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:3543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,543 | train | mutant | 2,056 | 48 | 2,295 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77T | I77T | 1 | 1 | 0 | 0 | 77 | I | T | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,007 | ProTherm | 2.62 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59T | 56.9 | null | null | null | 103.97 | 1.67 | 104.92 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.62,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59T","type":"_P... | [{"datasets":[],"id":14788,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14789,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14790,"numValue":1.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14791,"numValue":104.92,"references... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3545 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,545 | train | mutant | 2,056 | 48 | 2,295 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77T | I77T | 1 | 1 | 0 | 0 | 77 | I | T | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,009 | ProTherm | 2.8 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59T | 59.5 | null | null | null | 106.12 | 1.17 | 109.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59T","type":"_PD... | [{"datasets":[],"id":14798,"numValue":59.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14799,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14800,"numValue":1.17,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14801,"numValue":109.94,"references... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3546 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,546 | train | mutant | 2,056 | 48 | 2,295 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77T | I77T | 1 | 1 | 0 | 0 | 77 | I | T | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,010 | ProTherm | 2.99 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59T | 62.9 | null | null | null | 107.07 | 1.39 | 107.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.99,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59T","type":"_P... | [{"datasets":[],"id":14803,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14804,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14805,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14806,"numValue":107.07,"references... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,547 | train | mutant | 2,056 | 48 | 2,295 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77T | I77T | 1 | 1 | 0 | 0 | 77 | I | T | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,011 | ProTherm | 3.15 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59T | 64.9 | null | null | null | 110.9 | 1.2 | 119.02 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.15,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59T","type":"_P... | [{"datasets":[],"id":14808,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14809,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14810,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14811,"numValue":119.02,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,549 | train | mutant | 2,056 | 48 | 2,295 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77T | I77T | 1 | 1 | 0 | 0 | 77 | I | T | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,044 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59T | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59T","type":"_PD... | [{"datasets":[],"id":14947,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14948,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3550 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,550 | train | mutant | 2,056 | 48 | 2,295 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77T | I77T | 1 | 1 | 0 | 0 | 77 | I | T | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,931 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59T | null | null | null | 2.22 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":24464,"numValue":2.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24465,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,551 | train | mutant | 2,057 | 48 | 2,296 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77Y | I77Y | 1 | 1 | 0 | 0 | 77 | I | Y | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,012 | ProTherm | 2.71 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59Y | 51.4 | null | null | null | 79.35 | 1.55 | 84.37 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.71,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59Y","type":"_P... | [{"datasets":[],"id":14813,"numValue":51.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14814,"numValue":79.35,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14815,"numValue":1.55,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14816,"numValue":84.37,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,553 | train | mutant | 2,057 | 48 | 2,296 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77Y | I77Y | 1 | 1 | 0 | 0 | 77 | I | Y | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,014 | ProTherm | 3.18 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59Y | 59.5 | null | null | null | 90.58 | 1.27 | 97.04 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.18,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59Y","type":"_P... | [{"datasets":[],"id":14823,"numValue":59.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14824,"numValue":90.58,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14825,"numValue":1.27,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14826,"numValue":97.04,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,554 | train | mutant | 2,057 | 48 | 2,296 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77Y | I77Y | 1 | 1 | 0 | 0 | 77 | I | Y | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,030 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59Y | 51.1 | -13.8 | null | null | 97.75 | 1.34 | 105.11 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59Y","type":"_PD... | [{"datasets":[],"id":14915,"numValue":51.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14916,"numValue":-13.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14917,"numValue":97.75,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,555 | train | mutant | 2,057 | 48 | 2,296 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77Y | I77Y | 1 | 1 | 0 | 0 | 77 | I | Y | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,045 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59Y | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59Y","type":"_PD... | [{"datasets":[],"id":14949,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14950,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,556 | train | mutant | 2,057 | 48 | 2,296 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77Y | I77Y | 1 | 1 | 0 | 0 | 77 | I | Y | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,932 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59Y | null | null | null | 3.78 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24466,"numValue":3.78,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24467,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,557 | train | mutant | 1,891 | 48 | 2,120 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S79A | S79A | 1 | 1 | 0 | 0 | 79 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 79 | A | T | false | false | 0 | 13.82 | 3,648 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S61A | 68.3 | null | null | null | 113.05 | 1.31 | 118.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S61A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13419,"numValue":68.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13420,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7034,"numValue":8.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,558 | train | mutant | 1,891 | 48 | 2,120 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S79A | S79A | 1 | 1 | 0 | 0 | 79 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 79 | A | T | false | false | 0 | 13.82 | 3,649 | ProTherm | 2.84 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S61A | 63.6 | null | null | null | 107.07 | 1.15 | 110.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S61A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13424,"numValue":63.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13425,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7034,"numValue":8.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,560 | train | mutant | 1,891 | 48 | 2,120 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S79A | S79A | 1 | 1 | 0 | 0 | 79 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 79 | A | T | false | false | 0 | 13.82 | 3,651 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S61A | 57 | null | null | null | 98.95 | 1.1 | 103.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.51,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S61A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13434,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13435,"numValue":98.95,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S19... | [{"id":7034,"numValue":8.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,561 | train | mutant | 1,891 | 48 | 2,120 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S79A | S79A | 1 | 1 | 0 | 0 | 79 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 79 | A | T | false | false | 0 | 13.82 | 3,663 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S61A | 60.6 | -4.3 | null | null | 108.51 | 1.27 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S61A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13494,"numValue":60.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13495,"numValue":-4.3,"references":[],"strValue":nul... | [{"id":7034,"numValue":8.0,"position":79,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,562 | train | mutant | 1,736 | 48 | 1,946 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y81F | Y81F | 1 | 1 | 0 | 0 | 81 | Y | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 81 | A | T | true | true | 114.885741 | 39.9125 | 3,266 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y63F | 64.2 | -0.7 | null | null | 110.8 | 1.53 | 116.6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y63F","type":"_PD... | [{"datasets":[],"id":11984,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11985,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11986,"numValue":110.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7036,"numValue":4.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,563 | train | mutant | 1,736 | 48 | 1,946 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y81F | Y81F | 1 | 1 | 0 | 0 | 81 | Y | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 81 | A | T | true | true | 114.885741 | 39.9125 | 3,286 | ProTherm | 3.17 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y63F | 72.7 | null | null | null | 123.2 | 0.67 | 129.19 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":3.17,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y63F","type":"_P... | [{"datasets":[],"id":12086,"numValue":72.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12087,"numValue":123.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12088,"numValue":0.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12089,"numValue":129.19,"references"... | [{"id":7036,"numValue":4.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,564 | train | mutant | 1,736 | 48 | 1,946 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y81F | Y81F | 1 | 1 | 0 | 0 | 81 | Y | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 81 | A | T | true | true | 114.885741 | 39.9125 | 3,287 | ProTherm | 3 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y63F | 69.5 | null | null | null | 117.2 | 0.6 | 122 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y63F","type":"_PD... | [{"datasets":[],"id":12091,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12092,"numValue":117.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12093,"numValue":0.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12094,"numValue":122.0,"references":[... | [{"id":7036,"numValue":4.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3566 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,566 | train | mutant | 1,736 | 48 | 1,946 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y81F | Y81F | 1 | 1 | 0 | 0 | 81 | Y | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 81 | A | T | true | true | 114.885741 | 39.9125 | 3,289 | ProTherm | 2.58 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y63F | 61.9 | null | null | null | 106.2 | 1.53 | 112.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.58,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y63F","type":"_P... | [{"datasets":[],"id":12101,"numValue":61.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12102,"numValue":106.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12103,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12104,"numValue":112.2,"references":... | [{"id":7036,"numValue":4.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,567 | train | mutant | 1,736 | 48 | 1,946 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y81F | Y81F | 1 | 1 | 0 | 0 | 81 | Y | F | 4 | CONSERVATION | 1LZ1 | 405 | null | 81 | A | T | true | true | 114.885741 | 39.9125 | 6,901 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:Y63F | null | null | null | 0.24 | null | 1.53 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24384,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24385,"numValue":0.24,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24386,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7036,"numValue":4.0,"position":81,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,568 | train | mutant | 7,276 | 48 | 7,946 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | W82C|C83A | W82C|C83A | 2 | 2 | 0 | 0 | 82 | W | C | 8 | CONSERVATION | 1LZ1 | 405 | null | 82|83 | A | T|S | true | true | 16.928696 | 14.160357 | 15,599 | ProTherm | 5.2 | CD | GdnHCl | Sodium acetate | 20 mM | 20 | 1LZ1_A:W64C 1LZ1_A:C65A | null | null | 12.5 | 2.2 | null | null | null | 3.79 | 3.3 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 936 | ARTICLE | Effect of an alternative disulfide bond on the structure, stability, and folding of human lysozyme. | 2,000 | 10.1021/bi9921945 | 10727242 | Biochemistry;39;3472-9 | 7 | Kanaya E|Arai M|Kuwajima K|Hamel P|Inaka K|Miki K|Kikuchi M | [{"numValue":5.2,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":57234,"numValue":12.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":57235,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":57236,"numValue":3.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":57237,"numValue":3.79,"references":[],"s... | [{"id":7037,"numValue":8.0,"position":82,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7038,"numValue":9.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,569 | train | mutant | 47 | 48 | 52 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D85N | D85N | 1 | 1 | 0 | 0 | 85 | D | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 85 | A | L | false | false | 35.266805 | 12.585 | 47 | ProTherm | 2.2 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | 1LZ1_A:D67N | 56.8 | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:D67... | [{"datasets":[],"id":160,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":161,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":162,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7040,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3570 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,570 | train | mutant | 47 | 48 | 52 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D85N | D85N | 1 | 1 | 0 | 0 | 85 | D | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 85 | A | L | false | false | 35.266805 | 12.585 | 53 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | null | 1LZ1_A:D67N | 74 | -6.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:D67N","typ... | [{"datasets":[],"id":178,"numValue":74.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":179,"numValue":-6.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":180,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7040,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,571 | train | mutant | 47 | 48 | 52 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D85N | D85N | 1 | 1 | 0 | 0 | 85 | D | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 85 | A | L | false | false | 35.266805 | 12.585 | 57 | ProTherm | 2.3 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | KCl | 0.2 M | 1LZ1_A:D67N | 55.2 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type... | [{"datasets":[],"id":190,"numValue":55.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":191,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":192,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7040,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,572 | train | mutant | 47 | 48 | 52 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D85N | D85N | 1 | 1 | 0 | 0 | 85 | D | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 85 | A | L | false | false | 35.266805 | 12.585 | 61 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | null | KCl | 0.2 M | 1LZ1_A:D67N | 72.5 | -5.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"... | [{"datasets":[],"id":202,"numValue":72.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":203,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":204,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7040,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,573 | train | mutant | 47 | 48 | 52 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D85N | D85N | 1 | 1 | 0 | 0 | 85 | D | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 85 | A | L | false | false | 35.266805 | 12.585 | 6,840 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | 65 | 1LZ1_A:D67N | null | null | 3.18 | 2.25 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":65.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"B... | [{"datasets":[],"id":24218,"numValue":3.18,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":24219,"numValue":2.25,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24220,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7040,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,574 | train | mutant | 47 | 48 | 52 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D85N | D85N | 1 | 1 | 0 | 0 | 85 | D | N | 4 | CONSERVATION | 1LZ1 | 405 | null | 85 | A | L | false | false | 35.266805 | 12.585 | 6,844 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | 65 | KCl | 0.2 M | 1LZ1_A:D67N | null | null | 2.37 | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":65.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"B... | [{"datasets":[],"id":24230,"numValue":2.37,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":24231,"numValue":1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24232,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7040,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:3575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,575 | train | mutant | 6,475 | 48 | 7,111 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D85H | D85H | 1 | 1 | 0 | 0 | 85 | D | H | 4 | CONSERVATION | 1LZ1 | 405 | null | 85 | A | L | false | false | 35.266805 | 12.585 | 13,913 | ProTherm | 4 | CD | GdnHCl | GdnHCl | 40 mM | 10 | 1LZ1_A:D67H | null | null | 9.44 | 4.54 | null | null | null | 3.1 | 3.2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 879 | ARTICLE | The stability and folding process of amyloidogenic mutant human lysozymes. | 2,001 | 10.1046/j.1432-1327.2001.01863.x | 11121116 | Eur J Biochem;268;155-9 | 3 | Takano K|Yutani K|Funahashi J | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"GdnHCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_CONC"... | [{"datasets":[],"id":51490,"numValue":9.44,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51491,"numValue":4.54,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":51492,"numValue":3.2,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":51493,"numValue":3.1,"references":[],"s... | [{"id":7040,"numValue":4.0,"position":85,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,576 | train | mutant | 292 | 48 | 324 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G86A | G86A | 1 | 1 | 0 | 0 | 86 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 86 | A | S | false | false | 66.520044 | 16.33 | 514 | ProTherm | 2.6 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G68A | 62.8 | null | null | null | 103.01 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G68A","type":"_PD... | [{"datasets":[],"id":2061,"numValue":62.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2062,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2063,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7041,"numValue":4.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,577 | train | mutant | 292 | 48 | 324 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G86A | G86A | 1 | 1 | 0 | 0 | 86 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 86 | A | S | false | false | 66.520044 | 16.33 | 515 | ProTherm | 2.72 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G68A | 64.9 | null | null | null | 108.99 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.72,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G68A","type":"_P... | [{"datasets":[],"id":2064,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2065,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":["M47andM8_S2760.csv"],"id":2066,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7041,"numValue":4.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3578 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,578 | train | mutant | 292 | 48 | 324 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G86A | G86A | 1 | 1 | 0 | 0 | 86 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 86 | A | S | false | false | 66.520044 | 16.33 | 516 | ProTherm | 3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G68A | 69.2 | null | null | null | 114.01 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G68A","type":"_PD... | [{"datasets":[],"id":2067,"numValue":69.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2068,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2069,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7041,"numValue":4.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,579 | train | mutant | 292 | 48 | 324 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G86A | G86A | 1 | 1 | 0 | 0 | 86 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 86 | A | S | false | false | 66.520044 | 16.33 | 534 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G68A | 64.5 | -0.4 | null | null | 107.55 | 1.65 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G68A","type":"_PD... | [{"datasets":[],"id":2128,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2129,"numValue":-0.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2130,"numValue":107.55,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2131,"numValue":1.65,"references":[],"... | [{"id":7041,"numValue":4.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,580 | train | mutant | 292 | 48 | 324 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G86A | G86A | 1 | 1 | 0 | 0 | 86 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 86 | A | S | false | false | 66.520044 | 16.33 | 6,877 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:G68A | null | null | null | 0.12 | null | 1.65 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24312,"numValue":1.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24313,"numValue":0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24314,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":7041,"numValue":4.0,"position":86,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,581 | train | mutant | 1,941 | 48 | 2,170 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88A | T88A | 1 | 1 | 0 | 0 | 88 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,731 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70A | 67.1 | null | null | null | 109.94 | null | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.1,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70A","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13769,"numValue":67.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13770,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13771,"numValue":113.05,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,582 | train | mutant | 1,941 | 48 | 2,170 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88A | T88A | 1 | 1 | 0 | 0 | 88 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,732 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70A | 64.7 | null | null | null | 107.07 | null | 109.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70A","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13773,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13774,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13775,"numValue":109.94,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,583 | train | mutant | 1,941 | 48 | 2,170 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88A | T88A | 1 | 1 | 0 | 0 | 88 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,733 | ProTherm | 2.85 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70A | 62.2 | null | null | null | 103.01 | null | 106.12 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.85,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70A","type"... | [{"datasets":["STRUM_Q3421.csv"],"id":13777,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13778,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13779,"numValue":106.12,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,584 | train | mutant | 1,941 | 48 | 2,170 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88A | T88A | 1 | 1 | 0 | 0 | 88 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,734 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70A | 60 | null | null | null | 101.1 | null | 103.97 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70A","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13781,"numValue":60.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13782,"numValue":101.1,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13783,"numValue":103.97,"references":[],"strValue":null,"type":"DHVH"},{"... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,585 | train | mutant | 1,941 | 48 | 2,170 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88A | T88A | 1 | 1 | 0 | 0 | 88 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,735 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70A | 57.3 | null | null | null | 98.47 | null | 99.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.5,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70A","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13785,"numValue":57.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13786,"numValue":98.47,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13787,"numValue":99.9,"references":[],"strValue":null,"type":"DHVH"},{"da... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3586 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,586 | train | mutant | 1,946 | 48 | 2,175 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88V | T88V | 1 | 1 | 0 | 0 | 88 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,754 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70V | 70.3 | null | null | null | 119.02 | null | 123.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.1,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70V","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13861,"numValue":70.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13862,"numValue":119.02,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,587 | train | mutant | 1,946 | 48 | 2,175 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88V | T88V | 1 | 1 | 0 | 0 | 88 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,755 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70V | 67.6 | null | null | null | 114.96 | null | 120.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70V","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13865,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13866,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,588 | train | mutant | 1,946 | 48 | 2,175 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88V | T88V | 1 | 1 | 0 | 0 | 88 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,756 | ProTherm | 2.85 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70V | 65.3 | null | null | null | 112.09 | null | 117.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.85,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70V","type"... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13869,"numValue":65.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13870,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,589 | train | mutant | 1,946 | 48 | 2,175 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88V | T88V | 1 | 1 | 0 | 0 | 88 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,757 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70V | 62.6 | null | null | null | 107.07 | null | 110.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70V","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13873,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13874,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13875,"numValue":110.9,"references":[],"s... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,590 | train | mutant | 1,946 | 48 | 2,175 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T88V | T88V | 1 | 1 | 0 | 0 | 88 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 88 | A | L | false | false | 11.163046 | 18.277143 | 3,758 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T70V | 59.5 | null | null | null | 102.06 | null | 106.12 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|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|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.5,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T70V","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13877,"numValue":59.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13878,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuS... | [{"id":7043,"numValue":5.0,"position":88,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3591 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,591 | train | mutant | 631 | 48 | 683 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P89G | P89G | 1 | 1 | 0 | 0 | 89 | P | G | 1 | CONSERVATION | 1LZ1 | 405 | null | 89 | A | T | false | false | 69.452454 | 29.662857 | 1,048 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | null | 1LZ1_A:P71G | 64.1 | -4.7 | null | null | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:P71G","type":"... | [{"datasets":[],"id":3916,"numValue":64.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3917,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3918,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":7044,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,592 | train | mutant | 631 | 48 | 683 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P89G | P89G | 1 | 1 | 0 | 0 | 89 | P | G | 1 | CONSERVATION | 1LZ1 | 405 | null | 89 | A | T | false | false | 69.452454 | 29.662857 | 6,701 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | 68.8 | 1LZ1_A:P71G | null | null | null | 1.6 | 120.7 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | DH|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|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":68.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":[],"id":23835,"numValue":120.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":23836,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23837,"numValue":1.6,"reference... | [{"id":7044,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3593 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,593 | train | mutant | 631 | 48 | 683 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P89G | P89G | 1 | 1 | 0 | 0 | 89 | P | G | 1 | CONSERVATION | 1LZ1 | 405 | null | 89 | A | T | false | false | 69.452454 | 29.662857 | 9,879 | ProTherm | 3 | CD | GdnHCl | glycine-HCl | 40 mM | 25 | 1LZ1_A:P71G | null | null | 8.5 | 1.2 | null | null | null | 2.63 | 5.43 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 658 | ARTICLE | Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization. | 1,991 | 10.1021/bi00105a011 | 1911779 | Biochemistry;30;9882-91 | 4 | Yutani K|Kikuchi M|Herning T|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":33954,"numValue":8.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33955,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33956,"numValue":5.43,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33957,"numValue":2.63,"references":[],"s... | [{"id":7044,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,594 | train | mutant | 6,797 | 48 | 7,439 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P89G|P121G | P89G|P121G | 2 | 2 | 0 | 0 | 89 | P | G | 1 | CONSERVATION | 1LZ1 | 405 | null | 89|121 | A | T | false | false | 105.139632 | 45.135714 | 14,594 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | null | 1LZ1_A:P71G 1LZ1_A:P103G | 64.3 | -4.5 | null | null | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:P71G 1LZ1_A:P1... | [{"datasets":[],"id":53965,"numValue":64.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53966,"numValue":-4.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53967,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53968,"numValue":null,"references":[... | [{"id":7044,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7076,"numValue":5.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,595 | train | mutant | 6,797 | 48 | 7,439 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P89G|P121G | P89G|P121G | 2 | 2 | 0 | 0 | 89 | P | G | 1 | CONSERVATION | 1LZ1 | 405 | null | 89|121 | A | T | false | false | 105.139632 | 45.135714 | 14,885 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | 68.8 | 1LZ1_A:P71G 1LZ1_A:P103G | null | null | null | 1.6 | 120.5 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":68.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":[],"id":54903,"numValue":120.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":54904,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":54905,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54906,"numValue":null,"references":[... | [{"id":7044,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7076,"numValue":5.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,596 | train | mutant | 6,797 | 48 | 7,439 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P89G|P121G | P89G|P121G | 2 | 2 | 0 | 0 | 89 | P | G | 1 | CONSERVATION | 1LZ1 | 405 | null | 89|121 | A | T | false | false | 105.139632 | 45.135714 | 15,245 | ProTherm | 3 | CD | GdnHCl | glycine-HCl | 40 mM | 25 | 1LZ1_A:P71G 1LZ1_A:P103G | null | null | 8.6 | 1.1 | null | null | null | 2.64 | 5.48 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 658 | ARTICLE | Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization. | 1,991 | 10.1021/bi00105a011 | 1911779 | Biochemistry;30;9882-91 | 4 | Yutani K|Kikuchi M|Herning T|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":55958,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":55959,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55960,"numValue":5.48,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":55961,"numValue":2.64,"references":[],"s... | [{"id":7044,"numValue":1.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":7076,"numValue":5.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,597 | train | mutant | 293 | 48 | 325 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G90A | G90A | 1 | 1 | 0 | 0 | 90 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 90 | A | T | false | false | 61.739216 | 54.8375 | 517 | ProTherm | 2.38 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G72A | 58.2 | null | null | null | 99.9 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.38,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G72A","type":"_P... | [{"datasets":[],"id":2070,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2071,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2072,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7045,"numValue":2.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,598 | train | mutant | 293 | 48 | 325 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G90A | G90A | 1 | 1 | 0 | 0 | 90 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 90 | A | T | false | false | 61.739216 | 54.8375 | 518 | ProTherm | 2.64 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G72A | 62.6 | null | null | null | 106.12 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.64,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G72A","type":"_P... | [{"datasets":[],"id":2073,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2074,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2075,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7045,"numValue":2.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,599 | train | mutant | 293 | 48 | 325 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G90A | G90A | 1 | 1 | 0 | 0 | 90 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 90 | A | T | false | false | 61.739216 | 54.8375 | 519 | ProTherm | 3.16 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G72A | 72.2 | null | null | null | 119.98 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.16,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G72A","type":"_P... | [{"datasets":[],"id":2076,"numValue":72.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2077,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2078,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7045,"numValue":2.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,600 | train | mutant | 293 | 48 | 325 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G90A | G90A | 1 | 1 | 0 | 0 | 90 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 90 | A | T | false | false | 61.739216 | 54.8375 | 535 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G72A | 63.8 | -1.1 | null | null | 109.46 | 1.43 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G72A","type":"_PD... | [{"datasets":[],"id":2133,"numValue":63.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2134,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2135,"numValue":109.46,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2136,"numValue":1.43,"references":[],"... | [{"id":7045,"numValue":2.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,601 | train | mutant | 293 | 48 | 325 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G90A | G90A | 1 | 1 | 0 | 0 | 90 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 90 | A | T | false | false | 61.739216 | 54.8375 | 6,878 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:G72A | null | null | null | 0.36 | null | 1.43 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24315,"numValue":1.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24316,"numValue":0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24317,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":7045,"numValue":2.0,"position":90,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,602 | train | mutant | 675 | 48 | 731 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92G | V92G | 1 | 1 | 0 | 0 | 92 | V | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,121 | ProTherm | 2.53 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74G | 61.28 | null | null | null | 108.03 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.53,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74G","type"... | [{"datasets":[],"id":4184,"numValue":61.28,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4185,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4186,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,604 | train | mutant | 675 | 48 | 731 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92G | V92G | 1 | 1 | 0 | 0 | 92 | V | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,123 | ProTherm | 2.95 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74G | 68.71 | null | null | null | 120.94 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.95,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74G","type"... | [{"datasets":[],"id":4190,"numValue":68.71,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4191,"numValue":120.94,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4192,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,605 | train | mutant | 675 | 48 | 731 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92G | V92G | 1 | 1 | 0 | 0 | 92 | V | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,124 | ProTherm | 3.09 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74G | 70.82 | null | null | null | 124.04 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.09,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74G","type"... | [{"datasets":[],"id":4193,"numValue":70.82,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4194,"numValue":124.04,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4195,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,606 | train | mutant | 675 | 48 | 731 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92G | V92G | 1 | 1 | 0 | 0 | 92 | V | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,125 | ProTherm | 3.3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74G | 74.04 | null | null | null | 129.06 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74G","type":... | [{"datasets":[],"id":4196,"numValue":74.04,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4197,"numValue":129.06,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4198,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,608 | train | mutant | 675 | 48 | 731 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92G | V92G | 1 | 1 | 0 | 0 | 92 | V | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,186 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74G | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74G","type":... | [{"datasets":[],"id":4404,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4405,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,609 | train | mutant | 675 | 48 | 731 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92G | V92G | 1 | 1 | 0 | 0 | 92 | V | G | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,944 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V74G | null | null | null | 0.22 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24498,"numValue":0.22,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24499,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,610 | train | mutant | 676 | 48 | 732 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92I | V92I | 1 | 1 | 0 | 0 | 92 | V | I | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,126 | ProTherm | 2.67 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74I | 66.07 | null | null | null | 89.87 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.67,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74I","type"... | [{"datasets":[],"id":4199,"numValue":66.07,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4200,"numValue":89.87,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4201,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,611 | train | mutant | 676 | 48 | 732 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92I | V92I | 1 | 1 | 0 | 0 | 92 | V | I | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,127 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74I | 68.29 | null | null | null | 92.5 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.8,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74I","type":... | [{"datasets":[],"id":4202,"numValue":68.29,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4203,"numValue":92.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4204,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,612 | train | mutant | 676 | 48 | 732 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92I | V92I | 1 | 1 | 0 | 0 | 92 | V | I | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,128 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74I | 71.67 | null | null | null | 96.56 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74I","type":... | [{"datasets":[],"id":4205,"numValue":71.67,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4206,"numValue":96.56,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4207,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,613 | train | mutant | 676 | 48 | 732 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92I | V92I | 1 | 1 | 0 | 0 | 92 | V | I | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,172 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74I | 66.6 | 1.7 | null | null | 88.43 | 1.2 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74I","type":... | [{"datasets":[],"id":4349,"numValue":66.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4350,"numValue":1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4351,"numValue":88.43,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id"... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,614 | train | mutant | 676 | 48 | 732 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92I | V92I | 1 | 1 | 0 | 0 | 92 | V | I | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,187 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74I | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74I","type":... | [{"datasets":[],"id":4406,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4407,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3615 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,615 | train | mutant | 676 | 48 | 732 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92I | V92I | 1 | 1 | 0 | 0 | 92 | V | I | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,945 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V74I | null | null | null | -0.45 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24500,"numValue":-0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24501,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3616 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,616 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,129 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74L | 62.35 | null | null | null | 100.14 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.5,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74L","type":... | [{"datasets":[],"id":4208,"numValue":62.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4209,"numValue":100.14,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4210,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,617 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,130 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74L | 65.28 | null | null | null | 103.97 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74L","type":... | [{"datasets":[],"id":4211,"numValue":65.28,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4212,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4213,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,618 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,131 | ProTherm | 2.83 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74L | 67.51 | null | null | null | 107.07 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.83,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74L","type"... | [{"datasets":[],"id":4214,"numValue":67.51,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4215,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4216,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,619 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,132 | ProTherm | 3.05 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74L | 71.61 | null | null | null | 112.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.05,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74L","type"... | [{"datasets":[],"id":4217,"numValue":71.61,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4218,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4219,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3620 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,620 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,133 | ProTherm | 3.15 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74L | 73.32 | null | null | null | 114.01 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.15,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74L","type"... | [{"datasets":[],"id":4220,"numValue":73.32,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4221,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4222,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,621 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,173 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74L | 65.5 | 0.6 | null | null | 103.49 | 1.27 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74L","type":... | [{"datasets":[],"id":4354,"numValue":65.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4355,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4356,"numValue":103.49,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,622 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,188 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74L | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74L","type":... | [{"datasets":[],"id":4408,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4409,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,623 | train | mutant | 677 | 48 | 733 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92L | V92L | 1 | 1 | 0 | 0 | 92 | V | L | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,946 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V74L | null | null | null | -0.19 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24502,"numValue":-0.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24503,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,624 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,134 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74M | 63.42 | null | null | null | 107.07 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.5,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74M","type":... | [{"datasets":[],"id":4223,"numValue":63.42,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4224,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4225,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,625 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,135 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74M | 66.86 | null | null | null | 113.05 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74M","type":... | [{"datasets":[],"id":4226,"numValue":66.86,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4227,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4228,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,626 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,136 | ProTherm | 2.83 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74M | 69.38 | null | null | null | 117.11 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.83,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74M","type"... | [{"datasets":[],"id":4229,"numValue":69.38,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4230,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4231,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,627 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,137 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74M | 73.23 | null | null | null | 123.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.1,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74M","type":... | [{"datasets":[],"id":4232,"numValue":73.23,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4233,"numValue":123.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4234,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,628 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,138 | ProTherm | 3.2 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74M | 74.95 | null | null | null | 125 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74M","type":... | [{"datasets":[],"id":4235,"numValue":74.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4236,"numValue":125.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4237,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,629 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,174 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74M | 66.9 | 2 | null | null | 109.46 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74M","type":... | [{"datasets":[],"id":4359,"numValue":66.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4360,"numValue":2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4361,"numValue":109.46,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,630 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,189 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74M | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74M","type":... | [{"datasets":[],"id":4410,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4411,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,631 | train | mutant | 678 | 48 | 734 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92M | V92M | 1 | 1 | 0 | 0 | 92 | V | M | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,947 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V74M | null | null | null | -0.65 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24504,"numValue":-0.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24505,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3632 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,632 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,139 | ProTherm | 2.68 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74F | 63.65 | null | null | null | 108.03 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.68,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74F","type"... | [{"datasets":[],"id":4238,"numValue":63.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4239,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4240,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,633 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,140 | ProTherm | 2.84 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74F | 66.32 | null | null | null | 112.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.84,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74F","type"... | [{"datasets":[],"id":4241,"numValue":66.32,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4242,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4243,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,634 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,141 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74F | 70.5 | null | null | null | 117.11 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.1,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74F","type":... | [{"datasets":[],"id":4244,"numValue":70.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4245,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4246,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,635 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,142 | ProTherm | 3.23 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74F | 72.44 | null | null | null | 119.98 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.23,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74F","type"... | [{"datasets":[],"id":4247,"numValue":72.44,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4248,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4249,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,636 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,143 | ProTherm | 3.4 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74F | 75.6 | null | null | null | 124.04 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.4,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74F","type":... | [{"datasets":[],"id":4250,"numValue":75.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4251,"numValue":124.04,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4252,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,637 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,175 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74F | 64 | -0.9 | null | null | 109.7 | 1.34 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74F","type":... | [{"datasets":[],"id":4364,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4365,"numValue":-0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4366,"numValue":109.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,638 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,190 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V74F | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74F","type":... | [{"datasets":[],"id":4412,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4413,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,639 | train | mutant | 679 | 48 | 735 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92F | V92F | 1 | 1 | 0 | 0 | 92 | V | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,948 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V74F | null | null | null | 0.29 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24506,"numValue":0.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24507,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,640 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,278 | ProTherm | 2.61 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74S | 62.1 | null | null | null | 104.92 | null | 109.94 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.61,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4704,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4705,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4706,"numValue":109.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["H... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,641 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,279 | ProTherm | 2.83 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74S | 66 | null | null | null | 108.99 | null | 114.96 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4708,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4709,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4710,"numValue":114.96,"references":[],"strValue":null,"type":"DH... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3642 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,642 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,280 | ProTherm | 3.28 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74S | 72.2 | null | null | null | 117.11 | null | 121.89 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.28,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_P... | [{"datasets":[],"id":4712,"numValue":72.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4713,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4714,"numValue":121.89,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4715,"numValue":null,"references":[... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3643 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,643 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 1,322 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V74S | 64.9 | 0 | null | null | 108.03 | 1.22 | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DH|DCP|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4875,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4876,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4877,"numValue":108.03,"r... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3644 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,644 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,893 | ProTherm | 2.61 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74S | 62.1 | null | null | null | 104.92 | null | 109.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.61,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_P... | [{"datasets":[],"id":14331,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14332,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14333,"numValue":109.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14334,"numValue":null,"reference... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,645 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,894 | ProTherm | 2.83 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74S | 66 | null | null | null | 108.99 | null | 114.96 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_P... | [{"datasets":[],"id":14335,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14336,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14337,"numValue":114.96,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14338,"numValue":null,"reference... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,646 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,895 | ProTherm | 3.28 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74S | 72.2 | null | null | null | 117.11 | null | 121.89 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":3.28,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_P... | [{"datasets":[],"id":14339,"numValue":72.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14340,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14341,"numValue":121.89,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14342,"numValue":null,"reference... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,647 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,911 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74S | 63.7 | -1.2 | null | null | 108.03 | 1.22 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14407,"numValue":63.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":14408,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMU... | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,648 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 3,920 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V74S | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V74S","type":"_PD... | [{"datasets":[],"id":14437,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14438,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3649 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,649 | train | mutant | 723 | 48 | 789 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V92S | V92S | 1 | 1 | 0 | 0 | 92 | V | S | 3 | CONSERVATION | 1LZ1 | 405 | null | 92 | A | L | false | false | 90.089223 | 46.395715 | 6,914 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V74S | null | null | null | 0.38 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24430,"numValue":0.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24431,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7047,"numValue":3.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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