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:3873 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,873 | train | mutant | 730 | 48 | 796 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128N | V128N | 1 | 1 | 0 | 0 | 128 | V | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,309 | ProTherm | 2.64 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110N | 64 | null | null | null | 108.03 | null | 108.99 | 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":2.64,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110N","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4828,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4829,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4830,"numValue":108.99,"references":[],"strValue":null,"type":"DH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3874 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,874 | train | mutant | 730 | 48 | 796 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128N | V128N | 1 | 1 | 0 | 0 | 128 | V | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,310 | ProTherm | 2.83 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110N | 67.2 | null | null | null | 113.05 | null | 114.96 | null | null | null | null | null | null | null | null | null | Unknown | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 131 | ARTICLE | Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability. | 2,002 | 10.1074/jbc.M110728200 | 11927576 | J Biol Chem;277;21792-800 | 4 | Funahashi Jun|Takano Kazufumi|Yamagata Yuriko|Yutani Katsuhide | [{"numValue":2.83,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110N","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4832,"numValue":67.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4833,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4834,"numValue":114.96,"references":[],"strValue":null,"type":"DH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3875 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,875 | train | mutant | 730 | 48 | 796 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128N | V128N | 1 | 1 | 0 | 0 | 128 | V | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,311 | ProTherm | 3.04 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110N | 70.6 | null | null | null | 118.07 | null | 118.07 | 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":3.04,"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:V110N","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4836,"numValue":70.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4837,"numValue":118.07,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4838,"numValue":118.07,"references":[],"strValue":null,"type":"DH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3876 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,876 | train | mutant | 730 | 48 | 796 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128N | V128N | 1 | 1 | 0 | 0 | 128 | V | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,312 | ProTherm | 3.13 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110N | 71.7 | null | null | null | 119.98 | null | 121.89 | 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":3.13,"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:V110N","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4840,"numValue":71.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4841,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4842,"numValue":121.89,"references":[],"strValue":null,"type":"DH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3877 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,877 | train | mutant | 730 | 48 | 796 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128N | V128N | 1 | 1 | 0 | 0 | 128 | V | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,329 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110N | 65.1 | 0.2 | 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:V110N","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4898,"numValue":65.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4899,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4900,"numValue":null,"ref... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3880 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,880 | train | mutant | 731 | 48 | 797 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128R | V128R | 1 | 1 | 0 | 0 | 128 | V | R | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,314 | ProTherm | 2.8 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110R | 69.3 | null | null | null | 108.03 | null | 110.18 | 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":2.8,"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:V110R","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4848,"numValue":69.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4849,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":4850,"numValue":110.18,"references":[],"strValue":null,"type":"DH... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3881 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,881 | train | mutant | 731 | 48 | 797 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128R | V128R | 1 | 1 | 0 | 0 | 128 | V | R | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,315 | ProTherm | 3.01 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110R | 72.8 | null | null | null | 114.01 | null | 116.16 | 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":3.01,"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:V110R","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4852,"numValue":72.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4853,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4854,"numValue":116.16,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3882 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,882 | train | mutant | 731 | 48 | 797 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128R | V128R | 1 | 1 | 0 | 0 | 128 | V | R | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,316 | ProTherm | 3.15 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110R | 75 | null | null | null | 117.11 | null | 119.98 | 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":3.15,"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:V110R","type":"_... | [{"datasets":[],"id":4856,"numValue":75.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4857,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":4858,"numValue":119.98,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":4859,"numValue":null,"references":[... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3883 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,883 | train | mutant | 731 | 48 | 797 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128R | V128R | 1 | 1 | 0 | 0 | 128 | V | R | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 1,330 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:V110R | 67.8 | 2.9 | 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:V110R","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":4901,"numValue":67.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":4902,"numValue":2.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":4903,"numValue":null,"ref... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3884 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,884 | train | mutant | 731 | 48 | 797 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128R | V128R | 1 | 1 | 0 | 0 | 128 | V | R | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,967 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:V110R | null | null | null | -0.88 | 100.62 | 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":24567,"numValue":100.62,"references":[],"strValue":null,"type":"DH"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24568,"numValue":-0.88,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24569,"numValue":null,"references":[],"strValue":"Unkno... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3885 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,885 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 3,194 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V110A | 49.5 | 0.3 | null | null | 80.86 | 1.51 | 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:V110A","type":"_P... | [{"datasets":[],"id":11678,"numValue":49.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11679,"numValue":0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11680,"numValue":80.86,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3886 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,886 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 3,243 | ProTherm | 3.13 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V110A | 57.2 | null | null | null | 93.3 | null | 93.3 | 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":3.13,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110A","type":"_... | [{"datasets":[],"id":11882,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11883,"numValue":93.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11884,"numValue":93.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11885,"numValue":null,"references":[... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3887 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,887 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 3,244 | ProTherm | 3 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V110A | 55 | null | null | null | 89 | null | 93.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V110A","type":"_P... | [{"datasets":[],"id":11886,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11887,"numValue":89.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11888,"numValue":93.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11889,"numValue":null,"references":[... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3888 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,888 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 3,245 | ProTherm | 2.87 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V110A | 52.5 | null | null | null | 85.9 | null | 87.6 | 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":2.87,"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:V110A","type":"_... | [{"datasets":[],"id":11890,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11891,"numValue":85.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11892,"numValue":87.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11893,"numValue":null,"references":[... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3890 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,890 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 3,247 | ProTherm | 2.55 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V110A | 46.8 | null | null | null | 76.8 | 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":2.55,"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:V110A","type":"_... | [{"datasets":[],"id":11898,"numValue":46.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11899,"numValue":76.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11900,"numValue":78.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11901,"numValue":null,"references":[... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3891 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,891 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 4,170 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V110A | 66.4 | 1.5 | null | null | 115.8 | 1.24 | 121.88 | 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:V110A","type":"_P... | [{"datasets":[],"id":15454,"numValue":66.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15455,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15456,"numValue":115.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3892 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,892 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 6,893 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V110A | null | null | null | -0.53 | null | 1.24 | 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":24360,"numValue":1.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":24361,"numValue":-0.53,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24362,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3893 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,893 | train | mutant | 1,728 | 48 | 1,938 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V128A | V128A | 1 | 1 | 0 | 0 | 128 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 128 | A | H | true | true | 85.09966 | 29.572857 | 7,748 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V110A | null | null | null | -0.07 | null | 1.51 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 294 | ARTICLE | A general rule for the relationship between hydrophobic effect and conformational stability of a protein: stability and structure of a series of hydrophobic mutants of human lysozyme. | 1,998 | 10.1006/jmbi.1998.1906 | 9677301 | J Mol Biol;280;749-61 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":49.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":26615,"numValue":1.51,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26616,"numValue":-0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26617,"numValue":null,"references":[],"strValue":"yes","type":"RE... | [{"id":7083,"numValue":5.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3894 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,894 | train | mutant | 195 | 48 | 223 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136A | N136A | 1 | 1 | 0 | 0 | 136 | N | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 356 | ProTherm | 2.51 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118A | 62.1 | null | null | null | 99.9 | null | 106.12 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | M47andM8_S2760.csv|SVM-WIN31_SVM-3D12_S499.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.51,"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:N118A","type":"_... | [{"datasets":["M47andM8_S2760.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":1458,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1459,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1460,"numValue":106.12,"references":[],"strValue":null,"t... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3895 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,895 | train | mutant | 195 | 48 | 223 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136A | N136A | 1 | 1 | 0 | 0 | 136 | N | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 357 | ProTherm | 2.74 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118A | 66.2 | null | null | null | 107.07 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.74,"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:N118A","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1462,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1463,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1464,"numValue":112.09,"references":[],"strValue":null,"type":"DH... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3896 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,896 | train | mutant | 195 | 48 | 223 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136A | N136A | 1 | 1 | 0 | 0 | 136 | N | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 358 | ProTherm | 2.87 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118A | 68.6 | null | null | null | 108.99 | null | 117.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.87,"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:N118A","type":"_... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1466,"numValue":68.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":1467,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1468,"numValue":117.11,"references":[],"strValue":null,"type":"DH... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3897 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,897 | train | mutant | 195 | 48 | 223 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136A | N136A | 1 | 1 | 0 | 0 | 136 | N | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 359 | ProTherm | 3.02 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118A | 70.9 | null | null | null | 110.9 | null | 118.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.02,"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:N118A","type":"_... | [{"datasets":[],"id":1470,"numValue":70.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1471,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1472,"numValue":118.07,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1473,"numValue":null,"references":[]... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3898 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,898 | train | mutant | 195 | 48 | 223 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136A | N136A | 1 | 1 | 0 | 0 | 136 | N | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 370 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118A | 65.5 | 0.6 | null | null | 104.21 | 1.24 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:N118A","type":"_P... | [{"datasets":[],"id":1521,"numValue":65.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1522,"numValue":0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1523,"numValue":104.21,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3899 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,899 | train | mutant | 195 | 48 | 223 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136A | N136A | 1 | 1 | 0 | 0 | 136 | N | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 6,870 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:N118A | null | null | null | -0.19 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24293,"numValue":-0.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24294,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3900 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,900 | train | mutant | 196 | 48 | 224 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136G | N136G | 1 | 1 | 0 | 0 | 136 | N | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 360 | ProTherm | 2.74 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118G | 65.7 | null | null | null | 103.01 | null | 109.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.74,"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:N118G","type":"_... | [{"datasets":[],"id":1474,"numValue":65.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1475,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1476,"numValue":109.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1477,"numValue":null,"references":[... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3901 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,901 | train | mutant | 196 | 48 | 224 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136G | N136G | 1 | 1 | 0 | 0 | 136 | N | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 361 | ProTherm | 2.95 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118G | 69.3 | null | null | null | 107.07 | null | 114.96 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.95,"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:N118G","type":"_... | [{"datasets":[],"id":1478,"numValue":69.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1479,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1480,"numValue":114.96,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1481,"numValue":null,"references":[... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3902 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,902 | train | mutant | 196 | 48 | 224 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136G | N136G | 1 | 1 | 0 | 0 | 136 | N | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 362 | ProTherm | 3.1 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118G | 71.6 | null | null | null | 113.05 | null | 119.02 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:N118G","type":"_P... | [{"datasets":[],"id":1482,"numValue":71.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1483,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1484,"numValue":119.02,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1485,"numValue":null,"references":[... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3903 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,903 | train | mutant | 196 | 48 | 224 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136G | N136G | 1 | 1 | 0 | 0 | 136 | N | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 371 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:N118G | 65.1 | 0.2 | null | null | 101.1 | 1.65 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:N118G","type":"_P... | [{"datasets":[],"id":1526,"numValue":65.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1527,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1528,"numValue":101.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id"... | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3904 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,904 | train | mutant | 196 | 48 | 224 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | N136G | N136G | 1 | 1 | 0 | 0 | 136 | N | G | 5 | CONSERVATION | 1LZ1 | 405 | null | 136 | A | T | false | false | 153.216984 | 52.847501 | 6,871 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:N118G | null | null | null | -0.05 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 38 | ARTICLE | Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme. | 2,001 | 10.1002/prot.1088 | 11455596 | Proteins;44;233-43 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24295,"numValue":-0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24296,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7091,"numValue":5.0,"position":136,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3905 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,905 | train | mutant | 49 | 48 | 54 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D138N | D138N | 1 | 1 | 0 | 0 | 138 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 138 | A | L | false | false | 93.197133 | 56.297501 | 49 | ProTherm | 2.2 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | 1LZ1_A:D120N | 57.8 | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|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:D12... | [{"datasets":[],"id":166,"numValue":57.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":167,"numValue":0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":168,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7093,"numValue":5.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3906 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,906 | train | mutant | 49 | 48 | 54 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D138N | D138N | 1 | 1 | 0 | 0 | 138 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 138 | A | L | false | false | 93.197133 | 56.297501 | 55 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | null | 1LZ1_A:D120N | 78.3 | -1.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"0.02 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:D120N","ty... | [{"datasets":[],"id":184,"numValue":78.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":185,"numValue":-1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":186,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7093,"numValue":5.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3907 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,907 | train | mutant | 49 | 48 | 54 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D138N | D138N | 1 | 1 | 0 | 0 | 138 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 138 | A | L | false | false | 93.197133 | 56.297501 | 59 | ProTherm | 2.3 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | KCl | 0.2 M | 1LZ1_A:D120N | 56.9 | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|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":196,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":197,"numValue":0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":198,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7093,"numValue":5.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3908 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,908 | train | mutant | 49 | 48 | 54 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D138N | D138N | 1 | 1 | 0 | 0 | 138 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 138 | A | L | false | false | 93.197133 | 56.297501 | 63 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | null | KCl | 0.2 M | 1LZ1_A:D120N | 77.8 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 6 | ARTICLE | Contribution of salt bridges near the surface of a protein to the conformational stability. | 2,000 | 10.1021/bi000849s | 11015217 | Biochemistry;39;12375-81 | 4 | Takano K|Tsuchimori K|Yamagata Y|Yutani K | [{"numValue":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":208,"numValue":77.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":209,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":210,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7093,"numValue":5.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3909 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,909 | train | mutant | 49 | 48 | 54 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D138N | D138N | 1 | 1 | 0 | 0 | 138 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 138 | A | L | false | false | 93.197133 | 56.297501 | 6,842 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | 65 | 1LZ1_A:D120N | 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":24224,"numValue":4.76,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":24225,"numValue":0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24226,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7093,"numValue":5.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3910 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,910 | train | mutant | 49 | 48 | 54 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D138N | D138N | 1 | 1 | 0 | 0 | 138 | D | N | 5 | CONSERVATION | 1LZ1 | 405 | null | 138 | A | L | false | false | 93.197133 | 56.297501 | 6,846 | ProTherm | 4.5 | DSC | Thermal | sodium acetate | 0.02 M | 65 | KCl | 0.2 M | 1LZ1_A:D120N | null | null | 4.13 | -0.05 | 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":24236,"numValue":4.13,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24237,"numValue":-0.05,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24238,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":7093,"numValue":5.0,"position":138,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:3911 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,911 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 3,195 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V121A | 39.9 | -9.3 | null | null | 65.31 | 1.37 | 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:V121A","type":"_P... | [{"datasets":[],"id":11683,"numValue":39.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11684,"numValue":-9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11685,"numValue":65.31,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3912 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,912 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 3,248 | ProTherm | 3.14 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V121A | 50.1 | -7.7 | null | null | 67.2 | null | 72.5 | 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":3.14,"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:V121A","type":"_... | [{"datasets":[],"id":11902,"numValue":50.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11903,"numValue":-7.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11904,"numValue":67.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3913 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,913 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 3,249 | ProTherm | 3 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V121A | 47 | null | null | null | 61.5 | null | 67.5 | 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:V121A","type":"_P... | [{"datasets":[],"id":11907,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11908,"numValue":61.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11909,"numValue":67.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11910,"numValue":null,"references":[... | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3914 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,914 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 3,250 | ProTherm | 2.86 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V121A | 43.6 | null | null | null | 57.9 | null | 62.7 | 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":2.86,"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:V121A","type":"_... | [{"datasets":[],"id":11911,"numValue":43.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11912,"numValue":57.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11913,"numValue":62.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11914,"numValue":null,"references":[... | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3915 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,915 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 3,251 | ProTherm | 2.72 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V121A | 40.3 | null | null | null | 53.6 | null | 56.9 | 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:V121A","type":"_... | [{"datasets":[],"id":11915,"numValue":40.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11916,"numValue":53.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11917,"numValue":56.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11918,"numValue":null,"references":[... | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3916 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,916 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 4,171 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V121A | 60.4 | -4.5 | null | null | 110 | 1.53 | 112.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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:V121A","type":"_P... | [{"datasets":[],"id":15460,"numValue":60.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15461,"numValue":-4.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15462,"numValue":110.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3917 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,917 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 6,894 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V121A | null | null | null | 1.44 | null | 1.53 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":24363,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24364,"numValue":1.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24365,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3918 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,918 | train | mutant | 1,729 | 48 | 1,939 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V139A | V139A | 1 | 1 | 0 | 0 | 139 | V | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 139 | A | L | false | false | 15.867836 | 24.542857 | 7,749 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V121A | null | null | null | 1.75 | null | 1.37 | 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":26618,"numValue":1.37,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26619,"numValue":1.75,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26620,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7094,"numValue":5.0,"position":139,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3919 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,919 | train | mutant | 1,737 | 48 | 1,947 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y142F | Y142F | 1 | 1 | 0 | 0 | 142 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 142 | A | G | false | false | 19.791252 | 22.901667 | 3,267 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y124F | 63.8 | -1.1 | null | null | 114.1 | 1.46 | 118.9 | 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 | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y124F","type":"_P... | [{"datasets":[],"id":11990,"numValue":63.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11991,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11992,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7097,"numValue":6.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3920 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,920 | train | mutant | 1,737 | 48 | 1,947 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y142F | Y142F | 1 | 1 | 0 | 0 | 142 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 142 | A | G | false | false | 19.791252 | 22.901667 | 3,290 | ProTherm | 3.06 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y124F | 69.7 | null | null | null | 121.1 | 1.82 | 125.12 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":3.06,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y124F","type":"_... | [{"datasets":[],"id":12106,"numValue":69.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12107,"numValue":121.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12108,"numValue":1.82,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12109,"numValue":125.12,"references"... | [{"id":7097,"numValue":6.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3921 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,921 | train | mutant | 1,737 | 48 | 1,947 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y142F | Y142F | 1 | 1 | 0 | 0 | 142 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 142 | A | G | false | false | 19.791252 | 22.901667 | 3,291 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y124F | 64 | null | null | null | 113.2 | 1.53 | 118.18 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.7,"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:Y124F","type":"_P... | [{"datasets":[],"id":12111,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12112,"numValue":113.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12113,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12114,"numValue":118.18,"references"... | [{"id":7097,"numValue":6.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3922 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,922 | train | mutant | 1,737 | 48 | 1,947 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y142F | Y142F | 1 | 1 | 0 | 0 | 142 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 142 | A | G | false | false | 19.791252 | 22.901667 | 3,292 | ProTherm | 2.68 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y124F | 63.4 | null | null | null | 112.2 | 1.08 | 116.03 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.68,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y124F","type":"_... | [{"datasets":[],"id":12116,"numValue":63.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12117,"numValue":112.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12118,"numValue":1.08,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12119,"numValue":116.03,"references"... | [{"id":7097,"numValue":6.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3923 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,923 | train | mutant | 1,737 | 48 | 1,947 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y142F | Y142F | 1 | 1 | 0 | 0 | 142 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 142 | A | G | false | false | 19.791252 | 22.901667 | 3,293 | ProTherm | 2.53 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y124F | 60.8 | null | null | null | 108.1 | 1.48 | 112.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.53,"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:Y124F","type":"_... | [{"datasets":[],"id":12121,"numValue":60.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12122,"numValue":108.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12123,"numValue":1.48,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12124,"numValue":112.2,"references":... | [{"id":7097,"numValue":6.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3924 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,924 | train | mutant | 1,737 | 48 | 1,947 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y142F | Y142F | 1 | 1 | 0 | 0 | 142 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 142 | A | G | false | false | 19.791252 | 22.901667 | 6,902 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:Y124F | null | null | null | 0.36 | null | 1.46 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24387,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24388,"numValue":0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24389,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7097,"numValue":6.0,"position":142,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3925 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,925 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 3,196 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V125A | 42.2 | -7 | null | null | 77.99 | 1.56 | 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:V125A","type":"_P... | [{"datasets":[],"id":11688,"numValue":42.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11689,"numValue":-7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11690,"numValue":77.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3926 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,926 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 3,252 | ProTherm | 3.17 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V125A | 50.8 | null | null | null | 81.1 | null | 82.8 | 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":3.17,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V125A","type":"_... | [{"datasets":[],"id":11919,"numValue":50.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11920,"numValue":81.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11921,"numValue":82.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11922,"numValue":null,"references":[... | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3927 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,927 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 3,253 | ProTherm | 3.02 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V125A | 47.9 | null | null | null | 76.3 | 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":3.02,"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:V125A","type":"_... | [{"datasets":[],"id":11923,"numValue":47.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11924,"numValue":76.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11925,"numValue":78.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11926,"numValue":null,"references":[... | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3928 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,928 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 3,254 | ProTherm | 2.87 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V125A | 45.9 | null | null | null | 72.2 | null | 76.3 | 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":2.87,"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:V125A","type":"_... | [{"datasets":[],"id":11927,"numValue":45.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11928,"numValue":72.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11929,"numValue":76.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11930,"numValue":null,"references":[... | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3929 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,929 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 3,255 | ProTherm | 2.72 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V125A | 42.8 | 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":2.72,"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:V125A","type":"_... | [{"datasets":[],"id":11931,"numValue":42.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11932,"numValue":67.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11933,"numValue":70.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11934,"numValue":null,"references":[... | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3931 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,931 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 4,172 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V125A | 60.9 | -4 | null | null | 112.9 | 1.29 | 116.4 | 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:V125A","type":"_P... | [{"datasets":[],"id":15466,"numValue":60.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15467,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15468,"numValue":112.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3932 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,932 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 6,895 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V125A | null | null | null | 1.32 | null | 1.29 | 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":24366,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24367,"numValue":1.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24368,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3933 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,933 | train | mutant | 1,730 | 48 | 1,940 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V143A | V143A | 1 | 1 | 0 | 0 | 143 | V | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 143 | A | T | false | false | 28.315593 | 20.082857 | 7,750 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V125A | null | null | null | 1.6 | null | 1.56 | 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":26621,"numValue":1.56,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26622,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26623,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7098,"numValue":4.0,"position":143,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3934 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,934 | train | mutant | 295 | 48 | 327 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G145A | G145A | 1 | 1 | 0 | 0 | 145 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 145 | A | T | false | false | 79.83054 | 23.59 | 523 | ProTherm | 2.2 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G127A | 54.6 | null | null | null | 94.17 | 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":2.2,"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:G127A","type":"_P... | [{"datasets":[],"id":2088,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2089,"numValue":94.17,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2090,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7100,"numValue":5.0,"position":145,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3935 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,935 | train | mutant | 295 | 48 | 327 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G145A | G145A | 1 | 1 | 0 | 0 | 145 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 145 | A | T | false | false | 79.83054 | 23.59 | 524 | ProTherm | 2.6 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G127A | 61.6 | null | null | null | 103.97 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G127A","type":"_P... | [{"datasets":[],"id":2091,"numValue":61.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2092,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2093,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7100,"numValue":5.0,"position":145,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3936 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,936 | train | mutant | 295 | 48 | 327 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G145A | G145A | 1 | 1 | 0 | 0 | 145 | G | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 145 | A | T | false | false | 79.83054 | 23.59 | 525 | ProTherm | 3.16 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G127A | 71.1 | null | null | null | 118.07 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.16,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G127A","type":"_... | [{"datasets":[],"id":2094,"numValue":71.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S2760.csv"],"id":2095,"numValue":118.07,"references":[],"strValue":null,"type":"DH"},{"datasets":["M47andM8_S2760.csv"],"id":2096,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7100,"numValue":5.0,"position":145,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3939 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,939 | train | mutant | 296 | 48 | 328 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G147A | G147A | 1 | 1 | 0 | 0 | 147 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 147 | A | L | false | false | 76.602844 | 32.427499 | 526 | ProTherm | 2.67 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G129A | 64.9 | null | null | null | 99.67 | 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":2.67,"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:G129A","type":"_... | [{"datasets":[],"id":2097,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2098,"numValue":99.67,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2099,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7102,"numValue":4.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3940 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,940 | train | mutant | 296 | 48 | 328 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G147A | G147A | 1 | 1 | 0 | 0 | 147 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 147 | A | L | false | false | 76.602844 | 32.427499 | 527 | ProTherm | 2.79 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G129A | 67.1 | null | null | null | 102.06 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.79,"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:G129A","type":"_... | [{"datasets":[],"id":2100,"numValue":67.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2101,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":["M47andM8_S2760.csv"],"id":2102,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7102,"numValue":4.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3941 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,941 | train | mutant | 296 | 48 | 328 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G147A | G147A | 1 | 1 | 0 | 0 | 147 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 147 | A | L | false | false | 76.602844 | 32.427499 | 528 | ProTherm | 2.8 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G129A | 67.2 | null | null | null | 103.01 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.8,"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:G129A","type":"_P... | [{"datasets":[],"id":2103,"numValue":67.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2104,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2105,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7102,"numValue":4.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3942 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,942 | train | mutant | 296 | 48 | 328 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G147A | G147A | 1 | 1 | 0 | 0 | 147 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 147 | A | L | false | false | 76.602844 | 32.427499 | 538 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G129A | 65.4 | 0.5 | null | null | 99.67 | 1.29 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G129A","type":"_P... | [{"datasets":[],"id":2148,"numValue":65.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2149,"numValue":0.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2150,"numValue":99.67,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2151,"numValue":1.29,"references":[],"st... | [{"id":7102,"numValue":4.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3943 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,943 | train | mutant | 296 | 48 | 328 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G147A | G147A | 1 | 1 | 0 | 0 | 147 | G | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 147 | A | L | false | false | 76.602844 | 32.427499 | 6,881 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:G129A | null | null | null | -0.14 | null | 1.29 | 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":24324,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24325,"numValue":-0.14,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24326,"numValue":null,"references":[],"strValue":"yes","... | [{"id":7102,"numValue":4.0,"position":147,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3944 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,944 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 3,197 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V130A | 44.4 | -4.8 | null | null | 78.23 | 1.87 | 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:V130A","type":"_P... | [{"datasets":[],"id":11693,"numValue":44.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11694,"numValue":-4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11695,"numValue":78.23,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3945 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,945 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 3,257 | ProTherm | 3.09 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V130A | 52.5 | null | null | null | 84.2 | null | 90.2 | 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":3.09,"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:V130A","type":"_... | [{"datasets":[],"id":11940,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11941,"numValue":84.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11942,"numValue":90.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11943,"numValue":null,"references":[... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3946 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,946 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 3,258 | ProTherm | 2.97 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V130A | 49.9 | null | null | null | 80.1 | null | 86.1 | 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":2.97,"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:V130A","type":"_... | [{"datasets":[],"id":11944,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11945,"numValue":80.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11946,"numValue":86.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11947,"numValue":null,"references":[... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3947 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,947 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 3,259 | ProTherm | 2.82 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V130A | 47 | null | null | null | 73 | 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":2.82,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:V130A","type":"_... | [{"datasets":[],"id":11948,"numValue":47.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11949,"numValue":73.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11950,"numValue":79.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11951,"numValue":null,"references":[... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3948 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,948 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 3,260 | ProTherm | 2.69 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V130A | 43.8 | null | null | null | 69.9 | null | 73 | 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":2.69,"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:V130A","type":"_... | [{"datasets":[],"id":11952,"numValue":43.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11953,"numValue":69.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11954,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11955,"numValue":null,"references":[... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3949 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,949 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 3,261 | ProTherm | 2.5 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V130A | 40.4 | null | null | null | 61 | null | 67.7 | 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":2.5,"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:V130A","type":"_P... | [{"datasets":[],"id":11956,"numValue":40.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11957,"numValue":61.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11958,"numValue":67.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11959,"numValue":null,"references":[... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3950 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,950 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 4,173 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:V130A | 62.3 | -2.6 | null | null | 111 | 1.51 | 119.4 | 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:V130A","type":"_P... | [{"datasets":[],"id":15472,"numValue":62.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15473,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15474,"numValue":111.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3951 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,951 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 6,896 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:V130A | null | null | null | 0.84 | null | 1.51 | 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":24369,"numValue":1.51,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24370,"numValue":0.84,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24371,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3952 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,952 | train | mutant | 1,731 | 48 | 1,941 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | V148A | V148A | 1 | 1 | 0 | 0 | 148 | V | A | 6 | CONSERVATION | 1LZ1 | 405 | null | 148 | A | L | false | false | 74.110045 | 41.8225 | 7,751 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:V130A | null | null | null | 1.12 | null | 1.87 | 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":26624,"numValue":1.87,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26625,"numValue":1.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26626,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7103,"numValue":6.0,"position":148,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3953 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,953 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,439 | ProTherm | 3.8 | NMR | Thermal | sodium acetate | 240 mM | null | 74.8 | null | null | null | null | null | 93.69 | null | null | null | null | null | null | null | null | null | yes | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1002 | ARTICLE | Hydrogen exchange in native and denatured states of hen egg-white lysozyme. | 1,992 | 10.1002/prot.340140210 | 1409571 | Proteins;14;237-48 | 5 | Buck M|Dobson C M|Radford S E|Topping K D|Evans P A | [{"numValue":3.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"240 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64369,"numValue":74.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64370,"numValue":93.69,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":64371,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:3954 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,954 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,471 | ProTherm | 7 | CD | Thermal | phosphate | 66 mM | null | 74.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 916 | ARTICLE | Role of the minor energetic determinants of chicken egg white lysozyme (HEWL) to the stability of the HEWL.antibody scFv-10 complex. | 2,000 | 10813830 | Proteins;40;49-57 | 2 | Rajpal A|Kirsch J F | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"66 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":64465,"numValue":74.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64466,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:3955 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,955 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,472 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 65.6 | null | null | null | 114.24 | 1.58 | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 7 | ARTICLE | Relationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine. | 2,000 | 10.1093/protein/13.10.691 | 11112507 | Protein Eng;13;691-5 | 4 | Masumoto K|Ueda T|Motoshima H|Imoto T | [{"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"}] | [{"datasets":[],"id":64467,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":64468,"numValue":114.24,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":64469,"numValue":1.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":64470,"numValue":null,"references":... | |||||||||||||||||||||||||
fireprotdb:3956 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,956 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,794 | ProTherm | 2.3 | DSC | Thermal | HCl-glycine | 0.2 M | null | 52.65 | null | null | null | 79.11 | 0.38 | 84.37 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.3,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65707,"numValue":52.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65708,"numValue":79.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65709,"numValue":0.38,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65710,"numValue":84.37,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3957 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,957 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,795 | ProTherm | 2.4 | DSC | Thermal | HCl-glycine | 0.2 M | null | 53.15 | null | null | null | 76.72 | 1.29 | 82.22 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65712,"numValue":53.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65713,"numValue":76.72,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65714,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65715,"numValue":82.22,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3958 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,958 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,796 | ProTherm | 2.4 | DSC | Thermal | HCl-glycine | 0.2 M | null | 53.65 | null | null | null | 99.9 | 1.4 | 95.36 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65717,"numValue":53.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65718,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65719,"numValue":1.4,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65720,"numValue":95.36,"references":[... | ||||||||||||||||||||||||||||
fireprotdb:3959 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,959 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,797 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 56.15 | null | null | null | 88.67 | 2.72 | 90.34 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65722,"numValue":56.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65723,"numValue":88.67,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65724,"numValue":2.72,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65725,"numValue":90.34,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3961 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,961 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,799 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 56.65 | null | null | null | 94.89 | 3.39 | 95.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65732,"numValue":56.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65733,"numValue":94.89,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65734,"numValue":3.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65735,"numValue":95.6,"references":... | ||||||||||||||||||||||||||||
fireprotdb:3962 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,962 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,800 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 56.65 | null | null | null | 98.71 | 1.96 | 94.41 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65737,"numValue":56.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65738,"numValue":98.71,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65739,"numValue":1.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65740,"numValue":94.41,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3963 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,963 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,801 | ProTherm | 2.7 | DSC | Thermal | HCl-glycine | 0.2 M | null | 56.65 | null | null | null | 90.11 | 1.73 | 92.73 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65742,"numValue":56.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65743,"numValue":90.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65744,"numValue":1.73,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65745,"numValue":92.73,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3964 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,964 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,802 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 56.65 | null | null | null | 97.51 | 2.39 | 95.6 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65747,"numValue":56.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65748,"numValue":97.51,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65749,"numValue":2.39,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65750,"numValue":95.6,"references":... | ||||||||||||||||||||||||||||
fireprotdb:3965 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,965 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,803 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 56.65 | null | null | null | 94.41 | 2.24 | 90.82 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65752,"numValue":56.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65753,"numValue":94.41,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65754,"numValue":2.24,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65755,"numValue":90.82,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3966 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,966 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,804 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 56.95 | null | null | null | 81.5 | 2.8 | 90.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65757,"numValue":56.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65758,"numValue":81.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65759,"numValue":2.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65760,"numValue":90.11,"references":[... | ||||||||||||||||||||||||||||
fireprotdb:3967 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,967 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,805 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 57.45 | null | null | null | 81.98 | 1.81 | 90.58 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65762,"numValue":57.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65763,"numValue":81.98,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65764,"numValue":1.81,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65765,"numValue":90.58,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3968 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,968 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,806 | ProTherm | 2.7 | DSC | Thermal | HCl-glycine | 0.2 M | null | 58.15 | null | null | null | 93.93 | 0.22 | 96.08 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65767,"numValue":58.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65768,"numValue":93.93,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65769,"numValue":0.22,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65770,"numValue":96.08,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3969 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,969 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,807 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 58.35 | null | null | null | 115.92 | 0.44 | 103.49 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65772,"numValue":58.35,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65773,"numValue":115.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65774,"numValue":0.44,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65775,"numValue":103.49,"reference... | ||||||||||||||||||||||||||||
fireprotdb:3970 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,970 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,808 | ProTherm | 2.7 | DSC | Thermal | HCl-glycine | 0.2 M | null | 58.95 | null | null | null | 97.75 | 0.76 | 98.23 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65777,"numValue":58.95,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65778,"numValue":97.75,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65779,"numValue":0.76,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65780,"numValue":98.23,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3971 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,971 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,809 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 59.65 | null | null | null | 92.5 | 0.77 | 93.45 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65782,"numValue":59.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65783,"numValue":92.5,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65784,"numValue":0.77,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65785,"numValue":93.45,"references":... | ||||||||||||||||||||||||||||
fireprotdb:3972 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,972 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,810 | ProTherm | 2.8 | DSC | Thermal | HCl-glycine | 0.2 M | null | 60.15 | null | null | null | 114.96 | 0.33 | 104.21 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65787,"numValue":60.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65788,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65789,"numValue":0.33,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65790,"numValue":104.21,"reference... | ||||||||||||||||||||||||||||
fireprotdb:3973 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,973 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,811 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 60.45 | null | null | null | 100.38 | 0.58 | 99.19 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65792,"numValue":60.45,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65793,"numValue":100.38,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65794,"numValue":0.58,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65795,"numValue":99.19,"references... | ||||||||||||||||||||||||||||
fireprotdb:3974 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,974 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,812 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 60.65 | null | null | null | 92.26 | 0.75 | 93.69 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65797,"numValue":60.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65798,"numValue":92.26,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65799,"numValue":0.75,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65800,"numValue":93.69,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3975 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,975 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,813 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 60.85 | null | null | null | 89.15 | 0.74 | 93.69 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65802,"numValue":60.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65803,"numValue":89.15,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65804,"numValue":0.74,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65805,"numValue":93.69,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3976 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,976 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,814 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 60.85 | null | null | null | 105.4 | 1.14 | 102.29 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65807,"numValue":60.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65808,"numValue":105.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65809,"numValue":1.14,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65810,"numValue":102.29,"references... | ||||||||||||||||||||||||||||
fireprotdb:3977 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,977 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,815 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 61.55 | null | null | null | 104.92 | 1.46 | 104.45 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65812,"numValue":61.55,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65813,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65814,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65815,"numValue":104.45,"reference... | ||||||||||||||||||||||||||||
fireprotdb:3978 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,978 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,816 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 61.65 | null | null | null | 94.17 | 0.65 | 99.43 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65817,"numValue":61.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65818,"numValue":94.17,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65819,"numValue":0.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65820,"numValue":99.43,"references"... | ||||||||||||||||||||||||||||
fireprotdb:3979 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,979 | train | sequence | 55 | 55 | -1 | 147 | -1 | 6 | Lysozyme C | Gallus gallus | 1 | 6 | Lysozyme C | Gallus gallus | 1 | P00698 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,817 | ProTherm | 2.6 | DSC | Thermal | HCl-glycine | 0.2 M | null | 61.65 | null | null | null | 92.26 | 0.65 | 97.28 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1034 | ARTICLE | -1 | DOI: 10.1016/0040-6031(89)85164-0 | 1 | Schwarz FP | [{"numValue":2.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"HCl-glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.2 M","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65822,"numValue":61.65,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65823,"numValue":92.26,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":65824,"numValue":0.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":65825,"numValue":97.28,"references"... |
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