 2,925 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | null | NaCl | 0.1 M | 2LZM_A:L46A | 58.9 | -6.3 | null | null | null | null | 114 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":10607,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10608,"numValue":-6.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10609,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1942 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,942 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 7,071 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:L46A | null | null | null | 1.86 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24816,"numValue":1.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24817,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1943 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,943 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 7,417 | ProTherm | 5.45 | CD | Thermal | Sodium acetate | 0.01 M | 53 | NaCl | 0.1 M | 2LZM_A:L46A | null | null | null | 2.1 | null | 4.5 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 258 | ARTICLE | Accommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis. | 1,994 | 10.1006/jmbi.1994.1195 | 8114100 | J Mol Biol;236;869-86 | 6 | Blaber M|Baase W A|Zhang X J|Heinz D W|Matthews B W|Dahlquist F W | [{"numValue":5.45,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"B... | [{"datasets":[],"id":25800,"numValue":4.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25801,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25802,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1944 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,944 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 7,499 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | 51.8 | KCl | 0.025 M | 2LZM_A:L46A | 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":25994,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":25995,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25996,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1945 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,945 | train | mutant | 38 | 41 | 42 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | L46A | L46A | 1 | 1 | 0 | 0 | 46 | L | A | 9 | CONSERVATION | 1L63|2LZM | 49|80 | null | 46 | A | H | true | true | 0 | 19.509375 | 7,546 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:L46A | null | null | null | 2.62 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":["capriotti_S1615_map.csv"],"id":26123,"numValue":2.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26124,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6837,"numValue":9.0,"position":46,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1946 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,946 | train | mutant | 92 | 41 | 102 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D47A | D47A | 1 | 1 | 0 | 0 | 47 | D | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 47 | A | H | true | false | 34.638129 | 24.6475 | 152 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:D47A | 50.84 | -0.81 | null | null | null | null | 114 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|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":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":596,"numValue":50.84,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":597,"numValue":-0.81,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":598,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6838,"numValue":6.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1948 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,948 | train | mutant | 92 | 41 | 102 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D47A | D47A | 1 | 1 | 0 | 0 | 47 | D | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 47 | A | H | true | false | 34.638129 | 24.6475 | 7,072 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:D47A | null | null | null | 0.95 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24818,"numValue":0.95,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24819,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6838,"numValue":6.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1949 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,949 | train | mutant | 92 | 41 | 102 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | D47A | D47A | 1 | 1 | 0 | 0 | 47 | D | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 47 | A | H | true | false | 34.638129 | 24.6475 | 7,547 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:D47A | null | null | null | 0.28 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26125,"numValue":0.28,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26126,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6838,"numValue":6.0,"position":47,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1950 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,950 | train | mutant | 93 | 41 | 103 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K48A | K48A | 1 | 1 | 0 | 0 | 48 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 48 | A | H | false | true | 144.634354 | 18.594444 | 153 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:K48A | 50.72 | -0.93 | null | null | null | null | 109 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|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":"H3PO4,KH2PO4,","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM,","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":600,"numValue":50.72,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":601,"numValue":-0.93,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":602,"numValue":109.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1951 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,951 | train | mutant | 93 | 41 | 103 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K48A | K48A | 1 | 1 | 0 | 0 | 48 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 48 | A | H | false | true | 144.634354 | 18.594444 | 160 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | null | KCl | 0.15 M | 2LZM_A:K48A | 60.52 | -1.68 | null | null | null | null | 110 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"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":"0.01 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":628,"numValue":60.52,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":629,"numValue":-1.68,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":630,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1952 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,952 | train | mutant | 93 | 41 | 103 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K48A | K48A | 1 | 1 | 0 | 0 | 48 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 48 | A | H | false | true | 144.634354 | 18.594444 | 4,071 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:K48A | 41.6 | -12.5 | null | null | 93.21 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:K48A","type":"... | [{"datasets":[],"id":15039,"numValue":41.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15040,"numValue":-12.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15041,"numValue":93.21,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1953 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,953 | train | mutant | 93 | 41 | 103 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K48A | K48A | 1 | 1 | 0 | 0 | 48 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 48 | A | H | false | true | 144.634354 | 18.594444 | 4,072 | ProTherm | 3.5 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:K48A | 49.9 | -12.2 | null | null | 104.21 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":3.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:K48A","type":"... | [{"datasets":[],"id":15043,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15044,"numValue":-12.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15045,"numValue":104.21,"references":[],"strValue":null,"type":"DH"},{"datasets":[... | [{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1954 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,954 | train | mutant | 93 | 41 | 103 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K48A | K48A | 1 | 1 | 0 | 0 | 48 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 48 | A | H | false | true | 144.634354 | 18.594444 | 4,073 | ProTherm | 4 | DSC | Thermal | glycine-HCl | 20 mM | null | 2LZM_A:K48A | 54.6 | null | null | null | 102.77 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 376 | ARTICLE | Thermodynamic effects of mutations on the denaturation of T4 lysozyme. | 1,996 | 10.1016/S0006-3495(96)79397-9 | 8889173 | Biophys J;71;1994-2001 | 3 | Privalov P L|Carra J H|Murphy E C | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2LZM_A:K48A","type":"... | [{"datasets":[],"id":15047,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15048,"numValue":102.77,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15049,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1955 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,955 | train | mutant | 93 | 41 | 103 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K48A | K48A | 1 | 1 | 0 | 0 | 48 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 48 | A | H | false | true | 144.634354 | 18.594444 | 7,073 | ProTherm | 6.7 | CD | Thermal | KH2PO4 | 0.01 M | 62.2 | KCl | 0.15 M | 2LZM_A:K48A | null | null | null | 0.56 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":6.7,"strValue":null,"type":"PH"},{"numValue":62.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"0.01 M","type":"BUFFER_CON... | [{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24820,"numValue":0.56,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24821,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1956 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,956 | train | mutant | 93 | 41 | 103 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | K48A | K48A | 1 | 1 | 0 | 0 | 48 | K | A | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 48 | A | H | false | true | 144.634354 | 18.594444 | 7,548 | ProTherm | 3 | CD | Thermal | H3PO4,KH2PO4 | 3 mM,17 mM | 51.65 | KCl | 25 mM | 2LZM_A:K48A | null | null | null | 0.32 | 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 | 13 | ARTICLE | Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. | 1,992 | 10.1073/pnas.89.9.3751 | 1570293 | Proc Natl Acad Sci U S A;89;3751-5 | 3 | Baase W A|Heinz D W|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"H3PO4,KH2PO4","type":"BUFFER"},{"numValue":null,"strValue":"3 mM,17 mM","type":... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26127,"numValue":0.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26128,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6839,"numValue":5.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1957 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,957 | train | mutant | 231 | 41 | 261 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A49S | A49S | 1 | 1 | 0 | 0 | 49 | A | S | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 49 | A | H | false | true | 46.040657 | 16.476 | 417 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A49S | 50.02 | -1.53 | null | null | null | null | 110 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":1719,"numValue":50.02,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1720,"numValue":-1.53,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1721,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6840,"numValue":4.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1958 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,958 | train | mutant | 231 | 41 | 261 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | A49S | A49S | 1 | 1 | 0 | 0 | 49 | A | S | 4 | CONSERVATION | 1L63|2LZM | 49|80 | null | 49 | A | H | false | true | 46.040657 | 16.476 | 7,586 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A49S | null | null | null | 0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 44 | ARTICLE | Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme. | 1,993 | 10.1021/bi00093a013 | 8218201 | Biochemistry;32;11363-73 | 6 | Xu J|Blaber M|Gassner N|Heinz D W|Matthews B W|Lindstrom J D | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.55,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26229,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26230,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6840,"numValue":4.0,"position":49,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1959 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,959 | train | mutant | 1,126 | 41 | 1,270 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I50A | I50A | 1 | 1 | 0 | 0 | 50 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 50 | A | H | false | false | 37.790825 | 22.13625 | 2,020 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I50A | 61.1 | -4.2 | null | null | null | null | 116 | 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|M47andM8_S1810.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 215 | ARTICLE | Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. | 1,999 | 10.1021/bi9915519 | 10545167 | Biochemistry;38;14451-60 | 6 | Lu J|Baase W A|Matthews B W|Gassner N C|Lindstrom J D|Dahlquist F W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD, Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"acetic acid, sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"1.4 mM, 8.6 mM","type":"BUFFER_CONC"},{"numValue":... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":7542,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_... | [{"id":6841,"numValue":6.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1960 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,960 | train | mutant | 1,126 | 41 | 1,270 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I50A | I50A | 1 | 1 | 0 | 0 | 50 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 50 | A | H | false | false | 37.790825 | 22.13625 | 3,127 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:I50A | 45.9 | -5.8 | null | null | null | 1.8 | 94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"I... | [{"datasets":[],"id":11387,"numValue":45.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11388,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11389,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"... | [{"id":6841,"numValue":6.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1961 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,961 | train | mutant | 1,126 | 41 | 1,270 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I50A | I50A | 1 | 1 | 0 | 0 | 50 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 50 | A | H | false | false | 37.790825 | 22.13625 | 6,787 | 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:I50A | null | null | null | 1.6 | 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":24063,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24064,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24065,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6841,"numValue":6.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1962 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,962 | train | mutant | 1,126 | 41 | 1,270 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I50A | I50A | 1 | 1 | 0 | 0 | 50 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 50 | A | H | false | false | 37.790825 | 22.13625 | 7,561 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.65 | KCl | 25 mM | 2LZM_A:I50A | null | null | null | 2 | null | 1.8 | null | null | null | null | null | null | null | null | null | null | Unknown | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|guerios_625_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 290 | ARTICLE | The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect. | 1,998 | 10.1002/pro.5560070117 | 9514271 | Protein Sci;7;158-77 | 4 | Baldwin E|Xu J|Baase W A|Matthews B W | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":51.65,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type... | [{"datasets":[],"id":26156,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26157,"numValue":2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26158,"numV... | [{"id":6841,"numValue":6.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1963 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,963 | train | mutant | 1,126 | 41 | 1,270 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I50A | I50A | 1 | 1 | 0 | 0 | 50 | I | A | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 50 | A | H | false | false | 37.790825 | 22.13625 | 10,022 | ProTherm | 6 | CD | Urea | Potassium phosphate | 20 mM | 25 | NaCl | 100 mM | 2LZM_A:I50A | null | null | 12 | 2.9 | 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":34425,"numValue":12.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":34426,"numValue":2.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":34427,"numValue":2.6,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":34428,"numValue":null,... | [{"id":6841,"numValue":6.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:1964 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,964 | train | mutant | 1,140 | 41 | 1,284 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | I50M | I50M | 1 | 1 | 0 | 0 | 50 | I | M | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 50 | A | H | false | false | 37.790825 | 22.13625 | 2,040 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:I50M | 64.7 | -0.6 | null | null | null | null | 120 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.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":7642,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":7643,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv"... | [{"id":6841,"numValue":6.0,"position":50,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:1966 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,966 | train | mutant | 5,831 | 41 | 6,396 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | G51D | G51D | 1 | 1 | 0 | 0 | 51 | G | D | 5 | CONSERVATION | 1L63|2LZM | 49|80 | null | 51 | A | T | false | false | 66.569346 | 26.9575 | 12,606 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:G51D | null | null | null | 2.63 | null | null | null | 5 | 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":45721,"numValue":2.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45722,"numValue":5.0,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45723,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6842,"numValue":5.0,"position":51,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1967 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,967 | train | mutant | 7,405 | 41 | 8,088 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | R52A|N53A|C54A|N55A|G56A|V57A|I58A | R52A|N53A|C54A|N55A|G56A|V57A|I58A | 7 | 7 | 0 | 0 | 52 | R | A | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 52|53|54|55|56|57|58 | A | S|L|T|B | true | false | 60.309741 | 32.816185 | 15,799 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:R52A 2LZM_A:N53A 2LZM_A:C54A 2LZM_A:N55A 2LZM_A:G56A 2LZM_A:V57A 2LZM_A:I58A | 37 | -16.4 | null | null | null | 1.8 | 40 | 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":58017,"numValue":37.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58018,"numValue":-16.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58019,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":58020,"numValue":40.0,"references":[... | [{"id":6843,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6844,"numValue":1.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1968 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,968 | train | mutant | 7,403 | 41 | 8,086 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N53A|N55A|V57A | N53A|N55A|V57A | 3 | 3 | 0 | 0 | 53 | N | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 53|55|57 | A | L|T|B | true | false | 103.860744 | 40.989821 | 15,797 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:N53A 2LZM_A:N55A 2LZM_A:V57A | 49.4 | -4 | null | null | null | 1.8 | 104 | 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":58007,"numValue":49.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58008,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58009,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":58010,"numValue":104.0,"references":[... | [{"id":6844,"numValue":1.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6848,"numValue":4.0,"position":57,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1969 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,969 | train | mutant | 7,403 | 41 | 8,086 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N53A|N55A|V57A | N53A|N55A|V57A | 3 | 3 | 0 | 0 | 53 | N | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 53|55|57 | A | L|T|B | true | false | 103.860744 | 40.989821 | 16,783 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:N53A 2LZM_A:N55A 2LZM_A:V57A | null | null | null | 1.5 | 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":61684,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61685,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61686,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":6844,"numValue":1.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6848,"numValue":4.0,"position":57,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1970 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,970 | train | mutant | 7,404 | 41 | 8,087 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N53A|C54A|N55A|G56A|V57A|I58A | N53A|C54A|N55A|G56A|V57A|I58A | 6 | 6 | 0 | 0 | 53 | N | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 53|54|55|56|57|58 | A | L|T|B | true | false | 53.787575 | 32.980928 | 15,798 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:N53A 2LZM_A:C54A 2LZM_A:N55A 2LZM_A:G56A 2LZM_A:V57A 2LZM_A:I58A | 37.6 | -15.8 | null | null | null | 1.8 | 43 | 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":58012,"numValue":37.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58013,"numValue":-15.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58014,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":58015,"numValue":43.0,"references":[... | [{"id":6844,"numValue":1.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1972 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,972 | train | mutant | 7,406 | 41 | 8,089 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N53A|N55A|V57A|E128A|V131A|N132A | N53A|N55A|V57A|E128A|V131A|N132A | 6 | 6 | 0 | 0 | 53 | N | A | 1 | BINDING_SITE|CONSERVATION | 1L63|2LZM | 49|80 | null | 53|55|57|128|131|132 | A | L|T|B|H | true | false | 89.985659 | 33.12683 | 16,784 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | 53.4 | KCl | 25.0 mM | 2LZM_A:N53A 2LZM_A:N55A 2LZM_A:V57A 2LZM_A:E128A 2LZM_A:V131A 2LZM_A:N132A | null | null | null | 0.8 | 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":61687,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":61688,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":61689,"numValue":null,"references":[],"strValue":"yes(>90%)","type":"REVERSIBILITY"}] | [{"id":23,"numValue":null,"position":132,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":6844,"numValue":1.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1973 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,973 | train | mutant | 7,407 | 41 | 8,090 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | N53A|C54A|N55A|G56A|V57A|I58A|E62A | N53A|C54A|N55A|G56A|V57A|I58A|E62A | 7 | 7 | 0 | 0 | 53 | N | A | 1 | CONSERVATION | 1L63|2LZM | 49|80 | null | 53|54|55|56|57|58|62 | A | L|T|B|H | true | false | 50.650189 | 31.177144 | 15,801 | ProTherm | 3 | CD | Thermal | KPO4 | 20.0 mM | null | KCl | 25.0 mM | 2LZM_A:N53A 2LZM_A:C54A 2LZM_A:N55A 2LZM_A:G56A 2LZM_A:V57A 2LZM_A:I58A 2LZM_A:E62A | 37 | -16.4 | null | null | null | 1.8 | 42 | 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":58027,"numValue":37.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58028,"numValue":-16.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58029,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":58030,"numValue":42.0,"references":[... | [{"id":6844,"numValue":1.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6846,"numValue":4.0,"position":55,"positionArray":null,"positionRange":... | |||||||||||
fireprotdb:1974 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,974 | train | mutant | 501 | 41 | 551 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54V | C54V | 1 | 1 | 0 | 0 | 54 | C | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54 | A | L | true | false | 6.193813 | 29.342976 | 814 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:C54V | 63 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3089,"numValue":63.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3090,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3091,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1975 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,975 | train | mutant | 501 | 41 | 551 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54V | C54V | 1 | 1 | 0 | 0 | 54 | C | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54 | A | L | true | false | 6.193813 | 29.342976 | 6,642 | ProTherm | 6.5 | CD | Thermal | Unknown | 70 | KCl | 0.2 M | 2LZM_A:C54V | null | null | null | 0.7 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":70.0,"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":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23691,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23692,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1976 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,976 | train | mutant | 502 | 41 | 552 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54T | C54T | 1 | 1 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54 | A | L | true | false | 6.193813 | 29.342976 | 815 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:C54T | 66 | 1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":3092,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3093,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3094,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1977 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,977 | train | mutant | 502 | 41 | 552 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54T | C54T | 1 | 1 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54 | A | L | true | false | 6.193813 | 29.342976 | 3,030 | ProTherm | 6 | CD | Thermal | Unknown | null | 2LZM_A:C54T | 69 | 3.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"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:C54T","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11011,"numValue":69.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":11012,"numValue":3.5,"references":[],"strValue":null... | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1978 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,978 | train | mutant | 502 | 41 | 552 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54T | C54T | 1 | 1 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54 | A | L | true | false | 6.193813 | 29.342976 | 6,643 | ProTherm | 6.5 | CD | Thermal | Unknown | 70 | KCl | 0.2 M | 2LZM_A:C54T | null | null | null | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":70.0,"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":"KCl","type":"ION"},{"numV... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":23693,"numValue":-0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23694,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1979 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,979 | train | mutant | 502 | 41 | 552 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54T | C54T | 1 | 1 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54 | A | L | true | false | 6.193813 | 29.342976 | 6,764 | ProTherm | 6 | CD | Thermal | Unknown | 65.5 | 2LZM_A:C54T | null | null | null | -1.36 | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|_PDB_CHAIN_MUTATION | 272 | ARTICLE | Protein stability curves. | 1,987 | 10.1002/bip.360261104 | 3689874 | Biopolymers;26;1859-77 | 2 | Schellman J A|Becktel W J | [{"numValue":6.0,"strValue":null,"type":"PH"},{"numValue":65.5,"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":"2LZM_A:C54T","type":"_PDB... | [{"datasets":["capriotti_S1615_map.csv"],"id":23998,"numValue":-1.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":23999,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:1980 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,980 | train | mutant | 5,832 | 41 | 6,397 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54Y | C54Y | 1 | 1 | 0 | 0 | 54 | C | Y | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54 | A | L | true | false | 6.193813 | 29.342976 | 12,607 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:C54Y | null | null | null | 5.02 | null | null | null | 3.8 | 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":45724,"numValue":5.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45725,"numValue":3.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45726,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1981 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,981 | train | mutant | 6,764 | 41 | 7,406 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54V|C97S | C54V|C97S | 2 | 2 | 0 | 0 | 54 | C | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54|97 | A | L|H | true | false | 9.462741 | 20.324071 | 14,536 | ProTherm | 6.5 | CD | Thermal | Unknown | null | KCl | 0.2 M | 2LZM_A:C54V 2LZM_A:C97S | 59 | -6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Unknown","type":"BUFFER"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue":null,"strValue":"0.2 M","type":"ION_CONC"},{"numValue... | [{"datasets":[],"id":53737,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53738,"numValue":-6.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53739,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6888,"numValue":5.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1982 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,982 | train | mutant | 6,764 | 41 | 7,406 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54V|C97S | C54V|C97S | 2 | 2 | 0 | 0 | 54 | C | V | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54|97 | A | L|H | true | false | 9.462741 | 20.324071 | 14,882 | ProTherm | 6.5 | CD | Thermal | Unknown | 70 | KCl | 0.2 M | 2LZM_A:C54V 2LZM_A:C97S | null | null | null | 2.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 88 | ARTICLE | Disulfide bonds and thermal stability in T4 lysozyme. | 1,988 | 10.1073/pnas.85.2.401 | 3277175 | Proc Natl Acad Sci U S A;85;401-5 | 4 | Baase W A|Becktel W J|Wetzel R|Perry L J | [{"numValue":6.5,"strValue":null,"type":"PH"},{"numValue":70.0,"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":"KCl","type":"ION"},{"numV... | [{"datasets":[],"id":54895,"numValue":2.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54896,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6888,"numValue":5.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:1984 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,984 | train | mutant | 6,770 | 41 | 7,412 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54T|C97A | C54T|C97A | 2 | 2 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54|97 | A | L|H | true | false | 9.462741 | 20.324071 | 14,552 | ProTherm | 5.5 | CD | Thermal | HCl | 10 mM | null | KCl | 0.15 M | 2LZM_A:C54T 2LZM_A:C97A | 65.4 | null | null | null | null | null | 132 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 302 | ARTICLE | Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. | 1,991 | 10.1021/bi00243a015 | 1854726 | Biochemistry;30;7142-53 | 4 | Nicholson H|Matthews B W|Sauer U|Sun D P | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValue"... | [{"datasets":[],"id":53797,"numValue":65.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53798,"numValue":132.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53799,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6888,"numValue":5.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:1987 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 1,987 | train | mutant | 6,770 | 41 | 7,412 | 164 | 164 | 4 | Endolysin | Enterobacteria phage T4 | 1 | 4 | Endolysin | Enterobacteria phage T4 | 1 | P00720 | IPR034690|IPR002196|IPR023346|IPR023347|IPR052619|IPR001165 | 3.2.1.17 | C54T|C97A | C54T|C97A | 2 | 2 | 0 | 0 | 54 | C | T | 7 | CONSERVATION | 1L63|2LZM | 49|80 | null | 54|97 | A | L|H | true | false | 9.462741 | 20.324071 | 14,555 | ProTherm | 2.5 | DSC | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:C54T 2LZM_A:C97A | 46.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 96 | ARTICLE | Differential scanning calorimetric study of the thermal unfolding of mutant forms of phage T4 lysozyme. | 1,992 | 10.1021/bi00121a009 | 1737020 | Biochemistry;31;1643-7 | 4 | Kitamura S|Tanaka A|Sturtevant J M|Hu C Q | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"... | [{"datasets":[],"id":53805,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53806,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6845,"numValue":7.0,"position":54,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6888,"numValue":5.0,"position":97,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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