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:3432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,432 | train | mutant | 2,049 | 48 | 2,288 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74L | I74L | 1 | 1 | 0 | 0 | 74 | I | L | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,976 | ProTherm | 2.65 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56L | 64 | null | null | null | 104.92 | 1.55 | 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":2.65,"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:I56L","type":"_P... | [{"datasets":[],"id":14633,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14634,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14635,"numValue":1.55,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14636,"numValue":119.02,"references... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,433 | train | mutant | 2,049 | 48 | 2,288 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74L | I74L | 1 | 1 | 0 | 0 | 74 | I | L | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,977 | ProTherm | 2.96 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56L | 68.7 | null | null | null | 112.09 | 1.27 | 125 | 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":2.96,"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:I56L","type":"_P... | [{"datasets":[],"id":14638,"numValue":68.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14639,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14640,"numValue":1.27,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14641,"numValue":125.0,"references"... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,435 | train | mutant | 2,049 | 48 | 2,288 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74L | I74L | 1 | 1 | 0 | 0 | 74 | I | L | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,018 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56L | 64.6 | -0.3 | null | null | 107.31 | 1.41 | 119.24 | 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:I56L","type":"_PD... | [{"datasets":[],"id":14843,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14844,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14845,"numValue":107.31,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3436 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,436 | train | mutant | 2,049 | 48 | 2,288 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74L | I74L | 1 | 1 | 0 | 0 | 74 | I | L | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,033 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56L | 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:I56L","type":"_PD... | [{"datasets":[],"id":14925,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14926,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3437 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,437 | train | mutant | 2,049 | 48 | 2,288 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74L | I74L | 1 | 1 | 0 | 0 | 74 | I | L | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,920 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56L | null | null | null | 0.1 | 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":24442,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24443,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3438 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,438 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,979 | ProTherm | 2.54 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56M | 56.3 | null | null | null | 92.5 | 1.39 | 103.01 | 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":2.54,"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:I56M","type":"_P... | [{"datasets":[],"id":14648,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14649,"numValue":92.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14650,"numValue":1.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14651,"numValue":103.01,"references":... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3439 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,439 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,980 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56M | 59.2 | null | null | null | 97.28 | 1.63 | 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":2.7,"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:I56M","type":"_PD... | [{"datasets":[],"id":14653,"numValue":59.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14654,"numValue":97.28,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14655,"numValue":1.63,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14656,"numValue":107.07,"references"... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3440 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,440 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,981 | ProTherm | 2.83 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56M | 61.3 | null | null | null | 101.1 | 1.72 | 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":2.83,"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:I56M","type":"_P... | [{"datasets":[],"id":14658,"numValue":61.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14659,"numValue":101.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14660,"numValue":1.72,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14661,"numValue":109.94,"references"... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3441 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,441 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,982 | ProTherm | 3.02 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56M | 64.2 | null | null | null | 104.92 | 1.43 | 113.05 | 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":3.02,"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:I56M","type":"_P... | [{"datasets":[],"id":14663,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14664,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14665,"numValue":1.43,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14666,"numValue":113.05,"references... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3442 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,442 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,983 | ProTherm | 3.11 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56M | 65.9 | null | null | null | 107.07 | 1.53 | 115.92 | 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":3.11,"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:I56M","type":"_P... | [{"datasets":[],"id":14668,"numValue":65.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14669,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14670,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14671,"numValue":115.92,"references... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3443 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,443 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,019 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56M | 59.1 | -5.8 | null | null | 105.88 | 1.53 | 115.08 | 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:I56M","type":"_PD... | [{"datasets":[],"id":14849,"numValue":59.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14850,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14851,"numValue":105.88,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3444 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,444 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,034 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56M | 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:I56M","type":"_PD... | [{"datasets":[],"id":14927,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14928,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3445 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,445 | train | mutant | 2,050 | 48 | 2,289 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74M | I74M | 1 | 1 | 0 | 0 | 74 | I | M | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,921 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56M | null | null | null | 1.77 | 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":24444,"numValue":1.77,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24445,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3446 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,446 | train | mutant | 2,051 | 48 | 2,290 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74F | I74F | 1 | 1 | 0 | 0 | 74 | I | F | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,984 | ProTherm | 2.75 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56F | 50.8 | null | null | null | 76 | 1.89 | 79.35 | 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":2.75,"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:I56F","type":"_P... | [{"datasets":[],"id":14673,"numValue":50.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14674,"numValue":76.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14675,"numValue":1.89,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14676,"numValue":79.35,"references":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3447 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,447 | train | mutant | 2,051 | 48 | 2,290 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74F | I74F | 1 | 1 | 0 | 0 | 74 | I | F | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,985 | ProTherm | 3.06 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56F | 56.3 | null | null | null | 86.04 | 1.77 | 89.63 | 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":3.06,"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:I56F","type":"_P... | [{"datasets":[],"id":14678,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14679,"numValue":86.04,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14680,"numValue":1.77,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14681,"numValue":89.63,"references":... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3448 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,448 | train | mutant | 2,051 | 48 | 2,290 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74F | I74F | 1 | 1 | 0 | 0 | 74 | I | F | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,020 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56F | 49.9 | -15 | null | null | 101.58 | 1.82 | 105.81 | 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:I56F","type":"_PD... | [{"datasets":[],"id":14855,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14856,"numValue":-15.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14857,"numValue":101.58,"references":[],"strValue":null,"type":"DH"},{"datasets":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3449 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,449 | train | mutant | 2,051 | 48 | 2,290 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74F | I74F | 1 | 1 | 0 | 0 | 74 | I | F | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,035 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56F | 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:I56F","type":"_PD... | [{"datasets":[],"id":14929,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14930,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3450 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,450 | train | mutant | 2,051 | 48 | 2,290 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74F | I74F | 1 | 1 | 0 | 0 | 74 | I | F | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,922 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56F | null | null | null | 4.09 | 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":24446,"numValue":4.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24447,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3451 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,451 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,021 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56T | 52.4 | -12.5 | null | null | 101.58 | 1.08 | 108.03 | 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:I56T","type":"_PD... | [{"datasets":[],"id":14861,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14862,"numValue":-12.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14863,"numValue":101.58,"references":[],"strValue":null,"type":"DH"},{"datasets":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3452 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,452 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,036 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56T | 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:I56T","type":"_PD... | [{"datasets":[],"id":14931,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14932,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3453 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,453 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,158 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56T | 52.4 | -12.5 | null | null | 101.67 | 1.24 | 108.16 | 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 | 389 | ARTICLE | The structure, stability, and folding process of amyloidogenic mutant human lysozyme. | 1,996 | 10.1093/oxfordjournals.jbchem.a021544 | 9010773 | J Biochem;120;1216-23 | 5 | Takano K|Yamagata Y|Yutani K|Ogasahara 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:I56T","type":"_PD... | [{"datasets":[],"id":15394,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15395,"numValue":-12.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15396,"numValue":101.67,"references":[],"strValue":null,"type":"DH"},{"datasets":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3454 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,454 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,159 | ProTherm | 3.11 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56T | 60.52 | null | null | null | 97.61 | 1.15 | 103.3 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 389 | ARTICLE | The structure, stability, and folding process of amyloidogenic mutant human lysozyme. | 1,996 | 10.1093/oxfordjournals.jbchem.a021544 | 9010773 | J Biochem;120;1216-23 | 5 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Funahashi J | [{"numValue":3.11,"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:I56T","type":"_P... | [{"datasets":[],"id":15400,"numValue":60.52,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15401,"numValue":97.61,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15402,"numValue":1.15,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":15403,"numValue":103.3,"references"... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3455 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,455 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,160 | ProTherm | 2.98 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56T | 57.96 | null | null | null | 93.3 | 1.2 | 102.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 389 | ARTICLE | The structure, stability, and folding process of amyloidogenic mutant human lysozyme. | 1,996 | 10.1093/oxfordjournals.jbchem.a021544 | 9010773 | J Biochem;120;1216-23 | 5 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Funahashi J | [{"numValue":2.98,"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:I56T","type":"_P... | [{"datasets":[],"id":15405,"numValue":57.96,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15406,"numValue":93.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15407,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":15408,"numValue":102.2,"references":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3456 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,456 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,161 | ProTherm | 2.67 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56T | 51.78 | null | null | null | 87.8 | 1 | 90.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 389 | ARTICLE | The structure, stability, and folding process of amyloidogenic mutant human lysozyme. | 1,996 | 10.1093/oxfordjournals.jbchem.a021544 | 9010773 | J Biochem;120;1216-23 | 5 | Takano K|Yamagata Y|Yutani K|Ogasahara 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","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56T","type":"_P... | [{"datasets":[],"id":15410,"numValue":51.78,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15411,"numValue":87.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15412,"numValue":1.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":15413,"numValue":90.9,"references":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3457 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,457 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,887 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56T | null | null | null | 3.64 | null | 1.24 | 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 | 389 | ARTICLE | The structure, stability, and folding process of amyloidogenic mutant human lysozyme. | 1,996 | 10.1093/oxfordjournals.jbchem.a021544 | 9010773 | J Biochem;120;1216-23 | 5 | Takano K|Yamagata Y|Yutani K|Ogasahara 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":[],"id":24342,"numValue":1.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24343,"numValue":3.64,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24344,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3458 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,458 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,923 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56T | null | null | null | 3.63 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | 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":[],"id":24448,"numValue":3.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24449,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3459 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,459 | train | mutant | 2,058 | 48 | 2,297 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74T | I74T | 1 | 1 | 0 | 0 | 74 | I | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 13,912 | ProTherm | 4 | CD | GdnHCl | GdnHCl | 40 mM | 10 | 1LZ1_A:I56T | null | null | 7.31 | 6.67 | null | null | null | 2.7 | 2.96 | 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":51485,"numValue":7.31,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":51486,"numValue":6.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":51487,"numValue":2.96,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":51488,"numValue":2.7,"references":[],"... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3460 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,460 | train | mutant | 193 | 48 | 221 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76A | Q76A | 1 | 1 | 0 | 0 | 76 | Q | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 349 | ProTherm | 2.5 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Q58A | 64.5 | null | null | null | 97.04 | null | 103.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | M47andM8_S2760.csv|EASE-MM_S1676.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.5,"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:Q58A","type":"_PD... | [{"datasets":["M47andM8_S2760.csv"],"id":1430,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1431,"numValue":97.04,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1432,"numValue":103.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["EASE-MM_S1676.csv","M4... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3461 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,461 | train | mutant | 193 | 48 | 221 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76A | Q76A | 1 | 1 | 0 | 0 | 76 | Q | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 350 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Q58A | 67.8 | null | null | null | 103.97 | null | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 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:Q58A","type":"_PD... | [{"datasets":[],"id":1434,"numValue":67.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":1435,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1436,"numValu... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3462 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,462 | train | mutant | 193 | 48 | 221 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76A | Q76A | 1 | 1 | 0 | 0 | 76 | Q | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 351 | ProTherm | 3.1 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Q58A | 75.1 | null | null | null | 114.96 | null | 123.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.1,"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:Q58A","type":"_PD... | [{"datasets":[],"id":1438,"numValue":75.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1439,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1440,"numValue":123.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1441,"numValue":null,"references":[... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3463 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,463 | train | mutant | 193 | 48 | 221 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76A | Q76A | 1 | 1 | 0 | 0 | 76 | Q | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 368 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Q58A | 68 | 3.1 | null | null | 98.23 | 1.65 | 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 | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 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:Q58A","type":"_PD... | [{"datasets":[],"id":1511,"numValue":68.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1512,"numValue":3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1513,"numValue":98.23,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id"... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3464 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,464 | train | mutant | 193 | 48 | 221 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76A | Q76A | 1 | 1 | 0 | 0 | 76 | Q | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 6,868 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:Q58A | null | null | null | -0.91 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24289,"numValue":-0.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24290,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3465 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,465 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 3,890 | ProTherm | 2.59 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Q58G | 68.3 | null | null | null | 113.05 | null | 120.94 | 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 | 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":2.59,"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:Q58G","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14319,"numValue":68.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14320,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3466 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,466 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 3,891 | ProTherm | 2.78 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Q58G | 72.5 | null | null | null | 119.02 | null | 126.91 | 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 | 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":2.78,"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:Q58G","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14323,"numValue":72.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14324,"numValue":119.02,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3467 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,467 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 3,892 | ProTherm | 3.15 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Q58G | 78.7 | null | null | null | 126.91 | null | 135.04 | 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 | 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":3.15,"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:Q58G","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14327,"numValue":78.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14328,"numValue":126.91,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14329,"numValue":135.04,"references":[],"strValue":null,"type":"DHVH"},{"datasets"... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3468 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,468 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 3,910 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Q58G | 70.6 | 5.7 | null | null | 108.75 | 1.34 | 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|PoPMuSiC-2.0_S2648.csv|Saraboji_S1791.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:Q58G","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":14402,"numValue":70.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":14403,"numValue":5.7,"refer... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3469 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,469 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 3,919 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Q58G | 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:Q58G","type":"_PD... | [{"datasets":[],"id":14435,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14436,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3470 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,470 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 4,202 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:Q58G | 70.6 | 5.7 | 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 | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Q58G","type":... | [{"datasets":[],"id":15578,"numValue":70.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15579,"numValue":5.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15580,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3471 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,471 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 4,206 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:Q58G | 64.9 | null | null | null | 108.75 | 1.34 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Q58G","type":... | [{"datasets":[],"id":15591,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":15592,"numValue":108.75,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":15593,"numValue":1.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":15594,"numValue":null,"references":... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3472 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,472 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 6,913 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:Q58G | null | null | null | -1.86 | 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":24428,"numValue":-1.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24429,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3474 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,474 | train | mutant | 2,021 | 48 | 2,257 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Q76G | Q76G | 1 | 1 | 0 | 0 | 76 | Q | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 76 | A | T | true | true | 12.49499 | 12.982222 | 14,094 | ProTherm | 4 | CD | GdnHCl | glycine-HCl | 40 mM | 10 | 1LZ1_A:Q58G | null | null | 16.4 | -2.06 | null | null | null | 4.26 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 3 | Takano K|Yamagata Y|Yutani K | [{"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":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":52134,"numValue":16.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":52135,"numValue":-2.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":52136,"numValue":4.26,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":52137,"numValue":null,"references":[... | [{"id":7031,"numValue":9.0,"position":76,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3477 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,477 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,336 | ProTherm | 2.98 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59A | 64.5 | null | null | null | 115.1 | 1.63 | 120.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.98,"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:I59A","type":"_P... | [{"datasets":[],"id":12279,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12280,"numValue":115.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12281,"numValue":1.63,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12282,"numValue":120.1,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3478 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,478 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,337 | ProTherm | 2.8 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59A | 61.5 | null | null | null | 110 | 1.2 | 115.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"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:I59A","type":"_PD... | [{"datasets":[],"id":12284,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12285,"numValue":110.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12286,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12287,"numValue":115.1,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,479 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,338 | ProTherm | 2.66 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59A | 59.1 | null | null | null | 106.2 | 1.2 | 114.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.66,"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:I59A","type":"_P... | [{"datasets":[],"id":12289,"numValue":59.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12290,"numValue":106.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12291,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12292,"numValue":114.1,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3480 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,480 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,339 | ProTherm | 2.49 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59A | 55.9 | null | null | null | 101.2 | 0.84 | 108.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.49,"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:I59A","type":"_P... | [{"datasets":[],"id":12294,"numValue":55.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12295,"numValue":101.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12296,"numValue":0.84,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12297,"numValue":108.1,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3481 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,481 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,358 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59A | 59.7 | -5.2 | null | null | null | 1.46 | 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 | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|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:I59A","type":"_PD... | [{"datasets":[],"id":12384,"numValue":59.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12385,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12386,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,482 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,023 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59A | 59.7 | -5.2 | null | null | 114.72 | 1.46 | 120.7 | 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:I59A","type":"_PD... | [{"datasets":[],"id":14873,"numValue":59.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14874,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14875,"numValue":114.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,484 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,905 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59A | null | null | null | 1.72 | 114.8 | 1.46 | 120.9 | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DHVH|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"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":24400,"numValue":114.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24401,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24402,"numValue":120.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["capriotti_S1615_map.csv"],"id":24403,"n... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,485 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,925 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59A | null | null | null | 1.72 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":["capriotti_S1615_map.csv"],"id":24452,"numValue":1.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24453,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3487 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,487 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 7,789 | ProTherm | 2.9 | DSC | Thermal | Gly-HCl | 0.05 M | 47.2 | 1LZ1_A:I59A | null | null | null | null | 72.66 | null | 74.81 | null | null | null | null | null | null | null | null | null | yes | DH|DHVH|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 141 | ARTICLE | Buried water molecules contribute to the conformational stability of a protein. | 2,003 | 10.1093/proeng/gzg001 | 12646687 | Protein Eng;16;5-9 | 3 | Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.9,"strValue":null,"type":"PH"},{"numValue":47.2,"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":26704,"numValue":72.66,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":26705,"numValue":74.81,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":26706,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3488 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,488 | train | mutant | 773 | 48 | 868 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77A | I77A | 1 | 1 | 0 | 0 | 77 | I | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 8,349 | ProTherm | 2.35 | DSC | Thermal | Gly-HCl | 0.05 M | 36.7 | 1LZ1_A:I59A | null | null | null | null | 55.69 | null | 58.08 | null | null | null | null | null | null | null | null | null | yes | DH|DHVH|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 141 | ARTICLE | Buried water molecules contribute to the conformational stability of a protein. | 2,003 | 10.1093/proeng/gzg001 | 12646687 | Protein Eng;16;5-9 | 3 | Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.35,"strValue":null,"type":"PH"},{"numValue":36.7,"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_... | [{"datasets":[],"id":28333,"numValue":55.69,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":28334,"numValue":58.08,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":28335,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,489 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,186 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 44.8 | -4.4 | null | null | 71.29 | 1.67 | 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 | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 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":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59V","type":"_PD... | [{"datasets":[],"id":11638,"numValue":44.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11639,"numValue":-4.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11640,"numValue":71.29,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,490 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,207 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 52 | null | null | null | 75.4 | null | 78.7 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"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:I59V","type":"_PD... | [{"datasets":[],"id":11735,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11736,"numValue":75.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11737,"numValue":78.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11738,"numValue":null,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,491 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,208 | ProTherm | 3 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 50.3 | null | null | null | 74.2 | null | 76.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 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":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I59V","type":"_PD... | [{"datasets":[],"id":11739,"numValue":50.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11740,"numValue":74.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11741,"numValue":76.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11742,"numValue":null,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3492 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,492 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,209 | ProTherm | 2.81 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 46.9 | -5.1 | null | null | 67.5 | null | 71.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.81,"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:I59V","type":"_P... | [{"datasets":[],"id":11743,"numValue":46.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11744,"numValue":-5.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11745,"numValue":67.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3493 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,493 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,210 | ProTherm | 2.68 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 44.3 | null | null | null | 62.9 | null | 67 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.68,"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:I59V","type":"_P... | [{"datasets":[],"id":11748,"numValue":44.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11749,"numValue":62.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11750,"numValue":67.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11751,"numValue":null,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,494 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,024 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 61.5 | -3.4 | null | null | 110.18 | 1.2 | 117.11 | 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:I59V","type":"_PD... | [{"datasets":[],"id":14879,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14880,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14881,"numValue":110.18,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,495 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,039 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 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:I59V","type":"_PD... | [{"datasets":[],"id":14937,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14938,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3496 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,496 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,155 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59V | 61.5 | -3.4 | null | null | 110.3 | 1.2 | 117.3 | 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 | 388 | ARTICLE | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. | 1,995 | 10.1006/jmbi.1995.0599 | 7473760 | J Mol Biol;254;62-76 | 6 | Takano K|Yamagata Y|Ogasahara K|Fujii S|Kaneda H|Kanaya E | [{"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:I59V","type":"_PD... | [{"datasets":[],"id":15376,"numValue":61.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15377,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15378,"numValue":110.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,498 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,926 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59V | null | null | null | 1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":["capriotti_S1615_map.csv"],"id":24454,"numValue":1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24455,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3499 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,499 | train | mutant | 1,720 | 48 | 1,930 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77V | I77V | 1 | 1 | 0 | 0 | 77 | I | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 7,740 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:I59V | null | null | null | 0.93 | null | 1.67 | 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 | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":49.2,"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":26591,"numValue":1.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26592,"numValue":0.93,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26593,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,500 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,351 | ProTherm | 3.16 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59G | 60.4 | null | null | null | 100.2 | 0.81 | 102.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":3.16,"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:I59G","type":"_P... | [{"datasets":[],"id":12351,"numValue":60.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12352,"numValue":100.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12353,"numValue":0.81,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12354,"numValue":102.2,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3501 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,501 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,352 | ProTherm | 3.02 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59G | 59.2 | null | null | null | 98.6 | 0.86 | 100 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":3.02,"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:I59G","type":"_P... | [{"datasets":[],"id":12356,"numValue":59.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12357,"numValue":98.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12358,"numValue":0.86,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12359,"numValue":100.0,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,502 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,353 | ProTherm | 2.82 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59G | 54.6 | null | null | null | 94.7 | 0.65 | 97.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.82,"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:I59G","type":"_P... | [{"datasets":[],"id":12361,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12362,"numValue":94.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12363,"numValue":0.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12364,"numValue":97.6,"references":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3503 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,503 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,354 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59G | 52 | null | null | null | 90.9 | 0.62 | 92.8 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|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:I59G","type":"_PD... | [{"datasets":[],"id":12366,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12367,"numValue":90.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12368,"numValue":0.62,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12369,"numValue":92.8,"references":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,504 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,355 | ProTherm | 2.49 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59G | 48.1 | null | null | null | 84.4 | 0.79 | 89.7 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.49,"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:I59G","type":"_P... | [{"datasets":[],"id":12371,"numValue":48.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12372,"numValue":84.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12373,"numValue":0.79,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12374,"numValue":89.7,"references":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,505 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,361 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59G | 52.2 | -12.7 | null | null | null | 1.24 | 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 | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|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:I59G","type":"_PD... | [{"datasets":[],"id":12396,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12397,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12398,"numValue":1.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3506 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,506 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,022 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59G | 52.2 | -12.7 | null | null | 106.12 | 1.24 | 109.39 | 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:I59G","type":"_PD... | [{"datasets":[],"id":14867,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14868,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14869,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,508 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,908 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59G | null | null | null | 3.83 | 106.2 | 1.24 | 109.5 | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DHVH|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"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":24415,"numValue":106.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24416,"numValue":1.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24417,"numValue":109.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["capriotti_S1615_map.csv","khan_protherm... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,509 | train | mutant | 1,758 | 48 | 1,971 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77G | I77G | 1 | 1 | 0 | 0 | 77 | I | G | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,924 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59G | null | null | null | 3.82 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | 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":[],"id":24450,"numValue":3.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24451,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,510 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,986 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59L | 61.4 | null | null | null | 108.99 | 1.12 | 117.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | khan_protherm_data_mapped.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":2.51,"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:I59L","type":"_P... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":14683,"numValue":61.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14684,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14685,"numValue":1.12,"referen... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3511 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,511 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,987 | ProTherm | 2.66 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59L | 64.5 | null | null | null | 113.05 | 1.17 | 121.89 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | khan_protherm_data_mapped.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":2.66,"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:I59L","type":"_P... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":14688,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14689,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14690,"numValue":1.17,"referen... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3512 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,512 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,988 | ProTherm | 2.83 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59L | 67 | null | null | null | 115.92 | 1.17 | 125.96 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | khan_protherm_data_mapped.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":2.83,"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:I59L","type":"_P... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":14693,"numValue":67.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14694,"numValue":115.92,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14695,"numValue":1.17,"referen... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3513 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,513 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,989 | ProTherm | 2.96 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59L | 69.8 | null | null | null | 119.02 | 1.31 | 128.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | khan_protherm_data_mapped.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":2.96,"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:I59L","type":"_P... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":14698,"numValue":69.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14699,"numValue":119.02,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14700,"numValue":1.31,"referen... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,514 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,990 | ProTherm | 3.17 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59L | 72.1 | null | null | null | 123.09 | 1.24 | 131.93 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | khan_protherm_data_mapped.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":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:I59L","type":"_P... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":14703,"numValue":72.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14704,"numValue":123.09,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14705,"numValue":1.24,"referen... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3515 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,515 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,025 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59L | 64.9 | 0 | null | null | 113.53 | 1.27 | 122.08 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | khan_protherm_data_mapped.csv|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:I59L","type":"_PD... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":14885,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":14886,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.c... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,516 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,040 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59L | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | khan_protherm_data_mapped.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:I59L","type":"_PD... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":14939,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["khan_protherm_data_mapped.csv"],"id":14940,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,517 | train | mutant | 2,052 | 48 | 2,291 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77L | I77L | 1 | 1 | 0 | 0 | 77 | I | L | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,927 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59L | null | null | null | 0 | 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":24456,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":24457,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,519 | train | mutant | 2,053 | 48 | 2,292 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77M | I77M | 1 | 1 | 0 | 0 | 77 | I | M | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,992 | ProTherm | 2.65 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59M | 59.9 | null | null | null | 98.47 | 1 | 108.03 | 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":2.65,"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:I59M","type":"_P... | [{"datasets":[],"id":14713,"numValue":59.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14714,"numValue":98.47,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14715,"numValue":1.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14716,"numValue":108.03,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,520 | train | mutant | 2,053 | 48 | 2,292 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77M | I77M | 1 | 1 | 0 | 0 | 77 | I | M | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,993 | ProTherm | 2.8 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59M | 62 | null | null | null | 103.01 | 1.2 | 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:I59M","type":"_PD... | [{"datasets":[],"id":14718,"numValue":62.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14719,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14720,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14721,"numValue":109.94,"references"... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3521 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,521 | train | mutant | 2,053 | 48 | 2,292 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77M | I77M | 1 | 1 | 0 | 0 | 77 | I | M | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,994 | ProTherm | 2.95 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59M | 64.8 | null | null | null | 106.12 | 1.1 | 114.01 | 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":2.95,"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:I59M","type":"_P... | [{"datasets":[],"id":14723,"numValue":64.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14724,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14725,"numValue":1.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14726,"numValue":114.01,"references"... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,522 | train | mutant | 2,053 | 48 | 2,292 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77M | I77M | 1 | 1 | 0 | 0 | 77 | I | M | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,995 | ProTherm | 3.13 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59M | 66.5 | null | null | null | 107.07 | 1.15 | 117.11 | 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":3.13,"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:I59M","type":"_P... | [{"datasets":[],"id":14728,"numValue":66.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14729,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14730,"numValue":1.15,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14731,"numValue":117.11,"references... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,523 | train | mutant | 2,053 | 48 | 2,292 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77M | I77M | 1 | 1 | 0 | 0 | 77 | I | M | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,026 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59M | 60.7 | -4.2 | null | null | 105.64 | 1.27 | 114.72 | 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:I59M","type":"_PD... | [{"datasets":[],"id":14891,"numValue":60.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14892,"numValue":-4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14893,"numValue":105.64,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,524 | train | mutant | 2,053 | 48 | 2,292 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77M | I77M | 1 | 1 | 0 | 0 | 77 | I | M | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,041 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59M | 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:I59M","type":"_PD... | [{"datasets":[],"id":14941,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14942,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3526 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,526 | train | mutant | 2,054 | 48 | 2,293 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77F | I77F | 1 | 1 | 0 | 0 | 77 | I | F | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,996 | ProTherm | 2.54 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59F | 59.8 | null | null | null | 99.9 | 1.41 | 108.03 | 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":2.54,"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:I59F","type":"_P... | [{"datasets":[],"id":14733,"numValue":59.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14734,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14735,"numValue":1.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14736,"numValue":108.03,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3527 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,527 | train | mutant | 2,054 | 48 | 2,293 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77F | I77F | 1 | 1 | 0 | 0 | 77 | I | F | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,997 | ProTherm | 2.73 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59F | 62.8 | null | null | null | 103.97 | 1.58 | 112.09 | 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":2.73,"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:I59F","type":"_P... | [{"datasets":[],"id":14738,"numValue":62.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14739,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14740,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14741,"numValue":112.09,"references... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,528 | train | mutant | 2,054 | 48 | 2,293 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77F | I77F | 1 | 1 | 0 | 0 | 77 | I | F | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,998 | ProTherm | 2.9 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59F | 65.4 | null | null | null | 108.03 | 1.2 | 115.92 | 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":2.9,"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:I59F","type":"_PD... | [{"datasets":[],"id":14743,"numValue":65.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14744,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14745,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14746,"numValue":115.92,"references"... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,529 | train | mutant | 2,054 | 48 | 2,293 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77F | I77F | 1 | 1 | 0 | 0 | 77 | I | F | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 3,999 | ProTherm | 3.05 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59F | 68 | null | null | null | 110.9 | 1.29 | 119.98 | 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":3.05,"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:I59F","type":"_P... | [{"datasets":[],"id":14748,"numValue":68.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14749,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14750,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14751,"numValue":119.98,"references"... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,530 | train | mutant | 2,054 | 48 | 2,293 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77F | I77F | 1 | 1 | 0 | 0 | 77 | I | F | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,000 | ProTherm | 3.15 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59F | 69.8 | null | null | null | 114.01 | 1.36 | 123.09 | 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:I59F","type":"_P... | [{"datasets":[],"id":14753,"numValue":69.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14754,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14755,"numValue":1.36,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14756,"numValue":123.09,"references... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,532 | train | mutant | 2,054 | 48 | 2,293 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77F | I77F | 1 | 1 | 0 | 0 | 77 | I | F | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,042 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59F | 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:I59F","type":"_PD... | [{"datasets":[],"id":14943,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14944,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,533 | train | mutant | 2,054 | 48 | 2,293 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77F | I77F | 1 | 1 | 0 | 0 | 77 | I | F | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,929 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59F | null | null | null | 0.81 | 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":24460,"numValue":0.81,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24461,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3534 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,534 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,001 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59S | 50.2 | null | null | null | 87 | 1.27 | 92.73 | 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":2.51,"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:I59S","type":"_P... | [{"datasets":[],"id":14758,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14759,"numValue":87.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14760,"numValue":1.27,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14761,"numValue":92.73,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,535 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,002 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59S | 53.1 | null | null | null | 90.82 | 1.2 | 96.8 | 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":2.7,"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:I59S","type":"_PD... | [{"datasets":[],"id":14763,"numValue":53.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14764,"numValue":90.82,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14765,"numValue":1.2,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14766,"numValue":96.8,"references":[]... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,536 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,003 | ProTherm | 2.84 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59S | 55.3 | null | null | null | 94.65 | 1.55 | 99.9 | 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":2.84,"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:I59S","type":"_P... | [{"datasets":[],"id":14768,"numValue":55.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14769,"numValue":94.65,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14770,"numValue":1.55,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14771,"numValue":99.9,"references":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3537 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,537 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,004 | ProTherm | 3.04 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59S | 58.2 | null | null | null | 98.23 | 1.48 | 103.97 | 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":3.04,"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:I59S","type":"_P... | [{"datasets":[],"id":14773,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14774,"numValue":98.23,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14775,"numValue":1.48,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14776,"numValue":103.97,"references"... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,538 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,005 | ProTherm | 3.17 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59S | 60 | null | null | null | 99.9 | 1.24 | 106.12 | 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":3.17,"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:I59S","type":"_P... | [{"datasets":[],"id":14778,"numValue":60.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14779,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14780,"numValue":1.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14781,"numValue":106.12,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3539 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,539 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,028 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59S | 53.1 | -11.8 | null | null | 106.84 | 1.34 | 113.65 | 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:I59S","type":"_PD... | [{"datasets":[],"id":14903,"numValue":53.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14904,"numValue":-11.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14905,"numValue":106.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3540 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,540 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 4,043 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59S | 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:I59S","type":"_PD... | [{"datasets":[],"id":14945,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14946,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3541 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,541 | train | mutant | 2,055 | 48 | 2,294 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I77S | I77S | 1 | 1 | 0 | 0 | 77 | I | S | 9 | CONSERVATION | 1LZ1 | 405 | null | 77 | A | E | true | true | 2.687419 | 13.04625 | 6,930 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I59S | null | null | null | 3.59 | 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":24462,"numValue":3.59,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24463,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,542 | 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 | 4,006 | ProTherm | 2.4 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I59T | 52.9 | null | null | null | 90.34 | 1.65 | 98.71 | 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":2.4,"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":14783,"numValue":52.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14784,"numValue":90.34,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14785,"numValue":1.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14786,"numValue":98.71,"references":... | [{"id":7032,"numValue":9.0,"position":77,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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