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:3324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,324 | train | mutant | 191 | 48 | 219 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56G | Y56G | 1 | 1 | 0 | 0 | 56 | Y | G | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 342 | ProTherm | 2.5 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38G | 53 | null | null | null | 85.8 | null | 87 | 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":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y38G","type":"_PD... | [{"datasets":[],"id":1402,"numValue":53.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1403,"numValue":85.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1404,"numValue":87.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1405,"numValue":null,"references":[],"s... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,325 | train | mutant | 191 | 48 | 219 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56G | Y56G | 1 | 1 | 0 | 0 | 56 | Y | G | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 343 | ProTherm | 2.78 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38G | 58.5 | null | null | null | 90.11 | null | 92.26 | 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":2.78,"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:Y38G","type":"_P... | [{"datasets":[],"id":1406,"numValue":58.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1407,"numValue":90.11,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":1408,"numValue":92.26,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["HotMuSiC_S1626.csv"],"i... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,326 | train | mutant | 191 | 48 | 219 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56G | Y56G | 1 | 1 | 0 | 0 | 56 | Y | G | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 344 | ProTherm | 3.24 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38G | 65.6 | null | null | null | 97.75 | null | 99.67 | 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":3.24,"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:Y38G","type":"_P... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1410,"numValue":65.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1411,"numValue":97.75,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1412,"numValue":99.67,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1413,"numValue":n... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,327 | train | mutant | 191 | 48 | 219 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56G | Y56G | 1 | 1 | 0 | 0 | 56 | Y | G | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 366 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:Y38G | 56.7 | -8.2 | null | null | 96.8 | 0.96 | 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:Y38G","type":"_PD... | [{"datasets":[],"id":1501,"numValue":56.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1502,"numValue":-8.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1503,"numValue":96.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id"... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,328 | train | mutant | 191 | 48 | 219 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56G | Y56G | 1 | 1 | 0 | 0 | 56 | Y | G | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 6,866 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:Y38G | null | null | null | 2.32 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|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":24285,"numValue":2.32,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24286,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3329 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,329 | train | mutant | 1,733 | 48 | 1,943 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56F | Y56F | 1 | 1 | 0 | 0 | 56 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 3,263 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y38F | 64.3 | -0.6 | null | null | 113.6 | 1.29 | 117.2 | 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:Y38F","type":"_PD... | [{"datasets":[],"id":11966,"numValue":64.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11967,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11968,"numValue":113.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3330 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,330 | train | mutant | 1,733 | 48 | 1,943 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56F | Y56F | 1 | 1 | 0 | 0 | 56 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 3,273 | ProTherm | 3.25 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y38F | 72.4 | null | null | null | 123.2 | 1.12 | 126.18 | 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":3.25,"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:Y38F","type":"_P... | [{"datasets":[],"id":12021,"numValue":72.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12022,"numValue":123.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12023,"numValue":1.12,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12024,"numValue":126.18,"references"... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,331 | train | mutant | 1,733 | 48 | 1,943 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56F | Y56F | 1 | 1 | 0 | 0 | 56 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 3,274 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y38F | 70.3 | null | null | null | 121.1 | 0.96 | 124.16 | 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":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y38F","type":"_PD... | [{"datasets":[],"id":12026,"numValue":70.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12027,"numValue":121.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12028,"numValue":0.96,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12029,"numValue":124.16,"references"... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3332 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,332 | train | mutant | 1,733 | 48 | 1,943 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56F | Y56F | 1 | 1 | 0 | 0 | 56 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 3,275 | ProTherm | 2.92 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y38F | 67.2 | null | null | null | 117.2 | 1.46 | 121.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":2.92,"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:Y38F","type":"_P... | [{"datasets":[],"id":12031,"numValue":67.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12032,"numValue":117.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12033,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12034,"numValue":121.05,"references"... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,333 | train | mutant | 1,733 | 48 | 1,943 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56F | Y56F | 1 | 1 | 0 | 0 | 56 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 3,276 | ProTherm | 2.71 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y38F | 64.6 | null | null | null | 113.2 | 1.03 | 117.22 | 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":2.71,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y38F","type":"_P... | [{"datasets":[],"id":12036,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12037,"numValue":113.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12038,"numValue":1.03,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12039,"numValue":117.22,"references"... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,334 | train | mutant | 1,733 | 48 | 1,943 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y56F | Y56F | 1 | 1 | 0 | 0 | 56 | Y | F | 6 | CONSERVATION | 1LZ1 | 405 | null | 56 | A | T | false | false | 19.76302 | 13.085 | 6,898 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:Y38F | null | null | null | 0.19 | 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 | 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":24375,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24376,"numValue":0.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24377,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7011,"numValue":6.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3335 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,335 | train | mutant | 1,938 | 48 | 2,167 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58A | T58A | 1 | 1 | 0 | 0 | 58 | T | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,717 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40A | 68.6 | null | null | null | 117.11 | null | 120.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40A","type":... | [{"datasets":[],"id":13713,"numValue":68.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13714,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13715,"numValue":120.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13716,"numValue":null,"reference... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,336 | train | mutant | 1,938 | 48 | 2,167 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58A | T58A | 1 | 1 | 0 | 0 | 58 | T | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,718 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40A | 66.5 | null | null | null | 114.01 | null | 117.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40A","type":... | [{"datasets":[],"id":13717,"numValue":66.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13718,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13719,"numValue":117.11,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13720,"numValue":null,"reference... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3337 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,337 | train | mutant | 1,938 | 48 | 2,167 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58A | T58A | 1 | 1 | 0 | 0 | 58 | T | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,719 | ProTherm | 2.85 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40A | 63.3 | null | null | null | 107.07 | null | 114.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.85,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40A","type"... | [{"datasets":[],"id":13721,"numValue":63.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13722,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13723,"numValue":114.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13724,"numValue":null,"reference... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,338 | train | mutant | 1,938 | 48 | 2,167 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58A | T58A | 1 | 1 | 0 | 0 | 58 | T | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,720 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40A | 59.4 | null | null | null | 99.9 | null | 102.06 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40A","type":... | [{"datasets":[],"id":13725,"numValue":59.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13726,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13727,"numValue":102.06,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13728,"numValue":null,"references"... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,339 | train | mutant | 1,938 | 48 | 2,167 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58A | T58A | 1 | 1 | 0 | 0 | 58 | T | A | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,721 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40A | 56.6 | null | null | null | 97.51 | null | 103.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40A","type":... | [{"datasets":[],"id":13729,"numValue":56.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13730,"numValue":97.51,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13731,"numValue":103.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13732,"numValue":null,"references... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,340 | train | mutant | 1,943 | 48 | 2,172 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58V | T58V | 1 | 1 | 0 | 0 | 58 | T | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,740 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40V | 68.7 | null | null | null | 114.96 | null | 122.85 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40V","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13805,"numValue":68.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13806,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13807,"numValue":122.85,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,341 | train | mutant | 1,943 | 48 | 2,172 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58V | T58V | 1 | 1 | 0 | 0 | 58 | T | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,741 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40V | 66.3 | null | null | null | 112.09 | null | 119.02 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40V","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13809,"numValue":66.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13810,"numValue":112.09,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13811,"numValue":119.02,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,342 | train | mutant | 1,943 | 48 | 2,172 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58V | T58V | 1 | 1 | 0 | 0 | 58 | T | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,742 | ProTherm | 2.85 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40V | 63.2 | null | null | null | 109.94 | null | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.85,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40V","type"... | [{"datasets":["STRUM_Q3421.csv"],"id":13813,"numValue":63.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13814,"numValue":109.94,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13815,"numValue":113.05,"references":[],"strValue":null,"type":"DHVH"},{... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3343 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,343 | train | mutant | 1,943 | 48 | 2,172 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58V | T58V | 1 | 1 | 0 | 0 | 58 | T | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,743 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40V | 59.2 | null | null | null | 92.97 | null | 99.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40V","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13817,"numValue":59.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13818,"numValue":92.97,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13819,"numValue":99.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["STRUM_Q... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3344 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,344 | train | mutant | 1,943 | 48 | 2,172 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T58V | T58V | 1 | 1 | 0 | 0 | 58 | T | V | 9 | CONSERVATION | 1LZ1 | 405 | null | 58 | A | T | true | false | 1.343709 | 12.362857 | 3,744 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T40V | 57 | null | null | null | 96.56 | null | 103.97 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T40V","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13821,"numValue":57.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":13822,"numValue":96.56,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13823,"numValue":103.97,"references":[],"strValue... | [{"id":7013,"numValue":9.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3346 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,346 | train | mutant | 1,939 | 48 | 2,168 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T61A | T61A | 1 | 1 | 0 | 0 | 61 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 61 | A | E | false | false | 65.921568 | 20.53 | 3,723 | ProTherm | 2.9 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T43A | 67.1 | null | null | null | 110.9 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.9,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T43A","type":... | [{"datasets":[],"id":13737,"numValue":67.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13738,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13739,"numValue":112.09,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13740,"numValue":null,"references... | [{"id":7016,"numValue":5.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3347 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,347 | train | mutant | 1,939 | 48 | 2,168 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T61A | T61A | 1 | 1 | 0 | 0 | 61 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 61 | A | E | false | false | 65.921568 | 20.53 | 3,724 | ProTherm | 2.74 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T43A | 64.5 | null | null | null | 108.03 | null | 108.99 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.74,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T43A","type"... | [{"datasets":[],"id":13741,"numValue":64.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13742,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13743,"numValue":108.99,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13744,"numValue":null,"reference... | [{"id":7016,"numValue":5.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3348 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,348 | train | mutant | 1,939 | 48 | 2,168 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T61A | T61A | 1 | 1 | 0 | 0 | 61 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 61 | A | E | false | false | 65.921568 | 20.53 | 3,725 | ProTherm | 2.54 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T43A | 61.1 | null | null | null | 103.97 | null | 104.92 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv|STRUM_Q3421.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.54,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T43A","type"... | [{"datasets":["HotMuSiC_S1626.csv","STRUM_Q3421.csv"],"id":13745,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":13746,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":["STRUM_Q3421.csv"],"id":13747... | [{"id":7016,"numValue":5.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,349 | train | mutant | 1,944 | 48 | 2,173 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T61V | T61V | 1 | 1 | 0 | 0 | 61 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 61 | A | E | false | false | 65.921568 | 20.53 | 3,745 | ProTherm | 3.2 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T43V | 75.4 | null | null | null | 113.05 | null | 120.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q3421.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T43V","type":... | [{"datasets":["STRUM_Q3421.csv"],"id":13825,"numValue":75.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13826,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421... | [{"id":7016,"numValue":5.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,350 | train | mutant | 1,944 | 48 | 2,173 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T61V | T61V | 1 | 1 | 0 | 0 | 61 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 61 | A | E | false | false | 65.921568 | 20.53 | 3,746 | ProTherm | 3.02 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T43V | 73 | null | null | null | 108.03 | null | 118.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.02,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T43V","type"... | [{"datasets":[],"id":13829,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13830,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13831,"numValue":118.07,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id... | [{"id":7016,"numValue":5.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,351 | train | mutant | 1,944 | 48 | 2,173 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T61V | T61V | 1 | 1 | 0 | 0 | 61 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 61 | A | E | false | false | 65.921568 | 20.53 | 3,747 | ProTherm | 2.71 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T43V | 68.4 | null | null | null | 104.92 | null | 114.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.71,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T43V","type"... | [{"datasets":[],"id":13833,"numValue":68.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S2204.csv","STRUM_Q3421.csv","... | [{"id":7016,"numValue":5.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3352 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,352 | train | mutant | 1,944 | 48 | 2,173 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T61V | T61V | 1 | 1 | 0 | 0 | 61 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 61 | A | E | false | false | 65.921568 | 20.53 | 3,748 | ProTherm | 2.51 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T43V | 65 | null | null | null | 99.9 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.51,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T43V","type"... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13837,"numValue":65.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13838,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13... | [{"id":7016,"numValue":5.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3353 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,353 | train | mutant | 1,734 | 48 | 1,944 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y63F | Y63F | 1 | 1 | 0 | 0 | 63 | Y | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 63 | A | E | false | false | 127.400374 | 22.9 | 3,264 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y45F | 65.1 | 0.2 | null | null | 112.2 | 1.1 | 118.1 | 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:Y45F","type":"_PD... | [{"datasets":[],"id":11972,"numValue":65.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11973,"numValue":0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11974,"numValue":112.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"... | [{"id":7018,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3354 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,354 | train | mutant | 1,734 | 48 | 1,944 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y63F | Y63F | 1 | 1 | 0 | 0 | 63 | Y | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 63 | A | E | false | false | 127.400374 | 22.9 | 3,277 | ProTherm | 3.13 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y45F | 72.5 | null | null | null | 121.1 | 1.63 | 127.03 | 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":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:Y45F","type":"_P... | [{"datasets":[],"id":12041,"numValue":72.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12042,"numValue":121.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12043,"numValue":1.63,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12044,"numValue":127.03,"references"... | [{"id":7018,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,355 | train | mutant | 1,734 | 48 | 1,944 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y63F | Y63F | 1 | 1 | 0 | 0 | 63 | Y | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 63 | A | E | false | false | 127.400374 | 22.9 | 3,278 | ProTherm | 2.89 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y45F | 68.7 | null | null | null | 116 | 0.65 | 122 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 295 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. | 1,998 | 10.1021/bi980431i | 9649316 | Biochemistry;37;9355-62 | 5 | Takano K|Yamagata Y|Funahashi J|Kubota M|Sumikawa Y | [{"numValue":2.89,"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:Y45F","type":"_P... | [{"datasets":[],"id":12046,"numValue":68.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12047,"numValue":116.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12048,"numValue":0.65,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12049,"numValue":122.0,"references":... | [{"id":7018,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3356 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,356 | train | mutant | 1,734 | 48 | 1,944 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y63F | Y63F | 1 | 1 | 0 | 0 | 63 | Y | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 63 | A | E | false | false | 127.400374 | 22.9 | 3,279 | ProTherm | 2.71 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y45F | 64.9 | null | null | null | 111 | 1.15 | 117.22 | 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":2.71,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y45F","type":"_P... | [{"datasets":[],"id":12051,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12052,"numValue":111.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12053,"numValue":1.15,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12054,"numValue":117.22,"references"... | [{"id":7018,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,357 | train | mutant | 1,734 | 48 | 1,944 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y63F | Y63F | 1 | 1 | 0 | 0 | 63 | Y | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 63 | A | E | false | false | 127.400374 | 22.9 | 3,280 | ProTherm | 2.67 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y45F | 64.6 | null | null | null | 112.2 | 1.34 | 117.22 | 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":2.67,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y45F","type":"_P... | [{"datasets":[],"id":12056,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12057,"numValue":112.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12058,"numValue":1.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12059,"numValue":117.22,"references"... | [{"id":7018,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3358 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,358 | train | mutant | 1,734 | 48 | 1,944 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y63F | Y63F | 1 | 1 | 0 | 0 | 63 | Y | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 63 | A | E | false | false | 127.400374 | 22.9 | 3,281 | ProTherm | 2.48 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y45F | 61.4 | null | null | null | 109.1 | 0.89 | 115.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":2.48,"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:Y45F","type":"_P... | [{"datasets":[],"id":12061,"numValue":61.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12062,"numValue":109.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12063,"numValue":0.89,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12064,"numValue":115.07,"references"... | [{"id":7018,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3359 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,359 | train | mutant | 1,734 | 48 | 1,944 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y63F | Y63F | 1 | 1 | 0 | 0 | 63 | Y | F | 3 | CONSERVATION | 1LZ1 | 405 | null | 63 | A | E | false | false | 127.400374 | 22.9 | 6,899 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:Y45F | null | null | null | -0.07 | null | 1.1 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":24378,"numValue":1.1,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24379,"numValue":-0.07,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24380,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7018,"numValue":3.0,"position":63,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3360 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,360 | train | mutant | 634 | 48 | 686 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A65P | A65P | 1 | 1 | 0 | 0 | 65 | A | P | 5 | CONSERVATION | 1LZ1 | 405 | null | 65 | A | T | false | false | 81.730736 | 36.688 | 1,051 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | null | 1LZ1_A:A47P | 69.1 | 0.3 | null | null | null | 1.56 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:A47P","type":"... | [{"datasets":[],"id":3928,"numValue":69.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3929,"numValue":0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3930,"numValue":1.56,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id"... | [{"id":7020,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3361 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,361 | train | mutant | 634 | 48 | 686 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A65P | A65P | 1 | 1 | 0 | 0 | 65 | A | P | 5 | CONSERVATION | 1LZ1 | 405 | null | 65 | A | T | false | false | 81.730736 | 36.688 | 6,704 | ProTherm | 2.8 | DSC | Thermal | glycine-HCl | 50 mM | 68.8 | 1LZ1_A:A47P | null | null | null | -0.1 | 119.4 | 1.56 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 107 | ARTICLE | Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. | 1,992 | 10.1021/bi00146a008 | 1643041 | Biochemistry;31;7077-85 | 5 | Yutani K|Kuroki R|Matsushima M|Inaka K|Herning T | [{"numValue":2.8,"strValue":null,"type":"PH"},{"numValue":68.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":[],"id":23847,"numValue":119.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":23848,"numValue":1.56,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":23849,"numValue":-0.1,"referenc... | [{"id":7020,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,362 | train | mutant | 634 | 48 | 686 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | A65P | A65P | 1 | 1 | 0 | 0 | 65 | A | P | 5 | CONSERVATION | 1LZ1 | 405 | null | 65 | A | T | false | false | 81.730736 | 36.688 | 9,881 | ProTherm | 3 | CD | GdnHCl | glycine-HCl | 40 mM | 25 | 1LZ1_A:A47P | null | null | 10.8 | -1.1 | null | null | null | 3.3 | 5.5 | null | null | null | null | null | null | null | yes (100%) | DG|DDG|M|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 658 | ARTICLE | Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization. | 1,991 | 10.1021/bi00105a011 | 1911779 | Biochemistry;30;9882-91 | 4 | Yutani K|Kikuchi M|Herning T|Taniyama Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"40 mM","type":"BUFFER_... | [{"datasets":[],"id":33964,"numValue":10.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":33965,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":33966,"numValue":5.5,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":33967,"numValue":3.3,"references":[],"s... | [{"id":7020,"numValue":5.0,"position":65,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,363 | train | mutant | 291 | 48 | 323 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G66A | G66A | 1 | 1 | 0 | 0 | 66 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 66 | A | T | false | false | 81.679 | 28.6325 | 511 | ProTherm | 2.4 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G48A | 61.1 | null | null | null | 94.89 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":2.4,"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:G48A","type":"_PD... | [{"datasets":["HotMuSiC_S1626.csv"],"id":2052,"numValue":61.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["HotMuSiC_S1626.csv"],"id":2053,"numValue":94.89,"references":[],"strValue":null,"type":"DH"},{"datasets":["HotMuSiC_S1626.csv"],"id":2054,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":7021,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,364 | train | mutant | 291 | 48 | 323 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G66A | G66A | 1 | 1 | 0 | 0 | 66 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 66 | A | T | false | false | 81.679 | 28.6325 | 512 | ProTherm | 2.68 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G48A | 66 | null | null | null | 102.06 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":2.68,"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:G48A","type":"_P... | [{"datasets":[],"id":2055,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2056,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2057,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7021,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3365 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,365 | train | mutant | 291 | 48 | 323 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G66A | G66A | 1 | 1 | 0 | 0 | 66 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 66 | A | T | false | false | 81.679 | 28.6325 | 513 | ProTherm | 3.2 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G48A | 75.1 | null | null | null | 117.11 | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 54 | ARTICLE | Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein. | 2,001 | 10.1002/prot.1147 | 11599030 | Proteins;45;274-80 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:G48A","type":"_PD... | [{"datasets":[],"id":2058,"numValue":75.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2059,"numValue":117.11,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2060,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7021,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3366 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,366 | train | mutant | 291 | 48 | 323 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G66A | G66A | 1 | 1 | 0 | 0 | 66 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 66 | A | T | false | false | 81.679 | 28.6325 | 533 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:G48A | 66.4 | 1.5 | null | null | 100.62 | 1.6 | 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:G48A","type":"_PD... | [{"datasets":[],"id":2123,"numValue":66.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":2124,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2125,"numValue":100.62,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":2126,"numValue":1.6,"references":[],"st... | [{"id":7021,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3367 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,367 | train | mutant | 291 | 48 | 323 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | G66A | G66A | 1 | 1 | 0 | 0 | 66 | G | A | 2 | CONSERVATION | 1LZ1 | 405 | null | 66 | A | T | false | false | 81.679 | 28.6325 | 6,876 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:G48A | null | null | null | -0.45 | null | 1.6 | 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":24309,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24310,"numValue":-0.45,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24311,"numValue":null,"references":[],"strValue":"yes","t... | [{"id":7021,"numValue":2.0,"position":66,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3368 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,368 | train | mutant | 46 | 48 | 51 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D67N | D67N | 1 | 1 | 0 | 0 | 67 | D | N | 6 | CONSERVATION | 1LZ1 | 405 | null | 67 | A | T | true | true | 69.164639 | 27.6325 | 46 | ProTherm | 2.2 | DSC | Thermal | glycine hydrochloride | 0.05 M | null | 1LZ1_A:D49N | 57.5 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | khan_protherm_data_mapped.csv|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:D49... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":157,"numValue":57.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":158,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"]... | [{"id":7022,"numValue":6.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3369 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,369 | train | mutant | 46 | 48 | 51 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D67N | D67N | 1 | 1 | 0 | 0 | 67 | D | N | 6 | CONSERVATION | 1LZ1 | 405 | null | 67 | A | T | true | true | 69.164639 | 27.6325 | 52 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | null | 1LZ1_A:D49N | 77.4 | -2.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | khan_protherm_data_mapped.csv|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:D49N","typ... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":175,"numValue":77.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","khan_protherm_data_mapped.csv","Saraboji_S1791.csv"],"id":176,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["khan_protherm_data_mapped.csv"... | [{"id":7022,"numValue":6.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3370 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,370 | train | mutant | 46 | 48 | 51 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | D67N | D67N | 1 | 1 | 0 | 0 | 67 | D | N | 6 | CONSERVATION | 1LZ1 | 405 | null | 67 | A | T | true | true | 69.164639 | 27.6325 | 6,839 | ProTherm | 4 | DSC | Thermal | sodium acetate | 0.02 M | 65 | 1LZ1_A:D49N | null | null | 4.42 | 1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv | 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":["khan_protherm_data_mapped.csv"],"id":24215,"numValue":4.42,"references":[],"strValue":null,"type":"DG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":24216,"numValue":1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":["khan_protherm_data_mapped.csv"],"id":24217,"numValue":null,"reference... | [{"id":7022,"numValue":6.0,"position":67,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3371 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,371 | train | mutant | 192 | 48 | 220 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68A | R68A | 1 | 1 | 0 | 0 | 68 | R | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 345 | ProTherm | 2.5 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R50A | 62.8 | null | null | null | 101.1 | null | 108.03 | 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":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50A","type":"_PD... | [{"datasets":[],"id":1414,"numValue":62.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1415,"numValue":101.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1416,"numValue":108.03,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1417,"numValue":null,"references":[]... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3372 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,372 | train | mutant | 192 | 48 | 220 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68A | R68A | 1 | 1 | 0 | 0 | 68 | R | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 346 | ProTherm | 2.71 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R50A | 66.6 | null | null | null | 106.12 | null | 113.05 | 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":2.71,"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:R50A","type":"_P... | [{"datasets":[],"id":1418,"numValue":66.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1419,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1420,"numValue":113.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1421,"numValue":null,"references":[... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3373 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,373 | train | mutant | 192 | 48 | 220 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68A | R68A | 1 | 1 | 0 | 0 | 68 | R | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 347 | ProTherm | 2.84 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R50A | 69.1 | null | null | null | 108.99 | null | 117.11 | 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":2.84,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50A","type":"_P... | [{"datasets":[],"id":1422,"numValue":69.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1423,"numValue":108.99,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1424,"numValue":117.11,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1425,"numValue":null,"references":[... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3374 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,374 | train | mutant | 192 | 48 | 220 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68A | R68A | 1 | 1 | 0 | 0 | 68 | R | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 348 | ProTherm | 3 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R50A | 70.9 | null | null | null | 114.01 | null | 120.94 | 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":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50A","type":"_PD... | [{"datasets":[],"id":1426,"numValue":70.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1427,"numValue":114.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":1428,"numValue":120.94,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":1429,"numValue":null,"references":[... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3375 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,375 | train | mutant | 192 | 48 | 220 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68A | R68A | 1 | 1 | 0 | 0 | 68 | R | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 367 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | null | 1LZ1_A:R50A | 66.3 | 1.4 | null | null | 103.97 | 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 | 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:R50A","type":"_PD... | [{"datasets":[],"id":1506,"numValue":66.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1507,"numValue":1.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1508,"numValue":103.97,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3376 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,376 | train | mutant | 192 | 48 | 220 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68A | R68A | 1 | 1 | 0 | 0 | 68 | R | A | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 6,867 | ProTherm | 2.7 | DSC | Thermal | Gly-HCl | 0.05 M | 64.9 | 1LZ1_A:R50A | null | null | null | -0.43 | 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":24287,"numValue":-0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24288,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3377 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,377 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 3,887 | ProTherm | 2.58 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:R50G | 63.7 | null | null | null | 99.9 | null | 110.9 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.58,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50G","type":"_P... | [{"datasets":[],"id":14307,"numValue":63.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14308,"numValue":99.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14309,"numValue":110.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"]... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3378 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,378 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 3,888 | ProTherm | 2.78 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:R50G | 67.3 | null | null | null | 102.06 | null | 114.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.78,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50G","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14311,"numValue":67.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14312,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3379 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,379 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 3,889 | ProTherm | 3.11 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:R50G | 73 | null | null | null | 113.05 | null | 123.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":3.11,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50G","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14315,"numValue":73.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14316,"numValue":113.05,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3380 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,380 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 3,909 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:R50G | 65.8 | 0.9 | null | null | 100.38 | 1.46 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50G","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":14397,"numValue":65.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":14398,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"d... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3381 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,381 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 3,918 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:R50G | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50G","type":"_PD... | [{"datasets":[],"id":14433,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14434,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3382 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,382 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 4,201 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:R50G | 65.8 | 0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:R50G","type":... | [{"datasets":[],"id":15575,"numValue":65.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15576,"numValue":0.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15577,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3384 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,384 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 6,912 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:R50G | null | null | null | -0.26 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 361 | ARTICLE | Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes. | 1,999 | 10.1093/protein/12.8.663 | 10469827 | Protein Eng;12;663-72 | 6 | Takano K|Yamagata Y|Yutani K|Ogasahara K|Ota M|Nishikawa K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24426,"numValue":-0.26,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24427,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3385 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,385 | train | mutant | 2,020 | 48 | 2,256 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | R68G | R68G | 1 | 1 | 0 | 0 | 68 | R | G | 4 | CONSERVATION | 1LZ1 | 405 | null | 68 | A | T | false | false | 147.895362 | 38.711818 | 6,933 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | 64.9 | 1LZ1_A:R50G | null | null | null | -0.26 | 100.38 | 1.46 | null | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DDG|REVERSIBILITY | khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 397 | ARTICLE | Role of amino acid residues at turns in the conformational stability and folding of human lysozyme. | 2,000 | 10.1021/bi9928694 | 10913274 | Biochemistry;39;8655-65 | 3 | Takano K|Yamagata Y|Yutani K | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFF... | [{"datasets":[],"id":24468,"numValue":100.38,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24469,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":["khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":24470,"numValue":-0.26,"references":[],"strValue":null,"... | [{"id":7023,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3387 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,387 | train | mutant | 1,890 | 48 | 2,119 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S69A | S69A | 1 | 1 | 0 | 0 | 69 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 69 | A | E | false | true | 0.394081 | 15.693333 | 3,644 | ProTherm | 3.11 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S51A | 70.8 | null | null | null | 119.98 | 1.36 | 125.96 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q306.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":3.11,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S51A","type":"_P... | [{"datasets":[],"id":13399,"numValue":70.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":13400,"numValue":119.98,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q306.... | [{"id":7024,"numValue":8.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3388 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,388 | train | mutant | 1,890 | 48 | 2,119 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S69A | S69A | 1 | 1 | 0 | 0 | 69 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 69 | A | E | false | true | 0.394081 | 15.693333 | 3,645 | ProTherm | 2.86 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S51A | 66.7 | null | null | null | 114.96 | 1.55 | 120.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.86,"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:S51A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13404,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13405,"numValue":114.96,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7024,"numValue":8.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3389 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,389 | train | mutant | 1,890 | 48 | 2,119 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S69A | S69A | 1 | 1 | 0 | 0 | 69 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 69 | A | E | false | true | 0.394081 | 15.693333 | 3,646 | ProTherm | 2.69 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S51A | 64.2 | null | null | null | 110.9 | 1.43 | 118.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|AUTOMUTE_S1962.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.69,"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:S51A","type":"_P... | [{"datasets":["AUTOMUTE_S1925.csv","AUTOMUTE_S1962.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S2204.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id"... | [{"id":7024,"numValue":8.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3390 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,390 | train | mutant | 1,890 | 48 | 2,119 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S69A | S69A | 1 | 1 | 0 | 0 | 69 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 69 | A | E | false | true | 0.394081 | 15.693333 | 3,647 | ProTherm | 2.51 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S51A | 61 | null | null | null | 106.12 | 1.48 | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.51,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S51A","type":"_P... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13414,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13415,"numValue":106.12,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7024,"numValue":8.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3391 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,391 | train | mutant | 1,890 | 48 | 2,119 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | S69A | S69A | 1 | 1 | 0 | 0 | 69 | S | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 69 | A | E | false | true | 0.394081 | 15.693333 | 3,662 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:S51A | 64.2 | -0.7 | null | null | 111.85 | 1.43 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 343 | ARTICLE | Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. | 1,999 | 10.1021/bi9901228 | 10350481 | Biochemistry;38;6623-9 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Kubota M|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:S51A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13489,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13490,"numValue":-0.7,"references":[],"strValue":nul... | [{"id":7024,"numValue":8.0,"position":69,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3392 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,392 | train | mutant | 1,940 | 48 | 2,169 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70A | T70A | 1 | 1 | 0 | 0 | 70 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,726 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52A | 68.9 | null | null | null | 108.99 | null | 118.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|PoPMuSi... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52A","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13749,"numValue":68.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47a... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3393 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,393 | train | mutant | 1,940 | 48 | 2,169 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70A | T70A | 1 | 1 | 0 | 0 | 70 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,727 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52A | 66.9 | null | null | null | 108.03 | null | 114.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52A","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13753,"numValue":66.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13754,"numValue":108.03,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3394 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,394 | train | mutant | 1,940 | 48 | 2,169 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70A | T70A | 1 | 1 | 0 | 0 | 70 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,728 | ProTherm | 2.85 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52A | 64.4 | null | null | null | 104.92 | null | 112.09 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.85,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52A","type"... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13757,"numValue":64.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13758,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3395 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,395 | train | mutant | 1,940 | 48 | 2,169 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70A | T70A | 1 | 1 | 0 | 0 | 70 | T | A | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,729 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52A | 61.9 | null | null | null | 103.01 | null | 108.99 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52A","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13761,"numValue":61.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13762,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3397 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,397 | train | mutant | 1,945 | 48 | 2,174 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70V | T70V | 1 | 1 | 0 | 0 | 70 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,749 | ProTherm | 3.1 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52V | 68.7 | null | null | null | 110.9 | null | 114.01 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52V","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13841,"numValue":68.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13842,"numValue":110.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13843,"numValue":114.01,"references":[],"strValue":null,"type":"DHVH"},{"datasets":... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3398 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,398 | train | mutant | 1,945 | 48 | 2,174 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70V | T70V | 1 | 1 | 0 | 0 | 70 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,750 | ProTherm | 3 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52V | 66.6 | null | null | null | 107.07 | null | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52V","type":... | [{"datasets":[],"id":13845,"numValue":66.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":13846,"numValue":107.07,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":13847,"numValue":113.05,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":13848,"numValue":null,"reference... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3399 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,399 | train | mutant | 1,945 | 48 | 2,174 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70V | T70V | 1 | 1 | 0 | 0 | 70 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,751 | ProTherm | 2.85 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52V | 64.2 | null | null | null | 104.92 | null | 109.94 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.85,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52V","type"... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13849,"numValue":64.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13850,"numValue":104.92,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3400 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,400 | train | mutant | 1,945 | 48 | 2,174 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70V | T70V | 1 | 1 | 0 | 0 | 70 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,752 | ProTherm | 2.7 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52V | 62.1 | null | null | null | 102.06 | null | 107.07 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52V","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13853,"numValue":62.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13854,"numValue":102.06,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3401 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,401 | train | mutant | 1,945 | 48 | 2,174 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | T70V | T70V | 1 | 1 | 0 | 0 | 70 | T | V | 5 | CONSERVATION | 1LZ1 | 405 | null | 70 | A | E | false | false | 10.301405 | 11.667143 | 3,753 | ProTherm | 2.5 | DSC | Thermal | glycine-HCl | 0.05 M | null | 1LZ1_A:T52V | 58.8 | null | null | null | 98.71 | null | 103.97 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 345 | ARTICLE | Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,). | 1,999 | 10.1021/bi9910169 | 10504240 | Biochemistry;38;12698-708 | 6 | Takano K|Yamagata Y|Yutani K|Funahashi J|Hioki Y|Kuramitsu S | [{"numValue":2.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:T52V","type":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":13857,"numValue":58.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":13858,"numValue":98.71,"references":[],"strValue":null,"type":"DH"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_... | [{"id":7025,"numValue":5.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3402 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,402 | train | mutant | 1,735 | 48 | 1,945 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y72F | Y72F | 1 | 1 | 0 | 0 | 72 | Y | F | 7 | CONSERVATION | 1LZ1 | 405 | null | 72 | A | E | false | false | 20.125012 | 11.801667 | 3,265 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y54F | 61.9 | -3 | null | null | 110.3 | 1.67 | 117.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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:Y54F","type":"_PD... | [{"datasets":[],"id":11978,"numValue":61.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11979,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11980,"numValue":110.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7027,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3403 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,403 | train | mutant | 1,735 | 48 | 1,945 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y72F | Y72F | 1 | 1 | 0 | 0 | 72 | Y | F | 7 | CONSERVATION | 1LZ1 | 405 | null | 72 | A | E | false | false | 20.125012 | 11.801667 | 3,282 | ProTherm | 3.13 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y54F | 69.1 | null | null | null | 117.2 | 1.12 | 124.16 | 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":3.13,"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:Y54F","type":"_P... | [{"datasets":[],"id":12066,"numValue":69.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12067,"numValue":117.2,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12068,"numValue":1.12,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12069,"numValue":124.16,"references"... | [{"id":7027,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3404 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,404 | train | mutant | 1,735 | 48 | 1,945 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y72F | Y72F | 1 | 1 | 0 | 0 | 72 | Y | F | 7 | CONSERVATION | 1LZ1 | 405 | null | 72 | A | E | false | false | 20.125012 | 11.801667 | 3,283 | ProTherm | 2.99 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y54F | 67 | null | null | null | 114.1 | 1.34 | 120.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":2.99,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:Y54F","type":"_P... | [{"datasets":[],"id":12071,"numValue":67.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12072,"numValue":114.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12073,"numValue":1.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12074,"numValue":120.1,"references":... | [{"id":7027,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3405 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,405 | train | mutant | 1,735 | 48 | 1,945 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y72F | Y72F | 1 | 1 | 0 | 0 | 72 | Y | F | 7 | CONSERVATION | 1LZ1 | 405 | null | 72 | A | E | false | false | 20.125012 | 11.801667 | 3,284 | ProTherm | 2.82 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y54F | 64 | null | null | null | 108.1 | 1.91 | 114.11 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":2.82,"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:Y54F","type":"_P... | [{"datasets":[],"id":12076,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12077,"numValue":108.1,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12078,"numValue":1.91,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12079,"numValue":114.11,"references"... | [{"id":7027,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3406 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,406 | train | mutant | 1,735 | 48 | 1,945 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y72F | Y72F | 1 | 1 | 0 | 0 | 72 | Y | F | 7 | CONSERVATION | 1LZ1 | 405 | null | 72 | A | E | false | false | 20.125012 | 11.801667 | 3,285 | ProTherm | 2.69 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:Y54F | 61.7 | null | null | null | 105 | 0.89 | 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":2.69,"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:Y54F","type":"_P... | [{"datasets":[],"id":12081,"numValue":61.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12082,"numValue":105.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12083,"numValue":0.89,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12084,"numValue":112.2,"references":... | [{"id":7027,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3407 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,407 | train | mutant | 1,735 | 48 | 1,945 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | Y72F | Y72F | 1 | 1 | 0 | 0 | 72 | Y | F | 7 | CONSERVATION | 1LZ1 | 405 | null | 72 | A | E | false | false | 20.125012 | 11.801667 | 6,900 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:Y54F | null | null | null | 0.96 | null | 1.67 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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":24381,"numValue":1.67,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24382,"numValue":0.96,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24383,"numValue":null,"references":[],"strValue":"yes","type":"REV... | [{"id":7027,"numValue":7.0,"position":72,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3408 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,408 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,185 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56V | 42.9 | -6.3 | null | null | 71.77 | 1.29 | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 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:I56V","type":"_PD... | [{"datasets":[],"id":11633,"numValue":42.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":11634,"numValue":-6.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":11635,"numValue":71.77,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3409 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,409 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,203 | ProTherm | 3.1 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56V | 50.5 | null | null | null | 74.4 | null | 78.2 | 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":3.1,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56V","type":"_PD... | [{"datasets":[],"id":11718,"numValue":50.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11719,"numValue":74.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11720,"numValue":78.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11721,"numValue":null,"references":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3410 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,410 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,204 | ProTherm | 3 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56V | 48.2 | null | null | null | 69.4 | 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":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:I56V","type":"_PD... | [{"datasets":[],"id":11722,"numValue":48.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11723,"numValue":69.4,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11724,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11725,"numValue":null,"references":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3411 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,411 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,205 | ProTherm | 2.8 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56V | 45.3 | null | null | null | 66.7 | null | 71.1 | 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":2.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56V","type":"_PD... | [{"datasets":[],"id":11726,"numValue":45.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":11727,"numValue":66.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":11728,"numValue":71.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":11729,"numValue":null,"references":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3413 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,413 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,017 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56V | 61.3 | -3.6 | null | null | 113.53 | 1.34 | 117.04 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56V","type":"_PD... | [{"datasets":[],"id":14837,"numValue":61.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14838,"numValue":-3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14839,"numValue":113.53,"references":[],"strValue":null,"type":"DH"},{"datasets":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3414 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,414 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,032 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56V | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56V","type":"_PD... | [{"datasets":[],"id":14923,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14924,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,415 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,154 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56V | 61.3 | -3.6 | null | null | 113.6 | 1.34 | 117.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DH|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 388 | ARTICLE | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. | 1,995 | 10.1006/jmbi.1995.0599 | 7473760 | J Mol Biol;254;62-76 | 6 | Takano K|Yamagata Y|Ogasahara K|Fujii S|Kaneda H|Kanaya E | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56V","type":"_PD... | [{"datasets":[],"id":15370,"numValue":61.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15371,"numValue":-3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15372,"numValue":113.6,"references":[],"strValue":null,"type":"DH"},{"datasets":[],... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3416 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,416 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,883 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56V | null | null | null | 1.2 | null | 1.34 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 388 | ARTICLE | Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. | 1,995 | 10.1006/jmbi.1995.0599 | 7473760 | J Mol Biol;254;62-76 | 6 | Takano K|Yamagata Y|Ogasahara K|Fujii S|Kaneda H|Kanaya E | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24330,"numValue":1.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24331,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24332,"numValue":null,"references":[],"strValue":"yes","type":"REVE... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3417 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,417 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,919 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56V | null | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24440,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24441,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,418 | train | mutant | 1,719 | 48 | 1,929 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74V | I74V | 1 | 1 | 0 | 0 | 74 | I | V | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 7,739 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 49.2 | 1LZ1_A:I56V | null | null | null | 1.34 | null | 1.29 | 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":26588,"numValue":1.29,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26589,"numValue":1.34,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26590,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,419 | train | mutant | 1,754 | 48 | 1,967 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74A | I74A | 1 | 1 | 0 | 0 | 74 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,330 | ProTherm | 3.08 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56A | 60.2 | null | null | null | 98.8 | 1.44 | 102.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":3.08,"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:I56A","type":"_P... | [{"datasets":[],"id":12249,"numValue":60.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12250,"numValue":98.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12251,"numValue":1.44,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12252,"numValue":102.2,"references":[... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3420 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,420 | train | mutant | 1,754 | 48 | 1,967 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74A | I74A | 1 | 1 | 0 | 0 | 74 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,331 | ProTherm | 2.96 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56A | 58.5 | null | null | null | 96.9 | 1.6 | 102.2 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.96,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56A","type":"_P... | [{"datasets":[],"id":12254,"numValue":58.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12255,"numValue":96.9,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12256,"numValue":1.6,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12257,"numValue":102.2,"references":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,421 | train | mutant | 1,754 | 48 | 1,967 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74A | I74A | 1 | 1 | 0 | 0 | 74 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,332 | ProTherm | 2.81 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56A | 54.2 | null | null | null | 90.7 | 1.46 | 92.1 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.81,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56A","type":"_P... | [{"datasets":[],"id":12259,"numValue":54.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12260,"numValue":90.7,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12261,"numValue":1.46,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12262,"numValue":92.1,"references":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,422 | train | mutant | 1,754 | 48 | 1,967 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74A | I74A | 1 | 1 | 0 | 0 | 74 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,333 | ProTherm | 2.67 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56A | 52.3 | null | null | null | 89 | 1.53 | 91.4 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.67,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56A","type":"_P... | [{"datasets":[],"id":12264,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12265,"numValue":89.0,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12266,"numValue":1.53,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12267,"numValue":91.4,"references":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3423 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,423 | train | mutant | 1,754 | 48 | 1,967 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74A | I74A | 1 | 1 | 0 | 0 | 74 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,334 | ProTherm | 2.5 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56A | 48.2 | null | null | null | 82.8 | 1.22 | 84 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.5,"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:I56A","type":"_PD... | [{"datasets":[],"id":12269,"numValue":48.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12270,"numValue":82.8,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":12271,"numValue":1.22,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":12272,"numValue":84.0,"references":[]... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,426 | train | mutant | 1,754 | 48 | 1,967 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74A | I74A | 1 | 1 | 0 | 0 | 74 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,031 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56A | 64.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56A","type":"_PD... | [{"datasets":[],"id":14921,"numValue":64.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14922,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,427 | train | mutant | 1,754 | 48 | 1,967 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74A | I74A | 1 | 1 | 0 | 0 | 74 | I | A | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 6,904 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | 64.9 | 1LZ1_A:I56A | null | null | null | 3.71 | 105.3 | 1.34 | 110.8 | null | null | null | null | null | null | null | null | null | yes | DH|DCP|DHVH|DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":64.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_C... | [{"datasets":[],"id":24395,"numValue":105.3,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":24396,"numValue":1.34,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":24397,"numValue":110.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":["capriotti_S1615_map.csv","khan_protherm... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,429 | train | mutant | 1,757 | 48 | 1,970 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74G | I74G | 1 | 1 | 0 | 0 | 74 | I | G | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,350 | ProTherm | 2.73 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56G | 62.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 298 | ARTICLE | Contribution of water molecules in the interior of a protein to the conformational stability. | 1,997 | 10.1006/jmbi.1997.1365 | 9398521 | J Mol Biol;274;132-42 | 5 | Takano K|Yamagata Y|Yutani K|Funahashi J|Fujii S | [{"numValue":2.73,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56G","type":"_P... | [{"datasets":[],"id":12349,"numValue":62.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":12350,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:3430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,430 | train | mutant | 1,757 | 48 | 1,970 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74G | I74G | 1 | 1 | 0 | 0 | 74 | I | G | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 4,015 | ProTherm | 2.7 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56G | 62.2 | -2.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.7,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56G","type":"_PD... | [{"datasets":[],"id":14828,"numValue":62.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14829,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14830,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:3431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 3,431 | train | mutant | 2,049 | 48 | 2,288 | 148 | 148 | 5 | Lysozyme C | Homo sapiens | 1 | 5 | Lysozyme C | Homo sapiens | 1 | P61626 | IPR001916|IPR019799|IPR000974|IPR023346 | 3.2.1.17 | I74L | I74L | 1 | 1 | 0 | 0 | 74 | I | L | 8 | CONSERVATION | 1LZ1 | 405 | null | 74 | A | T | true | false | 1.390719 | 12.1675 | 3,975 | ProTherm | 2.48 | DSC | Thermal | glycine | 0.05 M | null | 1LZ1_A:I56L | 61.2 | null | null | null | 103.01 | 1.41 | 113.05 | null | null | null | null | null | null | null | null | null | yes | TM|DH|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 371 | ARTICLE | Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme. | 1,999 | 10.1093/protein/12.10.841 | 10556244 | Protein Eng;12;841-50 | 4 | Takano K|Yamagata Y|Yutani K|Funahashi J | [{"numValue":2.48,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"DSC","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1LZ1_A:I56L","type":"_P... | [{"datasets":[],"id":14628,"numValue":61.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":14629,"numValue":103.01,"references":[],"strValue":null,"type":"DH"},{"datasets":[],"id":14630,"numValue":1.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":14631,"numValue":113.05,"references... | [{"id":7029,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.