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:3760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,760 | train | mutant | 178 | 48 | 206 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117T | V117T | 1 | 1 | 0 | 0 | 117 | V | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 317 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V99T | 63.3 | -1.6 | null | null | null | 1.41 | 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 | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 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:V99T","type":"_PD... | [{"datasets":[],"id":1304,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1305,"numValue":-1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1306,"numValue":1.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3761 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,761 | train | mutant | 178 | 48 | 206 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117T | V117T | 1 | 1 | 0 | 0 | 117 | V | T | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 6,853 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V99T | null | null | null | null | 104.45 | 1.41 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24257,"numValue":104.45,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24258,"numValue":1.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24259,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,763 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 3,192 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V99A | 44.8 | -4.4 | null | null | 66.99 | 1.27 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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:V99A","type":"_PD... | [{"datasets":[],"id":11668,"numValue":44.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11669,"numValue":-4.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11670,"numValue":66.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3764 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,764 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 3,233 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V99A | 52.6 | null | null | null | 70.6 | null | 73.7 | 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:V99A","type":"_PD... | [{"datasets":[],"id":11842,"numValue":52.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11843,"numValue":70.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11844,"numValue":73.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11845,"numValue":null,"references":[... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,765 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 3,234 | ProTherm | 3.02 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V99A | 51 | null | null | null | 68.9 | null | 72.2 | 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":3.02,"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:V99A","type":"_P... | [{"datasets":[],"id":11846,"numValue":51.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11847,"numValue":68.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11848,"numValue":72.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11849,"numValue":null,"references":[... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3766 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,766 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 3,235 | ProTherm | 2.85 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V99A | 48.2 | null | null | null | 67.2 | null | 70.6 | 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":2.85,"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:V99A","type":"_P... | [{"datasets":[],"id":11850,"numValue":48.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11851,"numValue":67.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11852,"numValue":70.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11853,"numValue":null,"references":[... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3767 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,767 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 3,236 | ProTherm | 2.72 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V99A | 45.3 | null | null | null | 62.2 | null | 65.8 | 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":2.72,"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:V99A","type":"_P... | [{"datasets":[],"id":11854,"numValue":45.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11855,"numValue":62.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11856,"numValue":65.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11857,"numValue":null,"references":[... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3768 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,768 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 3,237 | ProTherm | 2.54 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V99A | 41.4 | null | null | null | 56 | null | 59.6 | 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":2.54,"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:V99A","type":"_P... | [{"datasets":[],"id":11858,"numValue":41.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11859,"numValue":56.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11860,"numValue":59.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11861,"numValue":null,"references":[... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,769 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 4,168 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V99A | 61.9 | -3 | null | null | 110.8 | 1.58 | 116.6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 391 | ARTICLE | Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. | 1,997 | 10.1021/bi9621829 | 9020766 | Biochemistry;36;688-98 | 4 | Takano K|Yamagata Y|Yutani K|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:V99A","type":"_PD... | [{"datasets":[],"id":15442,"numValue":61.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15443,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15444,"numValue":110.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,770 | train | mutant | 1,726 | 48 | 1,936 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V117A | V117A | 1 | 1 | 0 | 0 | 117 | V | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 117 | A | H | true | true | 3.475582 | 13.637143 | 6,891 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V99A | null | null | null | 0.98 | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 391 | ARTICLE | Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. | 1,997 | 10.1021/bi9621829 | 9020766 | Biochemistry;36;688-98 | 4 | Takano K|Yamagata Y|Yutani K|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":24354,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":24355,"numValue":0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24356,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7072,"numValue":8.0,"position":117,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,773 | train | mutant | 179 | 48 | 207 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118T | V118T | 1 | 1 | 0 | 0 | 118 | V | T | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 6,854 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V100T | null | null | null | null | 106.84 | 1.53 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 35 | ARTICLE | Contribution of polar groups in the interior of a protein to the conformational stability. | 2,001 | 10.1021/bi002792f | 11294653 | Biochemistry;40;4853-8 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24260,"numValue":106.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24261,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24262,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3775 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,775 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,193 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100A | 46.6 | -2.6 | null | null | 72.25 | 1.84 | 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:V100A","type":"_P... | [{"datasets":[],"id":11673,"numValue":46.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11674,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11675,"numValue":72.25,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3776 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,776 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,238 | ProTherm | 3.15 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100A | 54.4 | null | null | null | 81.8 | null | 84.7 | 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":3.15,"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:V100A","type":"_... | [{"datasets":[],"id":11862,"numValue":54.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11863,"numValue":81.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11864,"numValue":84.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11865,"numValue":null,"references":[... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,777 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,239 | ProTherm | 3.02 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100A | 52 | null | null | null | 77.8 | null | 81.6 | 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":3.02,"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:V100A","type":"_... | [{"datasets":[],"id":11866,"numValue":52.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11867,"numValue":77.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11868,"numValue":81.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11869,"numValue":null,"references":[... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3778 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,778 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,240 | ProTherm | 2.9 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100A | 49.9 | null | null | null | 72.5 | null | 79.2 | 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":2.9,"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:V100A","type":"_P... | [{"datasets":[],"id":11870,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11871,"numValue":72.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11872,"numValue":79.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11873,"numValue":null,"references":[... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,779 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,241 | ProTherm | 2.72 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100A | 46.8 | null | null | null | 68.9 | null | 73.4 | 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":2.72,"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:V100A","type":"_... | [{"datasets":[],"id":11874,"numValue":46.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11875,"numValue":68.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11876,"numValue":73.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11877,"numValue":null,"references":[... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,780 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,242 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100A | 43.5 | null | null | null | 61.5 | null | 70.1 | 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":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:V100A","type":"_... | [{"datasets":[],"id":11878,"numValue":43.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11879,"numValue":61.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11880,"numValue":70.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11881,"numValue":null,"references":[... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3781 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,781 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 4,169 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100A | 64.1 | -0.8 | null | null | 110.3 | 1 | 119.9 | 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 | 391 | ARTICLE | Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. | 1,997 | 10.1021/bi9621829 | 9020766 | Biochemistry;36;688-98 | 4 | Takano K|Yamagata Y|Yutani K|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:V100A","type":"_P... | [{"datasets":[],"id":15448,"numValue":64.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15449,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15450,"numValue":110.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3782 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,782 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 6,892 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V100A | null | null | null | 0.26 | null | 1 | 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 | 391 | ARTICLE | Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. | 1,997 | 10.1021/bi9621829 | 9020766 | Biochemistry;36;688-98 | 4 | Takano K|Yamagata Y|Yutani K|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":24357,"numValue":1.0,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24358,"numValue":0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24359,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3783 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,783 | train | mutant | 1,727 | 48 | 1,937 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118A | V118A | 1 | 1 | 0 | 0 | 118 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 7,747 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V100A | null | null | null | 0.57 | null | 1.84 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":26612,"numValue":1.84,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26613,"numValue":0.57,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26614,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,784 | train | mutant | 2,024 | 48 | 2,260 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118F | V118F | 1 | 1 | 0 | 0 | 118 | V | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,902 | ProTherm | 2.62 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100F | 56.8 | null | null | null | 79.11 | null | 85.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.62,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V100F","type":"_... | [{"datasets":[],"id":14367,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14368,"numValue":79.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14369,"numValue":85.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":14370,"numValue":null,"references"... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3785 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,785 | train | mutant | 2,024 | 48 | 2,260 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118F | V118F | 1 | 1 | 0 | 0 | 118 | V | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,903 | ProTherm | 2.83 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100F | 61 | null | null | null | 84.61 | null | 92.02 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V100F","type":"_... | [{"datasets":[],"id":14371,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14372,"numValue":84.61,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14373,"numValue":92.02,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv",... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3786 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,786 | train | mutant | 2,024 | 48 | 2,260 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118F | V118F | 1 | 1 | 0 | 0 | 118 | V | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,904 | ProTherm | 3.26 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100F | 67.6 | null | null | null | 89.39 | null | 95.36 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv|M47andM8_S1810.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":3.26,"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:V100F","type":"_... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":14375,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv"... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,787 | train | mutant | 2,024 | 48 | 2,260 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118F | V118F | 1 | 1 | 0 | 0 | 118 | V | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,914 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100F | 58.4 | -6.5 | null | null | 87.24 | 0.93 | 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 | 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:V100F","type":"_P... | [{"datasets":[],"id":14422,"numValue":58.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14423,"numValue":-6.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14424,"numValue":87.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,788 | train | mutant | 2,024 | 48 | 2,260 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118F | V118F | 1 | 1 | 0 | 0 | 118 | V | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 3,923 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V100F | 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:V100F","type":"_P... | [{"datasets":[],"id":14443,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14444,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,789 | train | mutant | 2,024 | 48 | 2,260 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V118F | V118F | 1 | 1 | 0 | 0 | 118 | V | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 118 | A | H | false | false | 1.083724 | 16.837143 | 6,917 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V100F | null | null | null | 1.65 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":24436,"numValue":1.65,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24437,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7073,"numValue":6.0,"position":118,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3790 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,790 | train | mutant | 48 | 48 | 53 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D120N | D120N | 1 | 1 | 0 | 0 | 120 | D | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 120 | A | S | false | false | 50.314383 | 31.253749 | 48 | ProTherm | 2.2 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | 1LZ1_A:D102N | 58.1 | 0.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:D10... | [{"datasets":[],"id":163,"numValue":58.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":164,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":165,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7075,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3792 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,792 | train | mutant | 48 | 48 | 53 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D120N | D120N | 1 | 1 | 0 | 0 | 120 | D | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 120 | A | S | false | false | 50.314383 | 31.253749 | 58 | ProTherm | 2.3 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | KCl | 0.2 M | 1LZ1_A:D102N | 56.7 | 0.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":2.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine hydrochloride","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type... | [{"datasets":[],"id":193,"numValue":56.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":194,"numValue":0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":195,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7075,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,793 | train | mutant | 48 | 48 | 53 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D120N | D120N | 1 | 1 | 0 | 0 | 120 | D | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 120 | A | S | false | false | 50.314383 | 31.253749 | 62 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | null | KCl | 0.2 M | 1LZ1_A:D102N | 77.9 | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"... | [{"datasets":[],"id":205,"numValue":77.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":206,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":207,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7075,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3794 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,794 | train | mutant | 48 | 48 | 53 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D120N | D120N | 1 | 1 | 0 | 0 | 120 | D | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 120 | A | S | false | false | 50.314383 | 31.253749 | 6,841 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | 65 | 1LZ1_A:D102N | null | null | 4.76 | 0.67 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":65.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"B... | [{"datasets":[],"id":24221,"numValue":4.76,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":24222,"numValue":0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24223,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7075,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3795 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,795 | train | mutant | 48 | 48 | 53 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D120N | D120N | 1 | 1 | 0 | 0 | 120 | D | N | 3 | CONSERVATION | 1LZ1 | 405 | null | 120 | A | S | false | false | 50.314383 | 31.253749 | 6,845 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | 65 | KCl | 0.2 M | 1LZ1_A:D102N | null | null | 4.13 | -0.07 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":65.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"B... | [{"datasets":[],"id":24233,"numValue":4.13,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24234,"numValue":-0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24235,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":7075,"numValue":3.0,"position":120,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,796 | train | mutant | 632 | 48 | 684 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P121G | P121G | 1 | 1 | 0 | 0 | 121 | P | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 121 | A | T | false | false | 140.82681 | 60.608572 | 1,049 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | null | 1LZ1_A:P103G | 68.7 | -0.1 | null | null | null | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | HotMuSiC_S1626.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:P103G","type":... | [{"datasets":["HotMuSiC_S1626.csv"],"id":3920,"numValue":68.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["Saraboji_S1791.csv"],"id":3921,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3922,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":7076,"numValue":5.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3797 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,797 | train | mutant | 632 | 48 | 684 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P121G | P121G | 1 | 1 | 0 | 0 | 121 | P | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 121 | A | T | false | false | 140.82681 | 60.608572 | 6,702 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | 68.8 | 1LZ1_A:P103G | null | null | null | 0.1 | 119.7 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":68.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":[],"id":23839,"numValue":119.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":23840,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23841,"numValue":0.1,"reference... | [{"id":7076,"numValue":5.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3798 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,798 | train | mutant | 632 | 48 | 684 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | P121G | P121G | 1 | 1 | 0 | 0 | 121 | P | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 121 | A | T | false | false | 140.82681 | 60.608572 | 9,880 | ProTherm | 3 | CD | GdnHCl | glycine-HCl | 40 mM | 25 | 1LZ1_A:P103G | null | null | 9.7 | 0 | null | null | null | 2.95 | 5.55 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 658 | ARTICLE | Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization. | 1,991 | 10.1021/bi00105a011 | 1911779 | Biochemistry;30;9882-91 | 4 | Yutani K|Kikuchi M|Herning T|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":33959,"numValue":9.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33960,"numValue":0.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33961,"numValue":5.55,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33962,"numValue":2.95,"references":[],"s... | [{"id":7076,"numValue":5.0,"position":121,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,799 | train | mutant | 294 | 48 | 326 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G123A | G123A | 1 | 1 | 0 | 0 | 123 | G | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 123 | A | G | false | false | 14.073099 | 18.595 | 520 | ProTherm | 2.3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G105A | 56.1 | null | null | null | 90.82 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.3,"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:G105A","type":"_P... | [{"datasets":[],"id":2079,"numValue":56.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2080,"numValue":90.82,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2081,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7078,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3800 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,800 | train | mutant | 294 | 48 | 326 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G123A | G123A | 1 | 1 | 0 | 0 | 123 | G | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 123 | A | G | false | false | 14.073099 | 18.595 | 521 | ProTherm | 2.65 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G105A | 61.3 | null | null | null | 97.51 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.65,"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:G105A","type":"_... | [{"datasets":[],"id":2082,"numValue":61.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2083,"numValue":97.51,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2084,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7078,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,801 | train | mutant | 294 | 48 | 326 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G123A | G123A | 1 | 1 | 0 | 0 | 123 | G | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 123 | A | G | false | false | 14.073099 | 18.595 | 522 | ProTherm | 3.2 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G105A | 71.8 | null | null | null | 112.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.2,"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:G105A","type":"_P... | [{"datasets":[],"id":2085,"numValue":71.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2086,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2087,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7078,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,802 | train | mutant | 294 | 48 | 326 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G123A | G123A | 1 | 1 | 0 | 0 | 123 | G | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 123 | A | G | false | false | 14.073099 | 18.595 | 536 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G105A | 62.8 | -2.1 | null | null | 102.53 | 1.36 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"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:G105A","type":"_P... | [{"datasets":[],"id":2138,"numValue":62.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2139,"numValue":-2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["M47andM8_S2760.csv"],"id":2140,"numValue":102.53,"references":[],"strValue":null,"type":"DH"},{"datasets":["M47andM8_S2760.csv"],"id... | [{"id":7078,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3803 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,803 | train | mutant | 294 | 48 | 326 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G123A | G123A | 1 | 1 | 0 | 0 | 123 | G | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 123 | A | G | false | false | 14.073099 | 18.595 | 6,879 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:G105A | null | null | null | 0.62 | null | 5.7 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24318,"numValue":5.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24319,"numValue":0.62,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24320,"numValue":null,"references":[],"strValue":"yes","ty... | [{"id":7078,"numValue":8.0,"position":123,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3804 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,804 | train | mutant | 1,722 | 48 | 1,932 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124V | I124V | 1 | 1 | 0 | 0 | 124 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,188 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106V | 44.5 | -4.7 | null | null | 70.33 | 1.72 | 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:I106V","type":"_P... | [{"datasets":[],"id":11648,"numValue":44.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11649,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11650,"numValue":70.33,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,805 | train | mutant | 1,722 | 48 | 1,932 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124V | I124V | 1 | 1 | 0 | 0 | 124 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,216 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106V | 51.3 | null | null | null | 73.7 | null | 78 | 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:I106V","type":"_P... | [{"datasets":[],"id":11772,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11773,"numValue":73.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11774,"numValue":78.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11775,"numValue":null,"references":[... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,806 | train | mutant | 1,722 | 48 | 1,932 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124V | I124V | 1 | 1 | 0 | 0 | 124 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,217 | ProTherm | 3 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106V | 49.5 | null | null | null | 70.6 | null | 75.6 | 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:I106V","type":"_P... | [{"datasets":[],"id":11776,"numValue":49.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11777,"numValue":70.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11778,"numValue":75.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11779,"numValue":null,"references":[... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,808 | train | mutant | 1,722 | 48 | 1,932 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124V | I124V | 1 | 1 | 0 | 0 | 124 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,219 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106V | 43.6 | -5.6 | null | null | 59.8 | null | 66.7 | 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":2.7,"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:I106V","type":"_P... | [{"datasets":[],"id":11784,"numValue":43.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11785,"numValue":-5.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11786,"numValue":59.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,809 | train | mutant | 1,722 | 48 | 1,932 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124V | I124V | 1 | 1 | 0 | 0 | 124 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 4,157 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106V | 62.7 | -2.2 | null | null | 109.3 | 1.41 | 113.8 | 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:I106V","type":"_P... | [{"datasets":[],"id":15388,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15389,"numValue":-2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15390,"numValue":109.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,810 | train | mutant | 1,722 | 48 | 1,932 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124V | I124V | 1 | 1 | 0 | 0 | 124 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 6,886 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I106V | null | null | null | 0.72 | null | 1.41 | 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 | 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":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":24339,"numValue":1.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24340,"numValue":0.72,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24341,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,811 | train | mutant | 1,722 | 48 | 1,932 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124V | I124V | 1 | 1 | 0 | 0 | 124 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 7,742 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:I106V | null | null | null | 0.98 | null | 1.72 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":26597,"numValue":1.72,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26598,"numValue":0.98,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26599,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,812 | train | mutant | 1,756 | 48 | 1,969 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124A | I124A | 1 | 1 | 0 | 0 | 124 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,345 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106A | 69.7 | null | null | null | 112.2 | 1.58 | 119.1 | 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":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:I106A","type":"_P... | [{"datasets":[],"id":12324,"numValue":69.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12325,"numValue":112.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12326,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12327,"numValue":119.1,"references":... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,813 | train | mutant | 1,756 | 48 | 1,969 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124A | I124A | 1 | 1 | 0 | 0 | 124 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,346 | ProTherm | 2.96 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106A | 67.4 | null | null | null | 109.1 | 1.17 | 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":2.96,"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:I106A","type":"_... | [{"datasets":[],"id":12329,"numValue":67.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12330,"numValue":109.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12331,"numValue":1.17,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12332,"numValue":114.1,"references":... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3814 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,814 | train | mutant | 1,756 | 48 | 1,969 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124A | I124A | 1 | 1 | 0 | 0 | 124 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,347 | ProTherm | 2.8 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106A | 64.1 | null | null | null | 104.1 | 0.98 | 111 | 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:I106A","type":"_P... | [{"datasets":[],"id":12334,"numValue":64.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12335,"numValue":104.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12336,"numValue":0.98,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12337,"numValue":111.0,"references":... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3816 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,816 | train | mutant | 1,756 | 48 | 1,969 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124A | I124A | 1 | 1 | 0 | 0 | 124 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,349 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106A | 57.7 | null | null | null | 96.4 | 1.15 | 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":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:I106A","type":"_... | [{"datasets":[],"id":12344,"numValue":57.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12345,"numValue":96.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12346,"numValue":1.15,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12347,"numValue":102.2,"references":[... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3817 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,817 | train | mutant | 1,756 | 48 | 1,969 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124A | I124A | 1 | 1 | 0 | 0 | 124 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 3,360 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I106A | 61.9 | -3 | null | null | null | 1.34 | 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:I106A","type":"_P... | [{"datasets":[],"id":12392,"numValue":61.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":12393,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":12394,"numValue":1.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3818 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,818 | train | mutant | 1,756 | 48 | 1,969 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I124A | I124A | 1 | 1 | 0 | 0 | 124 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 124 | A | G | false | false | 4.884364 | 19.35 | 6,907 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I106A | null | null | null | 0.93 | 105.5 | 1.34 | 112.2 | 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":24410,"numValue":105.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24411,"numValue":1.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24412,"numValue":112.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["capriotti_S1615_map.csv","khan_protherm... | [{"id":7079,"numValue":8.0,"position":124,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3819 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,819 | train | mutant | 635 | 48 | 687 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128P | V128P | 1 | 1 | 0 | 0 | 128 | V | P | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,052 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | null | 1LZ1_A:V110P | 70 | 1.2 | null | null | null | 1.57 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110P","type":... | [{"datasets":[],"id":3932,"numValue":70.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3933,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3934,"numValue":1.57,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3820 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,820 | train | mutant | 635 | 48 | 687 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128P | V128P | 1 | 1 | 0 | 0 | 128 | V | P | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,705 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | 68.8 | 1LZ1_A:V110P | null | null | null | -0.5 | 120.3 | 1.57 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":68.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":[],"id":23851,"numValue":120.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":23852,"numValue":1.57,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23853,"numValue":-0.5,"referenc... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3821 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,821 | train | mutant | 635 | 48 | 687 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128P | V128P | 1 | 1 | 0 | 0 | 128 | V | P | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 9,883 | ProTherm | 3 | CD | GdnHCl | glycine-HCl | 40 mM | 25 | 1LZ1_A:V110P | null | null | 12.1 | -2.4 | null | null | null | 3.05 | 6.69 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 658 | ARTICLE | Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization. | 1,991 | 10.1021/bi00105a011 | 1911779 | Biochemistry;30;9882-91 | 4 | Yutani K|Kikuchi M|Herning T|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":33974,"numValue":12.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33975,"numValue":-2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33976,"numValue":6.69,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33977,"numValue":3.05,"references":[],... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3822 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,822 | train | mutant | 680 | 48 | 736 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128G | V128G | 1 | 1 | 0 | 0 | 128 | V | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,144 | ProTherm | 2.6 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110G | 64.6 | null | null | null | 99.9 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110G","type"... | [{"datasets":[],"id":4253,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4254,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4255,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3824 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,824 | train | mutant | 680 | 48 | 736 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128G | V128G | 1 | 1 | 0 | 0 | 128 | V | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,146 | ProTherm | 2.94 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110G | 70.59 | null | null | null | 109.94 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.94,"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:V110G","type... | [{"datasets":[],"id":4259,"numValue":70.59,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4260,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4261,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3825 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,825 | train | mutant | 680 | 48 | 736 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128G | V128G | 1 | 1 | 0 | 0 | 128 | V | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,147 | ProTherm | 3.11 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110G | 73.44 | null | null | null | 114.96 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.11,"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:V110G","type... | [{"datasets":[],"id":4262,"numValue":73.44,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4263,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4264,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3826 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,826 | train | mutant | 680 | 48 | 736 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128G | V128G | 1 | 1 | 0 | 0 | 128 | V | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,148 | ProTherm | 3.3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110G | 76.63 | null | null | null | 121.89 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110G","type"... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":4265,"numValue":76.63,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4266,"numValue":121.89,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4267,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3827 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,827 | train | mutant | 680 | 48 | 736 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128G | V128G | 1 | 1 | 0 | 0 | 128 | V | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,176 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110G | 66.5 | 1.6 | null | null | 99.9 | 1.82 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110G","type"... | [{"datasets":[],"id":4369,"numValue":66.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4370,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4371,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3828 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,828 | train | mutant | 680 | 48 | 736 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128G | V128G | 1 | 1 | 0 | 0 | 128 | V | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,191 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110G | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110G","type"... | [{"datasets":[],"id":4414,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4415,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3829 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,829 | train | mutant | 680 | 48 | 736 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128G | V128G | 1 | 1 | 0 | 0 | 128 | V | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,949 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V110G | null | null | null | -0.48 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24508,"numValue":-0.48,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24509,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3830 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,830 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,149 | ProTherm | 2.53 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110I | 64.89 | null | null | null | 107.07 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.53,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110I","type... | [{"datasets":[],"id":4268,"numValue":64.89,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4269,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4270,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3831 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,831 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,150 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110I | 67.27 | null | null | null | 110.9 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110I","type"... | [{"datasets":[],"id":4271,"numValue":67.27,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4272,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4273,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3832 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,832 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,151 | ProTherm | 2.9 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110I | 70.93 | null | null | null | 117.11 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.9,"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:V110I","type"... | [{"datasets":[],"id":4274,"numValue":70.93,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4275,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4276,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3833 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,833 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,152 | ProTherm | 3.13 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110I | 74.86 | null | null | null | 123.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.13,"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:V110I","type... | [{"datasets":[],"id":4277,"numValue":74.86,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4278,"numValue":123.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4279,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3834 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,834 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,153 | ProTherm | 3.23 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110I | 76.82 | null | null | null | 126.91 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.23,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110I","type... | [{"datasets":[],"id":4280,"numValue":76.82,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4281,"numValue":126.91,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4282,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3835 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,835 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,177 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110I | 67.6 | 2.7 | null | null | 106.84 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110I","type"... | [{"datasets":[],"id":4374,"numValue":67.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4375,"numValue":2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4376,"numValue":106.84,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3836 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,836 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,192 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110I | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110I","type"... | [{"datasets":[],"id":4416,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4417,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3837 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,837 | train | mutant | 681 | 48 | 737 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128I | V128I | 1 | 1 | 0 | 0 | 128 | V | I | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,950 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V110I | null | null | null | -0.86 | 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 | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24510,"numValue":-0.86,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24511,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3838 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,838 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,154 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110L | 61.92 | null | null | null | 105.16 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110L","type"... | [{"datasets":[],"id":4283,"numValue":61.92,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4284,"numValue":105.16,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4285,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3839 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,839 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,155 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110L | 65.02 | null | null | null | 108.03 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"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:V110L","type"... | [{"datasets":[],"id":4286,"numValue":65.02,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4287,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4288,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3840 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,840 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,156 | ProTherm | 2.82 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110L | 67.01 | null | null | null | 111.14 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.82,"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:V110L","type... | [{"datasets":[],"id":4289,"numValue":67.01,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4290,"numValue":111.14,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4291,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3841 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,841 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,157 | ProTherm | 3.03 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110L | 70.53 | null | null | null | 114.96 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.03,"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:V110L","type... | [{"datasets":[],"id":4292,"numValue":70.53,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4293,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4294,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3842 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,842 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,158 | ProTherm | 3.25 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110L | 74.52 | null | null | null | 121.18 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.25,"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:V110L","type... | [{"datasets":[],"id":4295,"numValue":74.52,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4296,"numValue":121.18,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4297,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3843 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,843 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,178 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110L | 65.1 | 0.2 | null | null | 108.51 | 1.29 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110L","type"... | [{"datasets":[],"id":4379,"numValue":65.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4380,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4381,"numValue":108.51,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3844 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,844 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,193 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110L | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110L","type"... | [{"datasets":[],"id":4418,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4419,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3845 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,845 | train | mutant | 682 | 48 | 738 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128L | V128L | 1 | 1 | 0 | 0 | 128 | V | L | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,951 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V110L | null | null | null | -0.07 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24512,"numValue":-0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24513,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3846 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,846 | train | mutant | 683 | 48 | 739 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128M | V128M | 1 | 1 | 0 | 0 | 128 | V | M | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,159 | ProTherm | 2.48 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110M | 62.8 | null | null | null | 108.99 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.48,"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:V110M","type... | [{"datasets":[],"id":4298,"numValue":62.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4299,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4300,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3847 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,847 | train | mutant | 683 | 48 | 739 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128M | V128M | 1 | 1 | 0 | 0 | 128 | V | M | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,160 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110M | 66.34 | null | null | null | 114.01 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":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:V110M","type"... | [{"datasets":[],"id":4301,"numValue":66.34,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4302,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4303,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3849 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,849 | train | mutant | 683 | 48 | 739 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128M | V128M | 1 | 1 | 0 | 0 | 128 | V | M | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,162 | ProTherm | 3.06 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110M | 72.79 | null | null | null | 123.09 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.06,"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:V110M","type... | [{"datasets":[],"id":4307,"numValue":72.79,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4308,"numValue":123.09,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4309,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3850 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,850 | train | mutant | 683 | 48 | 739 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128M | V128M | 1 | 1 | 0 | 0 | 128 | V | M | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,179 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110M | 66.5 | 1.6 | null | null | 111.85 | 1.41 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110M","type"... | [{"datasets":[],"id":4384,"numValue":66.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4385,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4386,"numValue":111.85,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3851 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,851 | train | mutant | 683 | 48 | 739 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128M | V128M | 1 | 1 | 0 | 0 | 128 | V | M | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,194 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110M | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110M","type"... | [{"datasets":[],"id":4420,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4421,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3853 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,853 | train | mutant | 684 | 48 | 740 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128F | V128F | 1 | 1 | 0 | 0 | 128 | V | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,163 | ProTherm | 2.72 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110F | 65.11 | null | null | null | 101.1 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.72,"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:V110F","type... | [{"datasets":[],"id":4310,"numValue":65.11,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4311,"numValue":101.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4312,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3854 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,854 | train | mutant | 684 | 48 | 740 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128F | V128F | 1 | 1 | 0 | 0 | 128 | V | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,164 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110F | 66.29 | null | null | null | 103.01 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110F","type"... | [{"datasets":[],"id":4313,"numValue":66.29,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4314,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4315,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3855 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,855 | train | mutant | 684 | 48 | 740 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128F | V128F | 1 | 1 | 0 | 0 | 128 | V | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,165 | ProTherm | 3.04 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110F | 70.49 | null | null | null | 110.18 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":3.04,"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:V110F","type... | [{"datasets":[],"id":4316,"numValue":70.49,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4317,"numValue":110.18,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4318,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3856 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,856 | train | mutant | 684 | 48 | 740 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128F | V128F | 1 | 1 | 0 | 0 | 128 | V | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,180 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110F | 64.7 | -0.2 | null | null | 100.62 | 1.7 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110F","type"... | [{"datasets":[],"id":4389,"numValue":64.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":4390,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4391,"numValue":100.62,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"i... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3857 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,857 | train | mutant | 684 | 48 | 740 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128F | V128F | 1 | 1 | 0 | 0 | 128 | V | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,195 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:V110F | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110F","type"... | [{"datasets":[],"id":4422,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4423,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3858 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,858 | train | mutant | 684 | 48 | 740 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128F | V128F | 1 | 1 | 0 | 0 | 128 | V | F | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,953 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:V110F | null | null | null | 0.05 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 115 | ARTICLE | Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions. | 2,000 | 10.1021/bi0015717 | 11087397 | Biochemistry;39;14448-56 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24516,"numValue":0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24517,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3859 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,859 | train | mutant | 728 | 48 | 794 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128Y | V128Y | 1 | 1 | 0 | 0 | 128 | V | Y | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,299 | ProTherm | 2.66 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110Y | 63.3 | null | null | null | 106.12 | null | 105.16 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.66,"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:V110Y","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4788,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4789,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4790,"numValue":105.16,"references":[],"strValue":null,"type":"DH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3861 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,861 | train | mutant | 728 | 48 | 794 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128Y | V128Y | 1 | 1 | 0 | 0 | 128 | V | Y | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,301 | ProTherm | 2.98 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110Y | 69.3 | null | null | null | 114.01 | null | 114.01 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.98,"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:V110Y","type":"_... | [{"datasets":[],"id":4796,"numValue":69.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4797,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4798,"numValue":114.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4799,"numValue":null,"references":[... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3862 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,862 | train | mutant | 728 | 48 | 794 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128Y | V128Y | 1 | 1 | 0 | 0 | 128 | V | Y | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,302 | ProTherm | 3.18 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110Y | 72.2 | null | null | null | 119.98 | null | 121.18 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.18,"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:V110Y","type":"_... | [{"datasets":[],"id":4800,"numValue":72.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4801,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4802,"numValue":121.18,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4803,"numValue":null,"references":[... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3863 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,863 | train | mutant | 728 | 48 | 794 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128Y | V128Y | 1 | 1 | 0 | 0 | 128 | V | Y | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,303 | ProTherm | 3.38 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110Y | 75.4 | null | null | null | 125 | null | 125 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.38,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110Y","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4804,"numValue":75.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4805,"numValue":125.0,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4806,"numValue":125.0,"references":[],"strValue":null,"type":"DHVH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3864 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,864 | train | mutant | 728 | 48 | 794 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128Y | V128Y | 1 | 1 | 0 | 0 | 128 | V | Y | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,327 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110Y | 64.4 | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110Y","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4892,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4893,"numValue":-0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4894,"numValue":null,"re... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3865 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,865 | train | mutant | 728 | 48 | 794 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128Y | V128Y | 1 | 1 | 0 | 0 | 128 | V | Y | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,964 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V110Y | null | null | null | 0.14 | 107.79 | null | null | null | null | null | null | null | null | null | null | null | Unknown | DH|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24558,"numValue":107.79,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24559,"numValue":0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24560,"numValue":null,"references":[],"strValue":"Unknow... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3866 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,866 | train | mutant | 729 | 48 | 795 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128D | V128D | 1 | 1 | 0 | 0 | 128 | V | D | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,304 | ProTherm | 2.63 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110D | 63.9 | null | null | null | 90.34 | null | 108.03 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.63,"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:V110D","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4808,"numValue":63.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4809,"numValue":90.34,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4810,"numValue":108.03,"references":[],"strValue":null,"type":"DHV... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3867 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,867 | train | mutant | 729 | 48 | 795 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128D | V128D | 1 | 1 | 0 | 0 | 128 | V | D | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,305 | ProTherm | 2.84 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110D | 67.9 | null | null | null | 96.8 | null | 112.09 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.84,"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:V110D","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4812,"numValue":67.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4813,"numValue":96.8,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4814,"numValue":112.09,"references":[],"strValue":null,"type":"DHVH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3868 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,868 | train | mutant | 729 | 48 | 795 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128D | V128D | 1 | 1 | 0 | 0 | 128 | V | D | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,306 | ProTherm | 3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110D | 70.4 | null | null | null | 103.01 | null | 119.98 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110D","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4816,"numValue":70.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4817,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4818,"numValue":119.98,"references":[],"strValue":null,"type":"DH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3870 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,870 | train | mutant | 729 | 48 | 795 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128D | V128D | 1 | 1 | 0 | 0 | 128 | V | D | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,308 | ProTherm | 3.34 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110D | 75.5 | null | null | null | 108.03 | null | 125 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":3.34,"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:V110D","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4824,"numValue":75.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4825,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4826,"numValue":125.0,"references":[],"strValue":null,"type":"DHV... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3871 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,871 | train | mutant | 729 | 48 | 795 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128D | V128D | 1 | 1 | 0 | 0 | 128 | V | D | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,328 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110D | 65.4 | 0.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110D","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4895,"numValue":65.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4896,"numValue":0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4897,"numValue":null,"ref... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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